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Conserved domains on  [gi|578806453|ref|XP_006713352|]
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semaphorin-3F isoform X3 [Homo sapiens]

Protein Classification

semaphorin-3( domain architecture ID 10336818)

semaphorin-3 is a class III semaphorin that is secreted and contains a Sema domain, an Ig domain, and a short basic domain; may function as an axonal guidance cue and may have a role in the regulation of the cardiovascular, immune, and respiratory systems

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sema super family cl15693
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
17-351 0e+00

The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins and plexins have a Sema domain on their N-termini. Plexins function as receptors for the semaphorins. Evolutionarily, plexins may be the ancestor of semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems, and cancer. Semaphorins can be divided into 7 classes. Vertebrates have members in classes 3-7, whereas classes 1 and 2 are known only in invertebrates. Class 2 and 3 semaphorins are secreted; classes 1 and 4 through 6 are transmembrane proteins; and class 7 is membrane associated via glycosylphosphatidylinositol (GPI) linkage. Plexins are a large family of transmembrane proteins, which are divided into four types (A-D) according to sequence similarity. In vertebrates, type A plexins serve as co-receptors for neuropilins to mediate the signalling of class 3 semaphorins. Plexins serve as direct receptors for several other members of the semaphorin family: class 6 semaphorins signal through type A plexins and class 4 semaphorins through type B plexins. This family also includes the MET and RON receptor tyrosine kinases. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves to recognize and bind receptors.


The actual alignment was detected with superfamily member cd11254:

Pssm-ID: 472829 [Multi-domain]  Cd Length: 470  Bit Score: 719.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  17 LDEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQSPAVY 96
Cdd:cd11254  136 INGELYAGVYIDFMGTDAAIFRTMGKQPAMRTDQYNSRWLNDPAFVHAHLIPDSSEKNDDKLYFFFREKSLEAPQSPAVL 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  97 ARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCV 176
Cdd:cd11254  216 SRIGRVCLNDDGGHCCLVNKWSTFLKARLVCSVPGADGIETHFDELRDVFIQPTQDTKNPVIYAVFSTSGSVFKGSAVCV 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 177 YSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPL 256
Cdd:cd11254  296 YSMADIRMVFNGPFAHKEGPNYQWMPYTGKIPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYNAVYPVHRRPL 375
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 257 VVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDQELEELMLEEVEVFKDPAPVKTMTISSKRQQLY 336
Cdd:cd11254  376 VVRTNVNYRFTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDLETEELTLEEVEVFKVPAPIKTMKISSKRQQLY 455
                        330
                 ....*....|....*
gi 578806453 337 VASAVGVTHLSLHRC 351
Cdd:cd11254  456 VSSAVGVTHLSLHRC 470
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
411-500 1.24e-38

Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed of the immunoglobulin (Ig)-like domain of Sema3 and similar proteins. Semaphorins are classified based on structural features additional to the Sema domain. Sema3 is a Class III semaphorin that is secreted. It is a vertebrate class having a Sema domain, an Ig domain, a short basic domain. They have been shown to be axonal guidance cues and have a part in the regulation of the cardiovascular, immune, and respiratory systems. Sema3A, the prototype member of this class III subfamily, induces growth cone collapse and is an inhibitor of axonal sprouting. In perinatal rat cortex, it acts as a chemoattractant and functions to direct the orientated extension of apical dendrites. It may play a role, prior to the development of apical dendrites, in signaling the radial migration of newborn cortical neurons towards the upper layers. Sema3A selectively inhibits vascular endothelial growth factor receptor (VEGF)-induced angiogenesis and induces microvascular permeability. This group also includes Sema3B, -C, -D, -E, -G.


:

Pssm-ID: 409455  Cd Length: 92  Bit Score: 137.09  E-value: 1.24e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 411 NAVESVQYGVAGSAAFLECQPRSPQATVKWLFQRDPGDRRREIRAEDRFLRTEQGLLLRALQLSDRGLYSCTATENNFKH 490
Cdd:cd05871    1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                         90
                 ....*....|
gi 578806453 491 VVTRVQLHVL 500
Cdd:cd05871   81 TLVKIRLHVI 90
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
350-387 3.14e-07

domain found in Plexins, Semaphorins and Integrins;


:

Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 47.15  E-value: 3.14e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 578806453   350 RCQAYGAaCADCCLARDPYCAWD--GQACSRYTASSKRRS 387
Cdd:smart00423   1 RCSKYTS-CSECLLARDPYCAWCssQGRCTSGERCDSRRQ 39
 
Name Accession Description Interval E-value
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
17-351 0e+00

The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is coexpressed with semaphorin3B. Both Sema3B and Sema3F proteins are candidate tumor suppressors that are down-regulated in highly metastatic tumors. Two receptor families, the neuropilins and plexins, have been implicated in mediating the actions of semaphorins 3B and 3F. Sema3F is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200515 [Multi-domain]  Cd Length: 470  Bit Score: 719.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  17 LDEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQSPAVY 96
Cdd:cd11254  136 INGELYAGVYIDFMGTDAAIFRTMGKQPAMRTDQYNSRWLNDPAFVHAHLIPDSSEKNDDKLYFFFREKSLEAPQSPAVL 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  97 ARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCV 176
Cdd:cd11254  216 SRIGRVCLNDDGGHCCLVNKWSTFLKARLVCSVPGADGIETHFDELRDVFIQPTQDTKNPVIYAVFSTSGSVFKGSAVCV 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 177 YSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPL 256
Cdd:cd11254  296 YSMADIRMVFNGPFAHKEGPNYQWMPYTGKIPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYNAVYPVHRRPL 375
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 257 VVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDQELEELMLEEVEVFKDPAPVKTMTISSKRQQLY 336
Cdd:cd11254  376 VVRTNVNYRFTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDLETEELTLEEVEVFKVPAPIKTMKISSKRQQLY 455
                        330
                 ....*....|....*
gi 578806453 337 VASAVGVTHLSLHRC 351
Cdd:cd11254  456 VSSAVGVTHLSLHRC 470
Sema smart00630
semaphorin domain;
19-324 4.46e-118

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 355.52  E-value: 4.46e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453    19 EELYAGVYIDFMGTDAAIFRTLG----KQTA---MRTDQYNSRWLNDPSFIHAELIpdsaernDDKLYFFFRERSAEA-P 90
Cdd:smart00630  92 GELYVGTVADFSGSDPAIPRSLSvrrlKGTSgvsLRTVLYDSKWLNEPNFVYAFES-------GDFVYFFFRETAVEDdN 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453    91 QSPAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGieTHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFR 170
Cdd:smart00630 165 CGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDP--FYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIP 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453   171 GSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFS-GKMPYPRPGTCPGGTFtpsmkSTKDYPDEVINFMRSHPLMYQAVY 249
Cdd:smart00630 243 GSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSrGKVPYPRPGTCPNKPP-----SSKDLPDETLNFIKSHPLMDEVVQ 317
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578806453   250 PLQRRPLVVRTGAPYRLTTIAVDQVdAADGRYEVLFLGTDRGTVQKVIVLPKDDQeLEELMLEEVEVFKDPAPVK 324
Cdd:smart00630 318 PLTGRPLFVKTDSNYLLTSIAVDRV-ATDGNYTVLFLGTSDGRILKVVLSESSSS-SESVVLEEISVFPDGSPIS 390
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
142-330 1.69e-74

Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and transmembrane proteins, some of which function as repellent signals during axon guidance. Sema domains also occur in the hepatocyte growth factor receptor and Swiss:P51805


Pssm-ID: 460197 [Multi-domain]  Cd Length: 180  Bit Score: 235.24  E-value: 1.69e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  142 LQDVFVQQ--TQDVRNPVIYAVFTSS-GSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGG 218
Cdd:pfam01403   1 LQDVFVLKpgAGDALDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  219 TFtpsmksTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGapYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIV 298
Cdd:pfam01403  81 PL------RLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTG--VRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVL 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 578806453  299 LPKDD-------QeleelmleeveVFKDPAPVKTMTISS 330
Cdd:pfam01403 153 VGSEEshiieeiQ-----------VFPEPQPVLNLLLSS 180
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
411-500 1.24e-38

Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed of the immunoglobulin (Ig)-like domain of Sema3 and similar proteins. Semaphorins are classified based on structural features additional to the Sema domain. Sema3 is a Class III semaphorin that is secreted. It is a vertebrate class having a Sema domain, an Ig domain, a short basic domain. They have been shown to be axonal guidance cues and have a part in the regulation of the cardiovascular, immune, and respiratory systems. Sema3A, the prototype member of this class III subfamily, induces growth cone collapse and is an inhibitor of axonal sprouting. In perinatal rat cortex, it acts as a chemoattractant and functions to direct the orientated extension of apical dendrites. It may play a role, prior to the development of apical dendrites, in signaling the radial migration of newborn cortical neurons towards the upper layers. Sema3A selectively inhibits vascular endothelial growth factor receptor (VEGF)-induced angiogenesis and induces microvascular permeability. This group also includes Sema3B, -C, -D, -E, -G.


Pssm-ID: 409455  Cd Length: 92  Bit Score: 137.09  E-value: 1.24e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 411 NAVESVQYGVAGSAAFLECQPRSPQATVKWLFQRDPGDRRREIRAEDRFLRTEQGLLLRALQLSDRGLYSCTATENNFKH 490
Cdd:cd05871    1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                         90
                 ....*....|
gi 578806453 491 VVTRVQLHVL 500
Cdd:cd05871   81 TLVKIRLHVI 90
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
350-387 3.14e-07

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 47.15  E-value: 3.14e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 578806453   350 RCQAYGAaCADCCLARDPYCAWD--GQACSRYTASSKRRS 387
Cdd:smart00423   1 RCSKYTS-CSECLLARDPYCAWCssQGRCTSGERCDSRRQ 39
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
415-499 5.26e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.50  E-value: 5.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453   415 SVQYGVAGSAAFLECQPRS-PQATVKWLFQRDpgdrrREIRAEDRFLRTEQG----LLLRALQLSDRGLYSCTATeNNFK 489
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGsPPPEVTWYKQGG-----KLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAAT-NSSG 75
                           90
                   ....*....|
gi 578806453   490 HVVTRVQLHV 499
Cdd:smart00410  76 SASSGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
415-484 9.60e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.01  E-value: 9.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806453  415 SVQYGVAGSAAFLECQPR-SPQATVKWLFqrdPGDRRREIRAEDRFLRTEQGLL-LRALQLSDRGLYSCTAT 484
Cdd:pfam13927   9 SSVTVREGETVTLTCEATgSPPPTITWYK---NGEPISSGSTRSRSLSGSNSTLtISNVTRSDAGTYTCVAS 77
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
350-391 1.03e-03

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 37.30  E-value: 1.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 578806453  350 RCQAYGAaCADCCLARDPYCAWD--GQACSRYTASSKRRSRRQD 391
Cdd:pfam01437   1 RCSQYTS-CSSCLAARDPYCGWCssEGRCVRRSACGAPEGNCEE 43
 
Name Accession Description Interval E-value
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
17-351 0e+00

The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is coexpressed with semaphorin3B. Both Sema3B and Sema3F proteins are candidate tumor suppressors that are down-regulated in highly metastatic tumors. Two receptor families, the neuropilins and plexins, have been implicated in mediating the actions of semaphorins 3B and 3F. Sema3F is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200515 [Multi-domain]  Cd Length: 470  Bit Score: 719.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  17 LDEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQSPAVY 96
Cdd:cd11254  136 INGELYAGVYIDFMGTDAAIFRTMGKQPAMRTDQYNSRWLNDPAFVHAHLIPDSSEKNDDKLYFFFREKSLEAPQSPAVL 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  97 ARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCV 176
Cdd:cd11254  216 SRIGRVCLNDDGGHCCLVNKWSTFLKARLVCSVPGADGIETHFDELRDVFIQPTQDTKNPVIYAVFSTSGSVFKGSAVCV 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 177 YSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPL 256
Cdd:cd11254  296 YSMADIRMVFNGPFAHKEGPNYQWMPYTGKIPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYNAVYPVHRRPL 375
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 257 VVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDQELEELMLEEVEVFKDPAPVKTMTISSKRQQLY 336
Cdd:cd11254  376 VVRTNVNYRFTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDLETEELTLEEVEVFKVPAPIKTMKISSKRQQLY 455
                        330
                 ....*....|....*
gi 578806453 337 VASAVGVTHLSLHRC 351
Cdd:cd11254  456 VSSAVGVTHLSLHRC 470
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
18-351 0e+00

The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins (Sema3s) are secreted regulator molecules involved in the development of the nervous system, vasculogenesis, angiogenesis,and tumorigenesis. There are 7 distinct subfamilies named Sema3A to 3G. Sema3s function as repellent signals during axon guidance by repelling neurons away from the source of Sema3s. However, Sema3s that are secreted by tumor cells play an inhibitory role in tumor growth and angiogenesis (specifically Sema3B and Sema3F). Sema3s functions by forming complexes with neuropilins and A-type plexins, where neuropilins serve as the ligand binding moiety and the plexins function as signal transduction component. Sema3s primarily inhibit the cell motility and migration of tumor and endothelial cells by inducing collapse of the actin cytoskeleton via neuropilins and plexins. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200500 [Multi-domain]  Cd Length: 471  Bit Score: 639.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  18 DEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQS-PAVY 96
Cdd:cd11239  137 DGELYSGTAIDFMGRDAAIFRSLGHRHYIRTEQYDSRWLNEPKFVGAYLIPDSDNPDDDKVYFFFREKAVEAEGSgKAIY 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  97 ARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCV 176
Cdd:cd11239  217 SRVGRICKNDVGGQRSLVNKWSTFLKARLVCSVPGPDGIDTYFDELEDVFLLPTRDPKNPLIYGVFTTSSNVFKGSAVCV 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 177 YSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPL 256
Cdd:cd11239  297 YSMADIRAAFNGPFAHKEGPNYQWVEYQGKVPYPRPGTCPSKTYGPLYKSTKDFPDDVISFARSHPLMYNPVYPLHGRPL 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 257 VVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDQELEELMLEEVEVFKDPAPVKTMTISSKRQQLY 336
Cdd:cd11239  377 LIRTNVPYRLTQIAVDRVEAEDGQYDVLFIGTDSGTVLKVVSLPKENWEMEEVILEELQVFKHPSPITSMEISSKRQQLY 456
                        330
                 ....*....|....*
gi 578806453 337 VASAVGVTHLSLHRC 351
Cdd:cd11239  457 VGSAEGVVQLPLHRC 471
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
17-351 1.99e-178

The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted semaphorin expressed in and adjacent to cardiac neural crest cells, and causes impaired migration of neural crest cells to the developing cardiac outflow tract, resulting in the interruption of the aortic arch and persistent truncus arteriosus. It has been proposed that Sema3C acts as a guidance molecule, regulating migration of neural crest cells that express semaphorin receptors such as plexin A2. Sema3C may also participate in tumor progression. The cleavage of Sema3C induced by ADAMTS1 promotes the migration of breast cancer cells. Sema3C is a member of the class 3 semaphorin family of secreted proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200512 [Multi-domain]  Cd Length: 470  Bit Score: 512.51  E-value: 1.99e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  17 LDEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQSP-AV 95
Cdd:cd11251  135 INEELFSGMYIDFMGTDAAIFRSLTKRNAVRTDQHNSKWLSEPIFVDAHLIPDGTDPNDAKLYFFLKERLTDNSGSTkQI 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  96 YARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVC 175
Cdd:cd11251  215 HSMIARVCPNDTGGQRSLVNKWTTFLKARLVCSVMDEDGTETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVC 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 176 VYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRP 255
Cdd:cd11251  295 VYHMSDIQTVFNGPFAHKEGPNHQLIAYQGRIPYPRPGTCPGGAFTPNMQSTKEFPDDVVTFIRNHPLMFNPIYPIGRRP 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 256 LVVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDQELEELMLEEVEVFKDPAPVKTMTISSKRQQL 335
Cdd:cd11251  375 LLVRTGTDYKYTKIAVDRVNAADGRYHVLFLGTDKGTVQKVVVLPTNGSLSGELILEELEVFKNHAPITNMKISSKKQQL 454
                        330
                 ....*....|....*.
gi 578806453 336 YVASAVGVTHLSLHRC 351
Cdd:cd11251  455 YVSSEEGISQVSLHRC 470
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
17-351 7.16e-163

The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been reported to inhibit the growth of certain experimental tumors and to regulate endothelial cell migration and apoptosis in vitro, as well as arteriogenesis in the muscle, skin vessel permeability, and tumor angiogenesis in vivo. The function of Sema3A is mediated through receptors neuropilin-1 (NP1) and plexins, although little is known about the requirement of specific plexins in its receptor complex. It is known however that Plexin-A4 is the receptor for Sema3A in the Toll-like receptor- and sepsis-induced cytokine storm during immune response. Sema3A is a member of the Class 3 semaphorin family of secreted proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200510 [Multi-domain]  Cd Length: 493  Bit Score: 474.10  E-value: 7.16e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  17 LDEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQS-PAV 95
Cdd:cd11249  157 IDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKIYFFFRENAIDGEHTgKAT 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  96 YARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVC 175
Cdd:cd11249  237 HARIGQLCKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYAVFTTSSNIFKGSAVC 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 176 VYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTpSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRP 255
Cdd:cd11249  317 MYSMTDIRRVFLGPYAHRDGPNYQWVPFQGRVPYPRPGTCPSKTFG-GFDSTKDLPDDVITFARSHPAMYNPVFPINNRP 395
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 256 LVVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDD-QELEELMLEEVEVFKDPAPVKTMTISSKRQQ 334
Cdd:cd11249  396 IIIKTDVDYQFTQIVVDRVEAEDGQYDVMFIGTDMGTVLKVVSIPKETwHDLEEVLLEEMTVFREPTAISAMELSTKQQQ 475
                        330
                 ....*....|....*..
gi 578806453 335 LYVASAVGVTHLSLHRC 351
Cdd:cd11249  476 LYIGSAIGVSQLPLHRC 492
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
19-351 1.38e-160

The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is coexpressed with semaphorin 3F and both proteins are candidate tumor suppressors. Both Sema3B and Sema3F show high levels of expression in normal tissues and low-grade tumors but are down-regulated in highly metastatic tumors in the lung, melanoma cells, bladder carcinoma cells and prostate carcinoma. They are upregulated by estrogen and inhibit cell motility and invasiveness through decreased FAK phosphorylation and inhibition of MMP-2 and MMP-9 expression. Two receptor families, the neuropilins (NP) and plexins, have been implicated in mediating the actions of semaphorins 3B and 3F. Sema3B is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200511 [Multi-domain]  Cd Length: 471  Bit Score: 467.08  E-value: 1.38e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  19 EELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQSPAV-YA 97
Cdd:cd11250  138 DELYSGVATDLMGRDFTIFRSLGQRPSLRTEQHDSRWLNEPKFVKVFWIPESENPDDDKIYFFFRETAVEAAGLGKQsYS 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  98 RIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVY 177
Cdd:cd11250  218 RIGQICRNDMGGQRSLVNKWTTFLKARLVCSVPGNEGGDTHFDELRDVFLLQTRDKRNPLIYAVFSTSSSVFQGSAVCVY 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 178 SMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTpSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLV 257
Cdd:cd11250  298 TMNDVRRAFLGPFAHKEGPNYQWVSYQGKVPYPRPGMCPSKTFG-SFESTKDFPDDVIQFARNHPLMFNPVLPLGGRPLF 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 258 VRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDD-QELEELMLEEVEVFKDPAPVKTMTISSKRQQLY 336
Cdd:cd11250  377 LRTGIPYTFTQIAVDRVAAADGHYDVMFIGTDVGSVLKVISVPKGSwPSNEELLLEELHVFKDSSPITSMQISSKRQQLY 456
                        330
                 ....*....|....*
gi 578806453 337 VASAVGVTHLSLHRC 351
Cdd:cd11250  457 VGSRSGVSQLPLHRC 471
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
18-351 2.47e-150

The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted semaphorin expressed during the development of the nervous system. In zebrafish, Sema3D is expressed in the ventral tectum. It guides retinal axons along the dorsoventral axis of the tectum and guides the laterality of retinal ganglion cell (RGC) projections. Both Sema3D knockdown or its ubiquitous overexpression induced aberrant ipsilateral projections. Proper balance of Sema3D is needed at the midline for the progression of RGC axons from the chiasm midline into the contralateral optic tract. Sema3D is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200513 [Multi-domain]  Cd Length: 474  Bit Score: 441.27  E-value: 2.47e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  18 DEELYAGVYIDFMGTDAAIFRTLG---KQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQS-P 93
Cdd:cd11252  137 DEYLYAGTASDFLGKDTTFTRSLGptpDHHYIRTDISEHYWLNGAKFIGTFPIPDTYNPDDDKIYFFFREASQDGSTSdK 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  94 AVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSA 173
Cdd:cd11252  217 SVLSRVGRVCKNDVGGQRSLINKWTTFLKARLVCSIPGPDGADTHFDELQDIFLLPTRDERNPVVYGVFTTTSSIFKGSA 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 174 VCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQR 253
Cdd:cd11252  297 VCVYSMADIRAVFNGPYAHKESPDHRWVQYEGRIPYPRPGTCPSKTYDPLIKSTKDFPDEVISFIKRHPLMYKSVYPLTG 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 254 RPLVVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDQELEELMLEEVEVFKDPAPVKTMTISSKRQ 333
Cdd:cd11252  377 GPVFTRINVDYRLTQIVVDHVAAEDGQYDVMFLGTDIGTVLKVVSITKEKWTMEEVVLEELQIFKHPSPILNMELSLKQQ 456
                        330
                 ....*....|....*...
gi 578806453 334 QLYVASAVGVTHLSLHRC 351
Cdd:cd11252  457 QLYIGSRDGLVQLSLHRC 474
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
7-351 5.41e-148

The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is identified as a primarily endothelial cell- expressed class 3 semaphorin that controls endothelial and smooth muscle cell functions in autocrine and paracrine manners, respectively. It is mainly expressed in the lung and kidney, and a little in the brain. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200516 [Multi-domain]  Cd Length: 474  Bit Score: 435.11  E-value: 5.41e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453   7 VTRRGEHVPGLDE-------------------------ELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQyNSRWLNDPSF 61
Cdd:cd11255  100 VGHRGEHVFSLDPttvesgrgrcphepkrpfastftggELYTGLTADFLGRDSVIFRGFGTRSPLRTET-DQRLLHEPRF 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  62 IHAELIPDSAERNDDKLYFFFRERSAEAPQSP--AVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHF 139
Cdd:cd11255  179 VAAHLIPDNADRDNDKVYFFFTERATETAEDDdgAIHSRVGRLCANDAGGQRVLVNKWSTFIKARLVCSVPGPHGIQTHF 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 140 DELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGG- 218
Cdd:cd11255  259 DQLEDVFLLRTKDGKSPEIYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQWGPYEGKVPYPRPGVCPSKi 338
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 219 TFTPS--MKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKV 296
Cdd:cd11255  339 TAQPGraFRSTKDYPDEVLQFARAHPLMWRPVYPSHRRPVLVKTGLPYRLTQIVVDRVEAEDGYYDVMFIGTDSGSVLKV 418
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578806453 297 IVLPKDDQELEELML-EEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSLHRC 351
Cdd:cd11255  419 IVLQKGNSAAGEEVTlEELQVFKVPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
20-351 3.04e-140

The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted molecule implicated in axonal path finding and inhibition of developmental and postischemic angiogenesis. It is also highly expressed in metastatic cancer cells. Sema3E signaling, through its high affinity functional receptor Plexin D1, drives cancer cell invasiveness and metastatic spreading. Sema3E is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200514 [Multi-domain]  Cd Length: 471  Bit Score: 415.41  E-value: 3.04e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  20 ELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQSP-AVYAR 98
Cdd:cd11253  138 ELFVGLYSDYWGRDAAIFRTMNHLAHIRTEHDDERLLKEPKFVGSYMIPDNEDPDDNKVYFFFTEKALEAEGGNhAIYTR 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  99 IGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYS 178
Cdd:cd11253  218 VGRVCANDQGGQRMLVNKWSTFLKTRLICSVPGPNGIDTHFDELEDVFLLRTRDNKNPEIFGLFSTTSNIFKGYAICVYH 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 179 MADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCP----GGTFTpsmkSTKDYPDEVINFMRSHPLMYQAVYPLQRR 254
Cdd:cd11253  298 MASIRAAFNGPFAHKEGPEYHWSVYEGKVPYPRPGSCAskvnGGHYG----TTKDYPDEALRFARSHPLMYQAVKPVHKR 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 255 PLVVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVI-VLPKDDQELEELMLEEVEVFKDPAPVKTMTISSKRQ 333
Cdd:cd11253  374 PILVKTDGKYNLKQIAVDRVEAEDGQYDVLFIGTDNGIVLKVItIYNQETETMEEVILEELQVFKVPVPIISMEISSKRQ 453
                        330
                 ....*....|....*...
gi 578806453 334 QLYVASAVGVTHLSLHRC 351
Cdd:cd11253  454 QLYIGSESGVAQIRFHQC 471
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
18-349 1.28e-118

The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. They can be divided into 7 classes. Vertebrates have members in classes 3-7, whereas classes 1 and 2 are known only in invertebrates. Class 2 and 3 semaphorins are secreted proteins; classes 1 and 4 through 6 are transmembrane proteins; and class 7 is membrane associated via glycosylphosphatidylinositol (GPI) linkage. The semaphorins exert their function through their receptors, the neuropilin and plexin families. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200496 [Multi-domain]  Cd Length: 437  Bit Score: 358.64  E-value: 1.28e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  18 DEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDsaernddKLYFFFRERSAE-APQSPAVY 96
Cdd:cd11235  121 DGELYSGTSADFLGTDPVIYRTLGHNPPLRTEYHDSKWLNEPQFVGAFDIGD-------YVYFFFREIAVEyINCGKAVY 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  97 ARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGieTHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCV 176
Cdd:cd11235  194 SRVARVCKNDQGGSRSLEKKWTTFLKARLNCSVPGEFP--FYFNELQDVFDLPSPSNKEKIFYAVFTTPYNSIPGSAVCA 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 177 YSMADIRMVFNGPFAHKEGPNYQWMPFSG-KMPYPRPGTCPGgtftpsmkSTKDYPDEVINFMRSHPLMYQAVYPLQRRP 255
Cdd:cd11235  272 YSLSDIEAVFNGPFKEQHSSNSAWLPVPDeRVPEPRPGTCVD--------DSSPLPDDTLNFIKSHPLMDEAVTPILNRP 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 256 LVVRTGAPYRLTTIAVDQVDAADGR-YEVLFLGTDRGTVQKVIVLPKDDQeLEELMLEEVEVFKDPAPVKTMTISSKRQQ 334
Cdd:cd11235  344 LFIKTDVNYRFTKIAVDRVQAKLGQtYDVLFVGTDRGIILKVVSLPEQGL-QASNILEEMPVGPPPEPIQTMQLSRKRRS 422
                        330
                 ....*....|....*
gi 578806453 335 LYVASAVGVTHLSLH 349
Cdd:cd11235  423 LYVGSETGVLQVPLA 437
Sema smart00630
semaphorin domain;
19-324 4.46e-118

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 355.52  E-value: 4.46e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453    19 EELYAGVYIDFMGTDAAIFRTLG----KQTA---MRTDQYNSRWLNDPSFIHAELIpdsaernDDKLYFFFRERSAEA-P 90
Cdd:smart00630  92 GELYVGTVADFSGSDPAIPRSLSvrrlKGTSgvsLRTVLYDSKWLNEPNFVYAFES-------GDFVYFFFRETAVEDdN 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453    91 QSPAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGieTHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFR 170
Cdd:smart00630 165 CGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDP--FYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIP 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453   171 GSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFS-GKMPYPRPGTCPGGTFtpsmkSTKDYPDEVINFMRSHPLMYQAVY 249
Cdd:smart00630 243 GSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSrGKVPYPRPGTCPNKPP-----SSKDLPDETLNFIKSHPLMDEVVQ 317
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578806453   250 PLQRRPLVVRTGAPYRLTTIAVDQVdAADGRYEVLFLGTDRGTVQKVIVLPKDDQeLEELMLEEVEVFKDPAPVK 324
Cdd:smart00630 318 PLTGRPLFVKTDSNYLLTSIAVDRV-ATDGNYTVLFLGTSDGRILKVVLSESSSS-SESVVLEEISVFPDGSPIS 390
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
18-348 3.56e-91

The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 semaphorins (Sema4s) are transmembrane regulator molecules involved in the development of the nervous system, immune response, cytoskeletal organization, angiogenesis, and cell-cell interactions. There are 7 distinct subfamilies in class 4 semaphorins, named 4A to 4G. Several class 4 subfamilies play important roles in the immune system and are called "immune semaphorins". Sema4A plays critical roles in T cell-DC interactions in the immune response. Sema4D/CD100, expressed by lymphocytes, promotes the aggregation and survival of B lymphocytes and inhibits cytokine-induced migration of immune cells in vitro. It is required for normal activation of B and T lymphocytes. Sema4B negatively regulates basophil functions through T cell-basophil contacts and significantly inhibits IL-4 and IL-6 production from basophils in response to various stimuli, including IL-3 and papain. Sema4s not only influence the activation state of cells but also modulate their migration and survival. The effects of Sema4s on nonlymphoid cells are mediated by plexin D1 and plexin Bs. The Sema4G and Sema4C genes are expressed in the developing cerebellar cortex and are involved in neural tube closure and development of cerebellar granules cells through receptor plexin B2. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200501 [Multi-domain]  Cd Length: 456  Bit Score: 288.54  E-value: 3.56e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  18 DEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDqYNSRWLNDPSFIHAELIP---DSAERNDDKLYFFFRERSAE-APQSP 93
Cdd:cd11240  131 DGELYSATVNNFLGSEPVISRNHSEGNVLKTE-NTLRWLNEPAFVGSAHIResiDSPDGDDDKIYFFFTETAVEyDFYEK 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  94 AVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEdgiETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSA 173
Cdd:cd11240  210 VTVSRVARVCKGDLGGQRTLQKKWTTFLKAQLVCSQPDS---GLPFNVLRDVFVLSPDSWDATIFYGVFTSQWNVSGLSA 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 174 VCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTC-PGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQ 252
Cdd:cd11240  287 VCAYSLEDIKKVFSGKYKEFNRETSKWSRYTGPVPDPRPGACiTNSARSQGITSSLNLPDNVLTFVKDHPLMDEQVHPIN 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 253 rRPLVVRTGAPYrlTTIAVDQVDAADGR-YEVLFLGTDRGTVQKVIVLPKddqelEELMLEEVEVFKDPAPVKTMTISSK 331
Cdd:cd11240  367 -RPLLVKSGVNY--TRIAVHRVQALDGQtYTVLFLGTEDGFLHKAVSLDG-----GMHIIEEIQLFDQPQPVKNLLLSSS 438
                        330
                 ....*....|....*..
gi 578806453 332 RQQLYVASAVGVTHLSL 348
Cdd:cd11240  439 KGVLYVGSSSGVVQVPL 455
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
18-351 2.02e-82

The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a transmembrane protein. It has been shown to mediate the defasciculation of motor axon bundles at specific choice points. Sema1A binds to its receptor plexin A (PlexA), which in turn triggers downstream signaling events involving the receptor tyrosine kinase Otk, the evolutionarily conserved flavoprotein monooxygenase molecule interacting with CasL (MICAL), and the A kinase anchoring protein Nervy, leading to repulsive growth-cone response. Sema1A has also been shown to be involved in synaptic formation. It is a member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200498 [Multi-domain]  Cd Length: 446  Bit Score: 265.35  E-value: 2.02e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  18 DEELYAGVYIDFMGTDAAIFRTlgkqtAMRTDQYNSRWLNDPSFIHaelipdSAERNDdKLYFFFRERSAEAPQ-SPAVY 96
Cdd:cd11237  124 DGQLYSATVADFSGADPLIYRE-----PLRTERYDLKQLNAPNFVS------SFAYGD-YVYFFFRETAVEYINcGKAIY 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  97 ARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEdgIETHFDELQ---DVFVQQTQDVRNPVIYAVFTSSGSVFRGSA 173
Cdd:cd11237  192 SRVARVCKNDKGGPHPFRDRWTSFLKARLNCSVPGE--YPFYFNEIQstsDIVEGGYGGKSAKLIYGVFTTPVNSISGSA 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 174 VCVYSMADIRMVFNGPFAHKEGPNYQWMPFSG-KMPYPRPGTCpggtftpsMKSTKDYPDEVINFMRSHPLMYQAVYPLQ 252
Cdd:cd11237  270 VCAFSLQDILEVFDGSFKEQQDINSNWLPVPSnKVPEPRPGQC--------VNDSRTLPDVTVNFIKSHPLMDEAVPSFF 341
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 253 RRPLVVRTGAPYRLTTIAVD-QVDAADGR-YEVLFLGTDRGTVQKVIVLPKDDQELEELML--EEVEVFKDPAPVKTMTI 328
Cdd:cd11237  342 GRPILVRTSLQYRFTQIAVDpQVKALDGKyYDVLFIGTDDGKVLKAVNIASADTVDKVSPVviEETQVFPRGVPIRNLLI 421
                        330       340
                 ....*....|....*....|....*
gi 578806453 329 SSKRQQ--LYVASAVGVTHLSLHRC 351
Cdd:cd11237  422 VRGKDDgrLVVVSDDEIVSIPLHRC 446
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
43-348 2.62e-80

The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and Sema4C genes are expressed in the developing cerebellar cortex. Sema4G and Sema4C proteins specifically bind to Plexin B2 expressed in the cerebellar granule cells. Sema4G and Sema4C are involved in neural tube closure and cerebellar granule cell development through Plexin B2.Sema4G belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200523 [Multi-domain]  Cd Length: 457  Bit Score: 260.08  E-value: 2.62e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  43 QTAMRTDQYNSRWLNDPSFIHAELIP---DSAERNDDKLYFFFRERSAEAPQSPAVY--ARIGRICLNDDGGHCCLVNKW 117
Cdd:cd11262  154 QPTLRTEEAPTRWLNDADFVGSVLVResmNSSVGDDDKIYFFFTERSQEETAYFSQSrvARVARVCKGDRGGKKTLQRKW 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 118 STFLKARLVCSVPGedgIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPN 197
Cdd:cd11262  234 TSFLKARLVCYIPE---YEFLFNVLRSVFVLWGSTPQDTVFYGIFGLEWKNVKASAICRYSLSDIQTAFEGPYMEYQDSS 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 198 YQWMPFSGKMPYPRPGTCPGGTF-TPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYrlTTIAVDQVDA 276
Cdd:cd11262  311 SKWSRYTGKVPEPRPGSCITDEHrSQGINSSQDLPDNVLDFVRRHPLMAEQVLPVEGRPLLFKRNVIY--TKIAVQTVRG 388
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806453 277 ADGR-YEVLFLGTDRGTVQKVIVLpkddqELEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSL 348
Cdd:cd11262  389 LDGRvYDVLFLGTDEGWLHKAVVI-----GSAVHIIEELQVFREPQPVENLVISKKQNSLYVGARSGVVQVPL 456
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
142-330 1.69e-74

Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and transmembrane proteins, some of which function as repellent signals during axon guidance. Sema domains also occur in the hepatocyte growth factor receptor and Swiss:P51805


Pssm-ID: 460197 [Multi-domain]  Cd Length: 180  Bit Score: 235.24  E-value: 1.69e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  142 LQDVFVQQ--TQDVRNPVIYAVFTSS-GSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGG 218
Cdd:pfam01403   1 LQDVFVLKpgAGDALDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  219 TFtpsmksTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGapYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIV 298
Cdd:pfam01403  81 PL------RLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTG--VRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVL 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 578806453  299 LPKDD-------QeleelmleeveVFKDPAPVKTMTISS 330
Cdd:pfam01403 153 VGSEEshiieeiQ-----------VFPEPQPVLNLLLSS 180
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
18-300 2.30e-72

The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 semaphorins (Sema6s) are membrane associated semaphorins. There are 6 subfamilies named 6A to 6D. Sema6s bind to plexin As in a neuropilin independent fashion. Sema6-plexin A signaling plays important roles in lamina-specific axon projections. Interactions between plexin A2, plexin A4, and Sema6A control lamina-restricted projection of hippocampal mossy fibers. Interactions between Sema6C, Sema6D and plexin A1 shape the stereotypic trajectories of sensory axons in the spinal cord. In addition to axon targeting, Sema6D-plexin A1 interactions influence a wide range of other biological processes. During cardiac development, Sema6D attracts or repels endothelial cells in the cardiac tube depending on the expression patterns of specific coreceptors in addition to plexin A1. Furthermore, Sema6D binds a receptor complex comprising of plexin A1, Trem2 (triggering receptor expressed on myeloid cells 2), and DAP12 on dendritic cells and osteoclasts to mediate T-cell-DC interactions and to control bone development, respectively. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200503 [Multi-domain]  Cd Length: 465  Bit Score: 239.34  E-value: 2.30e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  18 DEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAElipdsaeRNDDKLYFFFRERSAE-APQSPAVY 96
Cdd:cd11242  132 DGKLYSATVTDFLASDAVIYRSLGDSPTLRTVKYDSKWLKEPHFVHAV-------EYGDYVYFFFREIAVEyNTLGKVVF 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  97 ARIGRICLNDDGGHCCLVNK-WSTFLKARLVCSVPGEDGIetHFDELQDVfvqqTQDVR---NPVIYAVFTSSGSVFRGS 172
Cdd:cd11242  205 SRVARVCKNDMGGSPRVLEKqWTSFLKARLNCSVPGDSHF--YFDVLQAV----TDVIRingRPVVLGVFTTQYNSIPGS 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 173 AVCVYSMADIRMVFNGPFAHKEGPNYQWMPFS-GKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPL 251
Cdd:cd11242  279 AVCAFDMDDIEKVFEGRFKEQKSPDSAWTPVPeDRVPKPRPGCCAGSGSAEKYKTSNDFPDDTLNFIKTHPLMDEAVPSI 358
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 578806453 252 QRRPLVVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLP 300
Cdd:cd11242  359 INRPWFTRTMVRYRLTQIAVDNAAGPYQNYTVVFLGSEAGTVLKFLARI 407
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
18-297 3.12e-69

The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed predominantly in the nervous system during embryogenesis and it uses Plexin-A1 as a receptor. It displays repellent activity for dorsal root ganglion axons. Sema6D also acts as a regulator of late phase primary immune responses. In addition, Sema6D is overexpressed in gastric carcinoma, indicating that it may have an important role in the occurrence and development of the cancer. Sema6D is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200530 [Multi-domain]  Cd Length: 465  Bit Score: 231.07  E-value: 3.12e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  18 DEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAElipdsaeRNDDKLYFFFRERSAEAPQ-SPAVY 96
Cdd:cd11269  132 DGKLYSATVADFLASDAVIYRSMGDGSALRTIKYDSKWIKEPHFLHAI-------EYGNYVYFFFREIAVEHNNlGKAVY 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  97 ARIGRICLNDDGGHCCLVNK-WSTFLKARLVCSVPGEDGIetHFDELQDVfvQQTQDVRN-PVIYAVFTSSGSVFRGSAV 174
Cdd:cd11269  205 SRVARICKNDMGGSQRVLEKhWTSFLKARLNCSVPGDSFF--YFDVLQSI--TDIIEINGiPTVVGVFTTQLNSIPGSAV 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 175 CVYSMADIRMVFNGPFAHKEGPNYQWMPF-SGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQR 253
Cdd:cd11269  281 CAFSMDDIEKVFKGRFKEQKTPDSVWTAVpEDKVPKPRPGCCAKHGLAEAYKTSIDFPDETLSFIKSHPLMDSAVPSIIE 360
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 578806453 254 RPLVVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVI 297
Cdd:cd11269  361 EPWFTKTRVRYRLTAIAVDHAAGPHQNYTVIFVGSEAGVVLKIL 404
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
18-348 4.48e-68

The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed in the epithelial cells that line the pharyngeal arches in zebrafish. It may act as a guidance molecule to restrict the branchiomotor axons to the mesenchymal cells. Gain-of-function and loss-of-function studies demonstrate that Sema4E is essential for the guidance of facial axons from the hindbrain into their pharyngeal arch targets and is sufficient for guidance of gill motor axons. Sema4E guides facial motor axons by a repulsive action. Sema4E belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200521 [Multi-domain]  Cd Length: 456  Bit Score: 227.87  E-value: 4.48e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  18 DEELYAGVYIDFMGTDAAIFRTlgKQTAMRTdQYNSRWLNDPSFIHAELIP---DSAERNDDKLYFFFRERSAEAP-QSP 93
Cdd:cd11260  131 DQDLYSATSMNFLGSEPVIMRS--SPITIRT-EFKSSWLNEPNFIYMAAVPeseDSPEGDDDKIYLFFSETAVEYDfYNK 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  94 AVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPgedgiETHFDEL-QDVFVQQTQDVRNPVIYAVFTSSGSVFRGS 172
Cdd:cd11260  208 LVVSRVARVCKGDLGGQRTLQKKWTSFLKARLDCSVP-----EPSLPYViQDVFHVCHQDWRKCVFYAVFTSQSDSSQSS 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 173 AVCVYSMADIRMVFN-----GPFAhKEGPNYQWMPFSGKMPYPRPGTC-PGGTFTPSMKSTKDYPDEVINFMRSHPLMYQ 246
Cdd:cd11260  283 AVCAYNVTDISNVFSrgkfkTPVA-VETSFVKWVMYSGELPVPRPGACiNNAARTSGIKKSLNLPDKTLQFVKDKPLMDQ 361
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 247 AVYPLQRRPLVVRTGAPyrLTTIAVDQVDAADG-RYEVLFLGTDRGTVQKVIvlpkdDQELEELMLEEVEVFKDPAPVKT 325
Cdd:cd11260  362 AVHPITGKPLLVKRGAL--FTRIVVDMVTAADGqSYPVMFIGTANGYVLKAV-----NYDGEMHIIEEVQLFEPEEPIDI 434
                        330       340
                 ....*....|....*....|...
gi 578806453 326 MTISSKrqQLYVASAVGVTHLSL 348
Cdd:cd11260  435 LRLSQN--QLYAGSASGVVQMPV 455
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
17-343 6.48e-68

The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); Sema4D/CD100 is expressed in immune cells and plays critical roles in immune response; it is thus termed an "immune semaphorin". It is expressed by lymphocytes and promotes the aggregation and survival of B lymphocytes and inhibits cytokine-induced migration of immune cells in vitro. Sema4D/CD100 knock-out mice demonstrate that Sema4D is required for normal activation of B and T lymphocytes. Sema4D increases B-cell and DC function using either Plexin B1 or CD72 as receptors. The function of Sema4D in immune response implicates its role in infectious and noninfectious diseases. Sema4D belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200520 [Multi-domain]  Cd Length: 471  Bit Score: 227.82  E-value: 6.48e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  17 LDEELYAGVYIDFMGTDAAIFRTLgKQTAMRTdQYNSRWLNDPSFIHAELI---PDSAERNDDKLYFFFRERSAEAP-QS 92
Cdd:cd11259  139 VDGELYSGTSYNFLGSEPIISRNS-SQSPLRT-EYAIPWLNEPSFVFADVIradPDSPDGEDDKIYFFFTEVSVEYEfVG 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  93 PAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIethFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGS 172
Cdd:cd11259  217 KLLIPRIARVCKGDQGGLRTLQKKWTSFLKARLICSIPDKNLV---FNVVNDVFILKSPTLKEPVIYGVFTPQLNNVGLS 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 173 AVCVYSMADIRMVFN-GPFAHK---EGPNYQWMPFSGKMPYPRPGTCPGGTFTPS-MKSTKDYPDEVINFMRSHPLMYQA 247
Cdd:cd11259  294 AVCAYNLSTVEEVFSkGKYMQSatvEQSHTKWVRYNGEVPKPRPGACINNEARAAnYTSSLNLPDKTLQFVKDHPLMDDS 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 248 VYPLQRRPLVVRTGAPYrlTTIAVDQVDAADGR-YEVLFLGTDRGTVQKVIVLPKDdqeleELMLEEVEVFKDPAPVKTM 326
Cdd:cd11259  374 VTPIGNRPRLIKKDVNY--TQIVVDRVQALDGTiYDVMFISTDRGALHKAISLENE-----VHIIEETQLFPDFEPVQTL 446
                        330
                 ....*....|....*....
gi 578806453 327 TISSK--RQQLYVASAVGV 343
Cdd:cd11259  447 LLSSKkgRRFLYAGSNSGV 465
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
18-298 1.72e-64

The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, Sema6A-plexin A2 signaling modulates granule cell migration by controlling centrosome positioning. Besides plexin A2, plexin A4 is also found to be a receptor of Sema6A. Interactions between plexin A2, plexin A4, and Sema6A control lamina-restricted projection of hippocampal mossy fibers. It is required for the clustering of boundary cap cells at the PNS/CNS interface and thus, prevents motoneurons from streaming out of the ventral spinal cord. At the dorsal root entry site, it organizes the segregation of dorsal roots. Sema6A may also be involved in axonal pathfinding processes in the periinfarct and homotopic contralateral cortex. Sema6A is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200527 [Multi-domain]  Cd Length: 466  Bit Score: 218.75  E-value: 1.72e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  18 DEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAElipdsaeRNDDKLYFFFRERSAE-APQSPAVY 96
Cdd:cd11266  132 DGKLYSATVTDFLAIDAVIYRSLGDSPTLRTVKHDSKWLKEPYFVQAV-------DYGDYIYFFFREIAVEyNSMGKVVF 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  97 ARIGRICLNDDGGHCCLVNK-WSTFLKARLVCSVPGEDGIetHFDELQDVFVQQTQDVRNpVIYAVFTSSGSVFRGSAVC 175
Cdd:cd11266  205 PRVAQVCKNDMGGSQRVLEKqWTSFLKARLNCSVPGDSHF--YFNILQAVTDVIHINGRD-VVLATFSTPYNSIPGSAVC 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 176 VYSMADIRMVFNGPFAHKEGPNYQWMPFSG-KMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRR 254
Cdd:cd11266  282 AYDMLDIASVFTGRFKEQKSPDSTWTPVPDeRVPKPRPGCCAGSSSLEKYATSNEFPDDTLNFIKTHPLMDEAVPSIINR 361
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 578806453 255 PLVVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIV 298
Cdd:cd11266  362 PWFLRTMVRYRLTKIAVDNAAGPYQNHTVVFLGSEKGIILKFLA 405
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
18-348 1.54e-63

The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. There are three subfamilies in class 5 semaphorins, namely 5A, 5B and 5C. Sema5A and Sema5B function as guidance cues for optic and corticofugal nerve development, respectively. Sema5A-induced cell migration requires Met signaling. Sema5C is an early development gene and may play a role in odor-guided behavior. Sema5A is also implicated in cancer. In a screening model for metastasis, the Drosophila Sema5A ortholog, Dsema-5C, has been found to be required in tumorigenicity and metastasis. Sema5A is highly expressed in human pancreatic cancer cells and is associated with tumor growth, invasion and metastasis. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200502 [Multi-domain]  Cd Length: 438  Bit Score: 215.50  E-value: 1.54e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  18 DEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIhaelipdSAERNDDKLYFFFRERSAEAPQS-PAVY 96
Cdd:cd11241  127 SGELYAGTVYDFSGRDPAIYRSLGGKPPLRTAQYNSKWLNEPNFV-------GSYEIGNHTYFFFRENAVEHQDCgKTVY 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  97 ARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEdgIETHFDELQDVFVQQTQDvrnpVIYAVFTSSGSVFRGSAVCV 176
Cdd:cd11241  200 SRIARVCKNDIGGRFLLEDTWTTFMKARLNCSLPGE--FPFYYNEIQGTFYLPETD----LIYAVFTTNVNGIAGSAICA 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 177 YSMADIRMVFNGPFAHKEGPNYQWMPFsgkmPYPRPGTCPGGTFTPSMKSTKDyPDEVINFMRsHPLMYQAVYPLQRRPL 256
Cdd:cd11241  274 FNLSAINQAFNGPFKYQENNGSAWLPT----PNPHPNFQCTTSIDRGQPANTT-ERDLQDAQK-YQLMAEVVQPVTKIPL 347
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 257 VVRTGApyRLTTIAVDQVDAADGR-YEVLFLGTDRGTVQKVIVLPKdDQELEELMLEEVEVFKDPAPVKTMTISSKRQQL 335
Cdd:cd11241  348 VTMDDV--RFSKLAVDVVQGRGTQlVHIFYVGTDYGTILKMYQPHR-SQKSCTLEEIKILPAMKGEPITSLQFLKSEKSL 424
                        330
                 ....*....|...
gi 578806453 336 YVASAVGVTHLSL 348
Cdd:cd11241  425 FVGLETGVLRIPL 437
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
18-303 1.36e-62

The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as repellents for axon growth; this repulsive activity is mediated by its receptor Plexin A4. Sema6B is expressed in CA3, and repels mossy fibers in a Plexin A4 dependent manner. In human, it was shown that peroxisome proliferator-activated receptors (PPARs) and 9-cis-retinoic acid receptor (RXR) regulate human semaphorin 6B (Sema6B) gene expression. Sema6B is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200528 [Multi-domain]  Cd Length: 466  Bit Score: 213.54  E-value: 1.36e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  18 DEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHA-ELIPdsaernddKLYFFFRERSAEAPQ-SPAV 95
Cdd:cd11267  132 DGMLFTATVTDFLAIDAVIYRSLGDSPALRTVKHDSKWFKEPYFVHAvEWGS--------HVYFFFREIAMEFNYlEKVV 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  96 YARIGRICLNDDGGHCCLVNK-WSTFLKARLVCSVPGEdgieTHFdelqdVF--VQQTQDVRN----PVIYAVFTSSGSV 168
Cdd:cd11267  204 VSRVARVCKNDMGGSQRVLEKqWTSFLKARLNCSVPGD----SHF-----YFnvLQAVSDILNlggrPVVLAVFSTPTNS 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 169 FRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKM-PYPRPGTCPGgtftPSMK--STKDYPDEVINFMRSHPLMY 245
Cdd:cd11267  275 IPGSAVCAFDMTQVAAVFEGRFREQKSPESIWTPVPEELvPRPRPGCCAA----PGMRynSSSTLPDEVLNFVKTHPLMD 350
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578806453 246 QAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDD 303
Cdd:cd11267  351 EAVPSLGHAPWIVRTMTRYQLTHMVVDTEAGPHGNHTVVFLGSTRGTVLKFLIIPNAS 408
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
18-348 7.22e-61

The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in T and B cells, is an immune semaphorin. It functions as a negative regulatory of basophils through T cell-basophil contacts and it significantly inhibits IL-4 and IL-6 production from basophils in response to various stimuli, including IL-3 and papain. In addition, T cell-derived Sema4B suppresses basophil-mediated Th2 skewing and humoral memory responses. Sema4B may be also involved in lung cancer cell mobility by inducing the degradation of CLCP1 (CUB, LCCL-homology, coagulation factor V/VIII homology domains protein). Sema4B is characterized by a PDZ-binding motif at the carboxy-terminus, which mediates interaction with the post-synaptic density protein PSD-95/SAP90, which is thought to play a central role during synaptogenesis and in the structure and function of post-synaptic specializations of excitatory synapses. Sema4B belongs to class 4 transmembrane semaphorin family proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200518 [Multi-domain]  Cd Length: 464  Bit Score: 208.95  E-value: 7.22e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  18 DEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDqyNS-RWLNDPSFIHAELIPDS---AERNDDKLYFFFRERSAEAPQ-S 92
Cdd:cd11257  138 DGELYTGTVSNFQGNDPIIYRSLGSGTPLKTE--NSlNWLQDPAFVGSAYIQESlpkLVGDDDKIYFFFSETGKEFDFfE 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  93 PAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGeDGIEthFDELQDVFV--QQTQDVRNPVIYAVFTS--SGSV 168
Cdd:cd11257  216 NTIVSRIARVCKGDEGGERVLQKRWTTFLKAQLLCSLPD-DGFP--FNVLQDVFVltPSPEDWKDTLFYGVFTSqwHKGT 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 169 FRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTP-SMKSTKDYPDEVINFMRSHPLMYQA 247
Cdd:cd11257  293 AGSSAVCVFTMDQVQRAFNGLYKEVNRETQQWYTYTHPVPEPRPGACITNSARErKINSSLHMPDRVLNFVKDHFLMDGQ 372
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 248 VyplQRRPLVVRTGAPYrlTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKddqelEELMLEEVEVFKDPAPVKTMT 327
Cdd:cd11257  373 V---RSQPLLLQPQVRY--TQIAVHRVKGLHKTYDVLFLGTDDGRLHKAVSVGP-----MVHIIEELQIFSEGQPVQNLL 442
                        330       340
                 ....*....|....*....|.
gi 578806453 328 ISSKRQQLYVASAVGVTHLSL 348
Cdd:cd11257  443 LDTHKGLLYASSHSGVVQVPV 463
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
18-297 4.20e-60

The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed predominantly in the nervous system during embryogenesis. It binds Plexin A1 and might utilize it as a receptor to repel axons of specific types during development. Sema6E acts as a repellent to dorsal root ganglion axons as well as sympathetic axons. Sema6E is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200531 [Multi-domain]  Cd Length: 462  Bit Score: 206.88  E-value: 4.20e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  18 DEELYAGVYIDFMGTDAAIFRTLGKQT-AMRTDQYNSRWLNDPSFIHAElipdsaeRNDDKLYFFFRERSAEAPQSPAV- 95
Cdd:cd11270  129 GGDFYSATMTDFLASDAVIYRSLGESSpVLRTVKYDSKWLREPHFLHAI-------EYGNYVYFFLSEIAVEYTTLGKVv 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  96 YARIGRICLNDDGGHCCLVNK-WSTFLKARLVCSVPGEDGIetHFDELQDVFVQQTQDVRnPVIYAVFTSSGSVFRGSAV 174
Cdd:cd11270  202 FSRVARVCKNDNGGSPRVLERyWTSFLKARLNCSVPGDSFF--YFDVLQSLTNVMQINHR-PAVLGVFTTQANSITGSAV 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 175 CVYSMADIRMVFNGPFAHKEGPNYQWMPF-SGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQR 253
Cdd:cd11270  279 CAFYMDDIEKVFNGKFKEQRNSESAWTPVpDEAVPKPRPGSCAGDGPAAGYKSSTNFPDETLTFIKSYPLMDEAVPSVNN 358
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 578806453 254 RPLVVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVI 297
Cdd:cd11270  359 RPCFTRTTSRFKLTQIAVDTAAGPYKNYTVVFLGSENGHVLKVL 402
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
3-297 2.76e-59

The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed in regions of the basal telencephalon in rat. Sema5B is an inhibitory cue for corticofugal axons and acts as a source of repulsion for the appropriate guidance of cortical axons away from structures such as the ventricular zone as they navigate toward and within subcortical regions. In addition to its role as a guidance cue, Sema5B regulates the development and maintenance of synapse size and number in hippocampal neurons. In addition, the sema domain of Sema5B can be cleaved of the whole protein and exerts its function in regulation of synapse morphology. Sema5B belongs to the class 5 semaphorin family of proteins, which are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200525 [Multi-domain]  Cd Length: 437  Bit Score: 204.06  E-value: 2.76e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453   3 SSGPVTRRGEhvpgldeeLYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAernddklYFFF 82
Cdd:cd11264  120 STAVITSRGE--------LYAATVIDFSGRDPAIYRSLGSVPPLRTAQYNSKWLNEPNFIAAYDIGLFT-------YFFF 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  83 RERSAEAPQSPAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEdgIETHFDELQDVFVQQTQDvrnpVIYAVF 162
Cdd:cd11264  185 RENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGE--IPFYYNELQSTFYLPEQD----LIYGVF 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 163 TSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPggtftpsmkstKDYPDE-----VINF 237
Cdd:cd11264  259 TTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLS-----------DDSPNEnlterSLQD 327
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 238 MRSHPLMYQAVYPLQRRPLVvrTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVI 297
Cdd:cd11264  328 AQRLFLMNDVVQPVTVDPLV--TQDSVRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKAL 385
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
21-348 8.31e-59

The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted semaphorin, signals through its receptor plexin B (PlexB) to regulate central and peripheral axon pathfinding. In the Drosophila embryo, Sema2A secreted by oenocytes interacts with PlexB to guide sensory axons. Sema2A is a member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200499 [Multi-domain]  Cd Length: 452  Bit Score: 203.04  E-value: 8.31e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  21 LYAGVYIDFMGTDAAIFRT----LGKQ---TAMRTDQYNSRWLNDPSFIHAELIpdsaernDDKLYFFFRERSAEAPQ-S 92
Cdd:cd11238  140 LYSGTRTEFTKANTVIYRPplynNTKGrheSFMRTLKYDSKWLDEPNFVGSFDI-------GDYVYFFFRETAVEYINcG 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  93 PAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEdgIETHFDELQDVF-VQQTQDVRnpvIYAVFTSSGSVFRG 171
Cdd:cd11238  213 KVVYSRVARVCKKDTGGKNVLRQNWTTFLKARLNCSISGE--FPFYFNEIQSVYkVPGRDDTL---FYATFTTSENGFTG 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 172 SAVCVYSMADIRMVFN-GPFAHKEGPNYQWMPF-SGKMPYPRPGTCPGgtftpsmkSTKDYPDEVINFMRSHPLMYQAVY 249
Cdd:cd11238  288 SAVCVFTLSDINAAFDtGKFKEQASSSSAWLPVlSSEVPEPRPGTCVN--------DSATLSDTVLHFARTHPLMDDAVS 359
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 250 plQRRPLVVRtgAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKvIVLPKDDQeLEELMLEEVEVFKDPAPVKTMTIs 329
Cdd:cd11238  360 --HGPPLLYL--RDVVFTHLVVDKLRIDDQEYVVFYAGSNDGKVYK-IVHWKDAG-ESKSNLLDVFELTPGEPIRAMEL- 432
                        330
                 ....*....|....*....
gi 578806453 330 SKRQQLYVASAVGVTHLSL 348
Cdd:cd11238  433 LPGEFLYVASDHRVSQIDL 451
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
17-348 1.45e-58

The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed in immune cells and is thus termed an "immune semaphorin". It plays critical roles in T cell-DC interactions in the immune response. It has been reported to enhance activation and differentiation of T cells in vitro and generation of antigen-specific T cells in vivo. The function of Sema4A in the immune response implicates its role in infectious and noninfectious diseases. Sema4A exerts its function through three receptors, namely Plexin B, Plexin D1, and Tim-2. Sema4A belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. TThe Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200517 [Multi-domain]  Cd Length: 447  Bit Score: 202.45  E-value: 1.45e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  17 LDEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNsRWLN-DPSFIHAELIPDsaernDDKLYFFFRERSAEAPQSPAV 95
Cdd:cd11256  136 VDGELYTGTMNNFRGNEPIIFRNLGTKVSLKTDGFL-RWLNaDAVFVASFNPQG-----DSKVYFFFEETAREFDFFEKL 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  96 Y-ARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEdgieTHFDELQDVFVQQTQDVRNPVIYAVFTSSGSV--FRGS 172
Cdd:cd11256  210 TvARVARVCKNDVGGEKLLQKKWTTFLKAQLTCSQQGH----FPFNVIHHVALLNQPDPNNSVFYAVFTSQWQLggRRSS 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 173 AVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTpsmkstkdypDEVINFMRSHPLMYQAVYPLQ 252
Cdd:cd11256  286 AVCAYKLNDIEKVFNGKYKELNKESSRWTRYMGPVSDPRPGSCSGGKSS----------DKALNFMKDHFLMDEVVLPGA 355
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 253 RRPLVVRTGAPYrlTTIAVDQVDAADGR-YEVLFLGTDRGTVQKVIVLPKDDqeleELMLEEVEVFKDPAPVKTMTISSK 331
Cdd:cd11256  356 GRPLLVKSNVQY--TRIAVDSVQGVSGHnYTVMFLGTDKGFLHKAVLMGGSE----SHIIEEIELLTPPEPVENLLLAAN 429
                        330
                 ....*....|....*..
gi 578806453 332 RQQLYVASAVGVTHLSL 348
Cdd:cd11256  430 EGVVYIGYSAGVWRVPL 446
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
17-348 2.28e-57

The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a Plexin B2 ligand to regulate the development of cerebellar granule cells and to modulate ureteric branching in the developing kidney. The binding of Sema4C to Plexin B2 results the phosphorylation of downstream regulator ErbB-2 and the plexin protein itself. The cytoplasmic region of Sema4C binds a neurite-outgrowth-related protein SFAP75, suggesting that Sema4C may also play a role in neural function. Sema4C belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200519 [Multi-domain]  Cd Length: 458  Bit Score: 199.26  E-value: 2.28e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  17 LDEELYAGVYIDFMGTDAAIFRTLGKQTAMRTdQYNSRWLNDPSFIHAELIPDSAER---NDDKLYFFFRERSAEAP-QS 92
Cdd:cd11258  131 VDGELYSATLNNFLGTEPVILRNLGQHYSMKT-EYLAFWLNEPHFVGSAFVPESVGSftgDDDKIYFFFSERAVEYDcDS 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  93 PAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPgedGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGS 172
Cdd:cd11258  210 EQVVARVARVCKGDLGGARTLQKKWTTFLKARLLCSIP---EWQLYFNQLKAVFTLEGASWRNTTFFAVFQARWGDMDVS 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 173 AVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTC-PGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPL 251
Cdd:cd11258  287 AVCEYQLGEIQQVFEGPYKEYSEQAQKWGRYTDPVPSPRPGSCiNNWHRDHGYTSSLELPDNTLNFVKKHPLMEDRVKPR 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 252 QRRPLVVRTGApyRLTTIAVDQVDAADGR-YEVLFLGTDRGTVQKVIVLpkddqELEELMLEEVEVFKDPAPVKTMTISS 330
Cdd:cd11258  367 LGRPLLVPCNS--NFTHVVWTRVLGLDGEtYSVLFIGTLDGWLIKAVSL-----GSWVHMIEELQVFDQEPPESLVVSQS 439
                        330
                 ....*....|....*...
gi 578806453 331 KRQQLYVASAVGVTHLSL 348
Cdd:cd11258  440 SKKLLFAGSRSELLQLPW 457
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
36-348 1.60e-56

The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); Sema7A plays regulatory roles in both immune and nervous systems. Unlike other semaphorins, which act as repulsive guidance cues, Sema7A enhances central and peripheral axon growth and is required for proper axon tract formation during embryonic development. Sema7A also plays a critical role in the negative regulation of T cell activation and function. Sema7A is a membrane-anchored member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200504 [Multi-domain]  Cd Length: 414  Bit Score: 195.83  E-value: 1.60e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  36 IFRTLGKQTAMRTDqynSRWLNDPSFIHAELIPdSAERNDDKLYFFFRERSAEA-PQSPAVYARIGRICLNDDGGHCCL- 113
Cdd:cd11243  131 RFRRYGGKKELYTS---DTVMQKPQFVKATLLP-EDEQYQDKIYYFFREDNEDKgPEAEPNISRVARLCKEDQGGTSSLs 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 114 VNKWSTFLKARLVCSVPGEDGietHFDELQDVFVQQTQDVRNPVIYAVFTSSgsvFRGSAVCVYSMADIRMVFNgpfahk 193
Cdd:cd11243  207 TSKWSTFLKARLVCGDPATPM---NFNRLQDVFLLPKEEWREAVVYGVFSNT---WGSSAVCSYSLGDIDKVFR------ 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 194 egpNYQWMPFSGKMPYPRPGTC-PGGTFTPSmkstkdypdEVINFMRSHPLMYQAVYPLQRRPLVVRTGApYRLTTIAVD 272
Cdd:cd11243  275 ---TSSLKGYSGSLPNPRPGTCvPPEQTHPS---------ETFSFADEHPELDDRIEPDEPRKLPVFQNK-DHYQKVVVD 341
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578806453 273 QVDAADGR-YEVLFLGTDRGTVQKVIVLPKDDqeleeLMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSL 348
Cdd:cd11243  342 EVRASDGVsYDVLYLATDKGKIHKVVESKGQT-----HNIMEIQPFKEQEPIQSMILDAERSHLYVGTKAEVTRLPL 413
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
20-337 2.58e-56

The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse Sema5A was identified as a protein that induces inhibitory responses during optic nerve development. Recent studies show that Sema5A controls innate immunity in mice. It also has been identified as a candidate gene for causing idiopathic autism in humans. Plexin B3 functions as a binding partner and receptor for Sema5A. Furthermore, Sema5A is also implicated in cancer. The role of the Drosophila Sema5A ortholog, Dsema-5C, in tumorigenicity and metastasis has been reported. Sema5A is highly expressed in human pancreatic cancer cells and is associated with tumor growth, invasion and metastasis. Sema5A belongs to class 5 semaphorin family of proteins, which are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200524 [Multi-domain]  Cd Length: 436  Bit Score: 196.02  E-value: 2.58e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  20 ELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAernddklYFFFRERSAEAPQSPAVYARI 99
Cdd:cd11263  129 ELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFT-------YFFFRENAVEHDCGKTVFSRA 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 100 GRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEdgIETHFDELQDVFVQQTQDvrnpVIYAVFTSSGSVFRGSAVCVYSM 179
Cdd:cd11263  202 ARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGE--IPFYYNELQSTFFLPELD----LIYGIFTTNVNSIAASAVCVFNL 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 180 ADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFtpsMKSTKDYPDEVINFMrshpLMYQAVYPLQRRPLVVR 259
Cdd:cd11263  276 SAISQAFNGPFKYQENSRSAWLPYPNPNPNFQCGTMDQGLY---VNLTERNLQDAQKFI----LMHEVVQPVTPVPYFME 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 260 TGApyRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKviVLPKDDQELEELMLEEVEVF--KDPAPVKTMTISSKRQQLYV 337
Cdd:cd11263  349 DNS--RFSHVAVDVVQGKDMLFHIIYLATDYGTIKK--VLAPLNQSSSSCLLEEIELFpkRQREPIRSLQILHSQSVLFV 424
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
20-346 1.45e-53

The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, Sema5C was identified as an early development gene, which is expressed in stage 2 embryos with a striped pattern emerging at later stages. Sema5c may play a role in odor-guided behavior and in tumorigenesis. Sema5C belongs to class 5 semaphorin family of proteins, which are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200526 [Multi-domain]  Cd Length: 433  Bit Score: 188.45  E-value: 1.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  20 ELYAGVYIDFMGTDAAIFRTLGKQTA--MRTDQYNSRWLNDPSFIhaelipDSAErNDDKLYFFFRERSAEAPQ-SPAVY 96
Cdd:cd11265  129 QLFVGSPTDFSGSDSAIYRTLGTSNKsfLRTKQYNSKWLNEPQFV------GSFE-TGNFVYFLFRESAVEYMNcGKVIY 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  97 ARIGRICLNDDGGHCCLV-NKWSTFLKARLVCSVPGEdgIETHFDELQDVFVQQTQDVrnpvIYAVFTSSGSVFRGSAVC 175
Cdd:cd11265  202 SRIARVCKNDVGGGTMLLkDNWTTFLKARLNCSLPGE--YPFYFDEIQGMTYLPDEGI----LYATFTTPENSIAGSAVC 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 176 VYSMADIRMVFNGPFAHKEGPNYQWmpfsGKMPYP---RPGTCPGGTFTPSMKSTKdypdevinfmrsHPLMYQAVYPLQ 252
Cdd:cd11265  276 AFNLSSINAAFDGPFKHQESSGAAW----ERVNVNhrdHFNQCSSSSSSHLLESSR------------YQLMDEAVQPIT 339
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 253 RRPLVVRTGApyRLTTIAVDQVDAA-DGRYEVLFLGTDRGTVQKVIVLPKDDQeleELMLEEVEVFKDPA-PVKTMTISS 330
Cdd:cd11265  340 LEPLHHAKLE--RFSHIAVDVIPTKiHQSVHVLYVATTGGLIKKISVLPRTQE---TCLVEIWQPLPTPDsPIKTMQYLK 414
                        330
                 ....*....|....*.
gi 578806453 331 KRQQLYVASAVGVTHL 346
Cdd:cd11265  415 VTDSLYVGTELALMRI 430
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
21-297 8.91e-51

The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called semaphorin Y); Sema6C is highly expressed in adult brain and skeletal muscle and it shows growth cone collapsing activity. It may play a role in the maintenance and remodelling of neuronal connections. In adult skeletal muscle, this role includes prevention of motor neuron sprouting and uncontrolled motor neuron growth. The expression of Sema6C in adult skeletal muscle is down-regulated following denervation. Sema6C is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200529 [Multi-domain]  Cd Length: 465  Bit Score: 181.82  E-value: 8.91e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  21 LYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAElipdsaeRNDDKLYFFFRERSAEAPQSPAV-YARI 99
Cdd:cd11268  134 LYSATAADFQASDAVVYRSLGPQPPLRSAKYDSKWLREPHFVQAL-------EHGDHVYFFFREVSVEDARLGRVqFSRV 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 100 GRICLNDDGGHCCLVNK-WSTFLKARLVCSVPGEDGIetHFDELQDVFVQQTQDVRNpVIYAVFTSSGSVFRGSAVCVYS 178
Cdd:cd11268  207 ARVCKRDMGGSPRALDRhWTSFLKLRLNCSVPGDSTF--YFDVLQALTGPVNLHGRS-ALFGVFTTQTNSIPGSAVCAFY 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 179 MADIRMVFNGPFAHKEGPNYQWMPFS-GKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLV 257
Cdd:cd11268  284 LDEIERGFEGKFKEQRSLDGAWTPVSeDRVPSPRPGSCAGVGGAALFSSSRDLPDDVLTFIKAHPLLDPAVPPVTHQPLL 363
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 578806453 258 VRTGAPYrLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVI 297
Cdd:cd11268  364 TLTSRAL-LTQVAVDGMAGPHSNITVMFLGSNDGTVLKVL 402
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
21-346 4.37e-50

The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in heterotypic cell-cell contacts and controls cell proliferation and suppresses tumorigenesis. In neurofibromatosis type 1 (NF1) patients, reduced Sema4F level disrupts Schwann cell/axonal interactions. Experiments using a yeast two-hybrid system show that the extreme C-terminus of Sema4F interacts with the PDZ domains of post-synaptic density protein SAP90/PSD-95, indicating possible functional involvement of Semas4F at glutamatergic synapses. Recent work also suggests a role for Sema4F in the injury response of intramedullary axotomized motoneuron. Sema4F belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulator molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200522 [Multi-domain]  Cd Length: 460  Bit Score: 179.70  E-value: 4.37e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  21 LYAGVYIDFMGTDAAIFRTLGK-QTAMRTDQYNSrWLNDPSFIHAELIPDSA---ERNDDKLYFFFRERSAEAPQ-SPAV 95
Cdd:cd11261  136 LYAATVKNFLGTEPIISRAVGRaEEWIRTETLPS-WLNAPAFVAAVFLSPAEwgdEDGDDEIYFFFTETAREYDSyERIK 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  96 YARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPgEDGieTHFDELQDVFVQQTQDVRN-PVIYAVFTSSGSVFRGSAV 174
Cdd:cd11261  215 VPRVARVCAGDLGGRKTLQQRWTTFLKADLLCPGP-EHG--RASSILQDVTTLRPLPGAGtPIFYGIFSSQWEGASISAV 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 175 CVYSMADIRMVFNGPFAHKEGPNYQWMPFS-GKMPYPRPGTCpggtFTPSMK-----STKDYPDEVINFMRSHPLMYQAV 248
Cdd:cd11261  292 CAFRPQDIRRVMNGPFREFKHDCNRGLPVMdSDVPQPRPGEC----ITNNMKllgfgSSLSLPDRVLTFVRDHPLMDRPV 367
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 249 YPLQRRPLVVRTGAPYrlTTIAVDQVDAADGR-YEVLFLGTDRGTVQKVIVLpkddqELEELMLEEVEVFKDPAPVKTMT 327
Cdd:cd11261  368 FPADGHPLLVTTDTAY--LRVAAHRVTSLSGKeYDVLYLGTEDGHLHRAVRI-----GAQLSVLEDLALFPEPQPVENLQ 440
                        330
                 ....*....|....*....
gi 578806453 328 IssKRQQLYVASAVGVTHL 346
Cdd:cd11261  441 L--HHNWLLVGSDTEVTQI 457
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
411-500 1.24e-38

Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed of the immunoglobulin (Ig)-like domain of Sema3 and similar proteins. Semaphorins are classified based on structural features additional to the Sema domain. Sema3 is a Class III semaphorin that is secreted. It is a vertebrate class having a Sema domain, an Ig domain, a short basic domain. They have been shown to be axonal guidance cues and have a part in the regulation of the cardiovascular, immune, and respiratory systems. Sema3A, the prototype member of this class III subfamily, induces growth cone collapse and is an inhibitor of axonal sprouting. In perinatal rat cortex, it acts as a chemoattractant and functions to direct the orientated extension of apical dendrites. It may play a role, prior to the development of apical dendrites, in signaling the radial migration of newborn cortical neurons towards the upper layers. Sema3A selectively inhibits vascular endothelial growth factor receptor (VEGF)-induced angiogenesis and induces microvascular permeability. This group also includes Sema3B, -C, -D, -E, -G.


Pssm-ID: 409455  Cd Length: 92  Bit Score: 137.09  E-value: 1.24e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 411 NAVESVQYGVAGSAAFLECQPRSPQATVKWLFQRDPGDRRREIRAEDRFLRTEQGLLLRALQLSDRGLYSCTATENNFKH 490
Cdd:cd05871    1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                         90
                 ....*....|
gi 578806453 491 VVTRVQLHVL 500
Cdd:cd05871   81 TLVKIRLHVI 90
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
18-344 6.07e-33

The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins and plexins have a Sema domain on their N-termini. Plexins function as receptors for the semaphorins. Evolutionarily, plexins may be the ancestor of semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems, and cancer. Semaphorins can be divided into 7 classes. Vertebrates have members in classes 3-7, whereas classes 1 and 2 are known only in invertebrates. Class 2 and 3 semaphorins are secreted; classes 1 and 4 through 6 are transmembrane proteins; and class 7 is membrane associated via glycosylphosphatidylinositol (GPI) linkage. Plexins are a large family of transmembrane proteins, which are divided into four types (A-D) according to sequence similarity. In vertebrates, type A plexins serve as co-receptors for neuropilins to mediate the signalling of class 3 semaphorins. Plexins serve as direct receptors for several other members of the semaphorin family: class 6 semaphorins signal through type A plexins and class 4 semaphorins through type B plexins. This family also includes the MET and RON receptor tyrosine kinases. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves to recognize and bind receptors.


Pssm-ID: 200495 [Multi-domain]  Cd Length: 392  Bit Score: 130.40  E-value: 6.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  18 DEELYAGVYIDFM-GTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSaernDDKLYFFFRERSAEAPQSPAVY 96
Cdd:cd09295  128 DSKLYSATDHDFKdGDRPALSRRSSNVHYLRIVVDSSTGLDEITFVYAFVSGDD----DDEVYFFFRQEPVEYLKKGMVY 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  97 -ARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDgieTHFDELQDVFVQQTQDVRNpVIYAVFTSSGSVFRGSAVC 175
Cdd:cd09295  204 vPRIARVCKLDVGGCHRLKKKLTSFLKADLNCSRPQSG---FAFNLLQDATGDTKNLIQD-VKFAIFSSCLNKSVESAVC 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 176 VYSMADIRMVFNGPfahkegpnyqwmpfsgkmpyprpgtcpggtftpsmkstkdypdevinfmrshplmyqaVYPLQRRP 255
Cdd:cd09295  280 AYLFTDINNVFDDP----------------------------------------------------------VEAINNRP 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 256 LVVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVlpkDDQELEELMLEEVEVFKDPAPVKTMTISSKRQQL 335
Cdd:cd09295  302 LYAHQNQRSRLTSIAVDATKQKSVGYQVVFLGLKLGSLGKALA---FFFLYKGHIIEEWKVFKDSSRITNLDLSRPPLYL 378

                 ....*....
gi 578806453 336 YVASAVGVT 344
Cdd:cd09295  379 YVGSESGVL 387
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
421-502 5.90e-13

Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are composed of the immunoglobulin (Ig)-like domain in semaphorins. Semaphorins are transmembrane protein that have important roles in a variety of tissues. Functionally, semaphorins were initially characterized for their importance in the development of the nervous system and in axonal guidance. Later they have been found to be important for the formation and functioning of the cardiovascular, endocrine, gastrointestinal, hepatic, immune, musculoskeletal, renal, reproductive, and respiratory systems. Semaphorins function through binding to their receptors and transmembrane semaphorins also serves as receptors themselves. Although molecular mechanism of semaphorins is poorly understood, the Ig-like domains may be involved in ligand binding or dimerization.


Pssm-ID: 409368  Cd Length: 88  Bit Score: 64.79  E-value: 5.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 421 AGSAAFLECQPRSPQATVKWLFQRDPGDRRReirAEDRFLRTEQGLLLRALQLSDRGLYSCTATENNFKHVVTRVQLHVL 500
Cdd:cd04979   10 EGDTVILSCSVKSNNAPVTWIHNGKKVPRYR---SPRLVLKTERGLLIRSAQEADAGVYECHSGERVLGSTLRSVTLHVL 86

                 ..
gi 578806453 501 GR 502
Cdd:cd04979   87 ER 88
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
281-391 3.38e-08

The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor for class 6 semaphorins. Interactions between Plexin A2, A4 and semaphorins 6A and 6B control the lamina-restricted projection of hippocampal mossy fibers. Sema6B also repels the growth of mossy fibers in a Plexin A4 dependent manner. Plexin A2 does not suppress Sema6B function. In addition, studies have shown that Plexin A2 may be related to anxiety and other psychiatric disorders. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200533 [Multi-domain]  Cd Length: 515  Bit Score: 56.09  E-value: 3.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 281 YEVLFLGTDRGTVQKVIVlpkDDQELEELMLEEVEVFKDPAPV-KTMTISSKRQQLYVASAVGVTHLSLHRCQAYgAACA 359
Cdd:cd11272  406 YSVVFVGTKSGKLKKIRA---DGPPHGGVQYEMVSVFKDGSPIlRDMAFSIDHKYLYVMSERQVSRVPVESCEQY-TTCG 481
                         90       100       110
                 ....*....|....*....|....*....|...
gi 578806453 360 DCCLARDPYCAWdgqaCSRYTASSKR-RSRRQD 391
Cdd:cd11272  482 ECLSSGDPHCGW----CALHNMCSRRdKCQRAW 510
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
350-387 3.14e-07

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 47.15  E-value: 3.14e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 578806453   350 RCQAYGAaCADCCLARDPYCAWD--GQACSRYTASSKRRS 387
Cdd:smart00423   1 RCSKYTS-CSECLLARDPYCAWCssQGRCTSGERCDSRRQ 39
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
415-499 5.26e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.50  E-value: 5.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453   415 SVQYGVAGSAAFLECQPRS-PQATVKWLFQRDpgdrrREIRAEDRFLRTEQG----LLLRALQLSDRGLYSCTATeNNFK 489
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGsPPPEVTWYKQGG-----KLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAAT-NSSG 75
                           90
                   ....*....|
gi 578806453   490 HVVTRVQLHV 499
Cdd:smart00410  76 SASSGTTLTV 85
Sema_plexin_like cd11236
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
79-301 7.16e-07

The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine kinases; Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestor of semaphorins. Ligand binding activates signal transduction pathways controlling axon guidance in the nervous system and other developmental processes including cell migration and morphogenesis, immune function, and tumor progression. Plexins are divided into four types (A-D) according to sequence similarity. In vertebrates, type A Plexins serve as the co-receptors for neuropilins to mediate the signalling of class 3 semaphorins except Sema3E, which signals through Plexin D1. Plexins serve as direct receptors for several other members of the semaphorin family: class 6 semaphorins signal through type A plexins and class 4 semaphorins through type B. Plexin C1 serves as the receptor of Sema7A and plays regulation roles in both immune and nervous systems. This family also includes the Met and RON receptor tyrosine kinases. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200497 [Multi-domain]  Cd Length: 401  Bit Score: 51.56  E-value: 7.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  79 YFFFRERSaEAPQSPAVYARIGRICLNDdgghcclvNKWSTFLKARLVCSvpGEDGieTHFDELQDVFV---------QQ 149
Cdd:cd11236  196 YFVTVQRK-SVDDESPYISRLVRVCQSD--------SNYYSYTEVPLQCT--GGDG--TNYNLLQAAYVgkagsdlarSL 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 150 TQDVRNPVIYAVF----TSSGSVFRGSAVCVYSMADIRMVFNgpfahkegpnyqwmpfsgkmpyprpgtcpggtftpsmk 225
Cdd:cd11236  263 GISTDDDVLFGVFskskGPSAEPSSKSALCVFSMKDIEAAFN-------------------------------------- 304
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578806453 226 stkdypdevinfmRSHPLmyQAVYPLQRRPLVVRTgapyRLTTIAVDQVDaadgRYEVLFLGTDRGTVQKVIVLPK 301
Cdd:cd11236  305 -------------DNCPL--GGGVPITTSAVLSDS----LLTSVAVTTTR----NHTVAFLGTSDGQLKKVVLESS 357
Sema_plexin_B cd11245
The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin ...
70-304 8.45e-06

The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin domains, function as receptors of semaphorins and may be the ancestors of semaphorins. There are three members of the Plexin B subfamily, namely B1, B2 and B3. Plexins B1, B2 and B3 are receptors for Sema4D, Sema4C and Sema4G, and Sema5A, respectively. The activation of plexin B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. By signaling the effect of Sema4C and Sema4G, the plexin B2 receptor is critically involved in neural tube closure and cerebellar granule cell development. Plexin B3, the receptor of Sema5A, is a highly potent stimulator of neurite outgrowth of primary murine cerebellar neurons. Plexin B3 has been linked to verbal performance and white matter volume in human brain. Small GTPases play important roles in plexin B signaling. Plexin B1 activates Rho through Rho-specific guanine nucleotide exchange factors, leading to neurite retraction. Plexin B1 possesses an intrinsic GTPase-activating protein activity for R-Ras and induces growth cone collapse through R-Ras inactivation. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200506 [Multi-domain]  Cd Length: 440  Bit Score: 48.39  E-value: 8.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  70 SAERNDDKLYFFFRERSAEAPQSPAVYarIGRICLNDdgghcclvNKWSTFLKARLVCsvpgEDGIETHFDELQDVFVQQ 149
Cdd:cd11245  188 YAFADNGYIYFLFSRRPGTADSTKRTY--ISRLCEND--------HHYYSYVELPLNC----TVNQENTYNLVQAAYLAK 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 150 TQDVRN-PVIYAVFTSSGSVFRG----SAVCVYSMADIRMVFN--------GPFAHKEGPNYQWMPFSGK-----MPYPR 211
Cdd:cd11245  254 PGKVLNgKVLFGVFSADEASTAApdgrSALCMYPLSSVDARFErtrescytGEGLEDDKPETAYIEYNVKsicktLPDKN 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 212 PGTCP-GGTFTPSmkstkdypdevinfmrshPLMYQavYPLQRRPLVVRtgaPYRLTTIAVdqvdAADGRYEVLFLGTDR 290
Cdd:cd11245  334 VKAYPcGAEHTPS------------------PLASR--YPLAAKPILTR---NDMLTAVAV----AVENGHTIAFLGDSG 386
                        250
                 ....*....|....
gi 578806453 291 GTVQKVIVLPKDDQ 304
Cdd:cd11245  387 GQLHKVYLDPNHTD 400
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
427-499 1.87e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 43.15  E-value: 1.87e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806453 427 LECQPR-SPQATVKWLFQRDPGDRRREiraedRFLRTEQGLLLRALQLSDRGLYSCTATeNNFKHVVTRVQLHV 499
Cdd:cd20978   21 LPCQVTgVPQPKITWLHNGKPLQGPME-----RATVEDGTLTIINVQPEDTGYYGCVAT-NEIGDIYTETLLHV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
425-484 4.89e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 41.55  E-value: 4.89e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806453 425 AFLECQPR-SPQATVKWLfqRDPGDRRREIRAEDRFLRTEQGLLLRALQLSDRGLYSCTAT 484
Cdd:cd00096    1 VTLTCSASgNPPPTITWY--KNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVAS 59
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
415-484 9.60e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.01  E-value: 9.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806453  415 SVQYGVAGSAAFLECQPR-SPQATVKWLFqrdPGDRRREIRAEDRFLRTEQGLL-LRALQLSDRGLYSCTAT 484
Cdd:pfam13927   9 SSVTVREGETVTLTCEATgSPPPTITWYK---NGEPISSGSTRSRSLSGSNSTLtISNVTRSDAGTYTCVAS 77
Sema_plexin_B1 cd11275
The Sema domain, a protein interacting module, of Plexin B1; Plexin B1 serves as the ...
6-303 1.06e-04

The Sema domain, a protein interacting module, of Plexin B1; Plexin B1 serves as the Semaphorin 4D receptor and functions as a regulator of developing neurons and a tumor suppressor protein for melanoma. The Sema4D-plexin B signaling complex regulates dendritic and axonal complexity. The activation of Plexin B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. As a tumor suppressor, plexin B1 abrogates activation of the oncogenic receptor, c-Met, by its ligand, hepatocyte growth factor (HGF), in melanoma. Furthermore, plexin B1 suppresses integrin-dependent migration and activation of pp125FAK and inhibits Rho activity. Plexin B1 is highly expressed in endothelial cells and its activation by Sema4D elicits a potent proangiogenic response. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200536 [Multi-domain]  Cd Length: 461  Bit Score: 44.95  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453   6 PVTRRGEHVPGLDEELYAGVYIdfmgtdaaiFRTLGKQTAMRTDQYNSRWLNdpSFIHAElipdsaernddKLYFFFRER 85
Cdd:cd11275  158 PITTRNLRAHGDDATDSHSIFS---------YEETAKLAVGRLSEYNHHFIK--AFTYGS-----------SVYFLFYRR 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  86 SAEApQSPAVYARIGRICLNDdgghcclvNKWSTFLKARLVCsvpgeDGIETHFDELQDVFVQQTQ--------DVRNPV 157
Cdd:cd11275  216 DLKS-QSREYKTYISRICLDD--------SHYYSYVELPLLC-----QSKANTYSLLQAAYVTQPGerlaqgqlDTDGEV 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 158 IYAVFTS----SGSVFRGSAVCVYSMADIRMVFN----------------GPFAHKE---GPNYQWMPFSGKMPYPrpgt 214
Cdd:cd11275  282 LFAAFSAwqasSGKLSEESALCAYPMDEVDRLTNwtrdvcytrdgkaedgTEVAYIEydvSSNCVQLPADTLDAYP---- 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 215 CpGGTFTPSMKSTKDypdevinfmrshplmyqavyPLQRRPLVVRTGApyRLTTIAVDqvdaADGRYEVLFLGTDRGTVQ 294
Cdd:cd11275  358 C-GSDHTPSPMASRV--------------------PLEATPLLEWTEI--RLTAVAVN----VEDGHTIAFLGDSRGRLH 410

                 ....*....
gi 578806453 295 KVIVLPKDD 303
Cdd:cd11275  411 KVYLGAGGD 419
Sema_plexin_B2 cd11276
The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor ...
75-296 1.49e-04

The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor of Sema4C and Sema4G. By signaling the effect of Sema4C and Sema4G, the plexin B2 receptor plays important roles in neural tube closure and cerebellar granule cell development. Mice lacking Plexin B2 demonstrated defects in closure of the neural tube and disorganization of the embryonic brain. In developing kidney, Sema4C-Plexin B2 signaling modulates ureteric branching. Plexin B2 is expressed both in the pretubular aggregates and the ureteric epithelium in the developing kidney. Deletion of Plexin B2 results in renal hypoplasia and occasional double ureters. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200537 [Multi-domain]  Cd Length: 449  Bit Score: 44.38  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  75 DDKLYFFFRERSAEAPQSPAVYarIGRICLNDDGGHcclvnkwsTFLKARLVCSVPgedgiETHFDELQDVFV------- 147
Cdd:cd11276  198 DNNYVYFLFNQQLGHPDKNRTL--IARLCENDHHYY--------SYTEMDLNCRDG-----ANAYNKCQAAYVstpgkel 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 148 -QQTQDVR--NPVIYAVFTSSGSVFRGSAVCVYSMADI--RMVFNGPFAH---KEGPNYQWMPFSGKMPyprpgtCPGGT 219
Cdd:cd11276  263 aQNYGNSIlsDKVLFAVFSRDEKDSGESALCMFPLKSInaKMEANREACYtgtIDDRDVFYKPFHSQKD------IICGS 336
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806453 220 FTPsmKSTKDYP--DEvinFMRShPLMYQAVYPLqRRPLVVRTGApyRLTTIAVdqvdAADGRYEVLFLGTDRGTVQKV 296
Cdd:cd11276  337 HQQ--KNSKSFPcgSE---HLPY-PLGSRDELAL-TAPVLQRGGL--NLTAVTV----AVENGHTVAFLGTSDGRILKV 402
I-set pfam07679
Immunoglobulin I-set domain;
422-499 2.79e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.93  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453  422 GSAAFLECQPR-SPQATVKWLFQRdpgdrrREIRAEDRFLRTEQG----LLLRALQLSDRGLYSCTATeNNFKHVVTRVQ 496
Cdd:pfam07679  15 GESARFTCTVTgTPDPEVSWFKDG------QPLRSSDRFKVTYEGgtytLTISNVQPDDSGKYTCVAT-NSAGEAEASAE 87

                  ...
gi 578806453  497 LHV 499
Cdd:pfam07679  88 LTV 90
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
410-488 3.21e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 39.75  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 410 KNAVESVQYGVAGSAAFLECQPR-SPQATVKWLFqrdpGDRRreIRAEDRFLRTEQG-LLLRALQLSDRGLYSCTAtENN 487
Cdd:cd04969    5 LNPVKKKILAAKGGDVIIECKPKaSPKPTISWSK----GTEL--LTNSSRICILPDGsLKIKNVTKSDEGKYTCFA-VNF 77

                 .
gi 578806453 488 F 488
Cdd:cd04969   78 F 78
Ig_Sema4D_like cd05873
Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members ...
422-500 3.83e-04

Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins. Sema4D is a Class IV semaphorin. Semaphorins are classified based on structural features additional to the Sema domain. Sema4D has extracellular Sema and Ig domains, a transmembrane domain, and a short cytoplasmic domain. Sema4D plays a part in the development of GABAergic synapses. Sema4D in addition is an immune semaphorin. It is abundant on resting T cells; its expression is weak on resting B cells and antigen presenting cells (APCs), but is upregulated by various stimuli. The receptor used by Sema4D in the immune system is CD72. Sem4D enhances the activation of B cells and DCs through binding CD72, perhaps by reducing CD72s inhibitory signals. The receptor used by Sema4D in the non-lymphatic tissues is plexin-B1. Sem4D is anchored to the cell surface but its extracellular domain can be released from the cell surface by a metalloprotease-dependent process. Sem4D may mediate its effects in its membrane-bound form and/or its cleaved form.


Pssm-ID: 409457  Cd Length: 87  Bit Score: 39.80  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 422 GSAAFLECQPRSPQATVKWLFQRDPgdrrreIRAED-RFLRTEQGLLLRALQLSDRGLYSCTATEN-NFKHVVTRVQLHV 499
Cdd:cd05873   11 GGNAELKCSPKSNLARVVWKFQGKV------LKAESpKYGLYGDGLLIFNASEADAGRYQCLSVEKsKAKTFFQTVAKYV 84

                 .
gi 578806453 500 L 500
Cdd:cd05873   85 L 85
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
350-391 1.03e-03

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 37.30  E-value: 1.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 578806453  350 RCQAYGAaCADCCLARDPYCAWD--GQACSRYTASSKRRSRRQD 391
Cdd:pfam01437   1 RCSQYTS-CSSCLAARDPYCGWCssEGRCVRRSACGAPEGNCEE 43
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
417-487 8.24e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 35.83  E-value: 8.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578806453 417 QYGVAGSAAFLECQPR-SPQATVKWlfQRDPG---DRRREIRaEDRFLRteqgllLRALQLSDRGLYSCTAtENN 487
Cdd:cd05725    7 QVVLVDDSAEFQCEVGgDPVPTVRW--RKEDGelpKGRYEIL-DDHSLK------IRKVTAGDMGSYTCVA-ENM 71
Ig_Sema4B_like cd05872
Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are ...
420-500 8.46e-03

Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are composed of the immunoglobulin (Ig)-like domain of Sema4B and similar proteins. Sema4B is a Class IV semaphorin. Semaphorins are classified based on structural features additional to the Sema domain. Sema4B has extracellular Sema and Ig domains, a transmembrane domain, and a short cytoplasmic domain. Sema4B has been shown to preferentially regulate the development of the postsynaptic specialization at the glutamatergic synapses. This cytoplasmic domain includes a PDZ-binding motif upon which the synaptic localization of Sem4B is dependent. Sema4B is a ligand of CLCP1. CLCP1 was identified in an expression profiling analysis, which compared a highly metastic lung cancer subline with its low metastic parental line. Sema4B was shown to promote CLCP1 endocytosis and their interaction is a potential target for therapeutic intervention of metastasis.


Pssm-ID: 409456  Cd Length: 86  Bit Score: 35.88  E-value: 8.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806453 420 VAGSAAFLECQPRSPQATVKWLFqrdPGdrrREIRAEDRFLR-TEQGLLLRALQLSDRGLYSCTATENNFKHVVTRVQLH 498
Cdd:cd05872    9 VAGADVVLPCQLRSNLASPVWLF---NG---TPLNAQFSYLRlGTDGLLILVTSPEHSGTYRCYSEEEGFQQLVASYSLN 82

                 ..
gi 578806453 499 VL 500
Cdd:cd05872   83 VV 84
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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