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Conserved domains on  [gi|1034643639|ref|XP_016864540|]
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hyaluronan and proteoglycan link protein 1 isoform X1 [Homo sapiens]

Protein Classification

immunoglobulin domain-containing family protein( domain architecture ID 10147181)

immunoglobulin (Ig) domain-containing family protein is a member of a large superfamily containing cell surface antigen receptors, co-receptors and co-stimulatory molecules of the immune system, molecules involved in antigen presentation to lymphocytes, cell adhesion molecules, certain cytokine receptors and intracellular muscle proteins; immunoglobulin domains are typically divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 43-161 2.70e-71

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), aggrecan, forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


:

Pssm-ID: 409461  Cd Length: 117  Bit Score: 217.58  E-value: 2.70e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  43 EAEQAKVFSHRGGNVTLPCKFYRDPTAfgSGIHKIRIKWTKLTSDYLKEVDVFVSMGYHKKTYGGYQGRVFLKGGSDSDA 122
Cdd:cd05877     1 ETVQAKVFSHRGGNVTLPCRYHYEPEL--SAPRKIRVKWTKLEVDYAKEEDVLVAIGTRHKSYGSYQGRVFLRRADDLDA 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034643639 123 SLVITDLTLEDYGRYKCEVIEGLEDDTVVVALDLQGVVF 161
Cdd:cd05877    79 SLVITDLRLEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 159-253 1.54e-69

Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


:

Pssm-ID: 239595  Cd Length: 95  Bit Score: 212.29  E-value: 1.54e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 159 VVFPYFPRLGRYNLNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGQNTVPGVRNY 238
Cdd:cd03518     1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRTVPGLRSY 80

                          90
                  ....*....|....*
gi 1034643639 239 GFWDKDKSRYDVFCF 253
Cdd:cd03518    81 GERDKMLSRYDAFCF 95
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 260-350 4.24e-57

Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


:

Pssm-ID: 239596  Cd Length: 91  Bit Score: 180.31  E-value: 4.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 260 RFYYLIHPTKLTYDEAVQACLNDGAQIAKVGQIFAAWKILGYDRCDAGWLADGSVRYPISRPRRRCSPTEAAVRFVGFPD 339
Cdd:cd03519     1 GVFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKFHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSFGFPD 80

                          90
                  ....*....|.
gi 1034643639 340 KKHKLYGVYCF 350
Cdd:cd03519    81 KKHKLYGVYCY 91
 
Name Accession Description Interval E-value
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 43-161 2.70e-71

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), aggrecan, forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409461  Cd Length: 117  Bit Score: 217.58  E-value: 2.70e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  43 EAEQAKVFSHRGGNVTLPCKFYRDPTAfgSGIHKIRIKWTKLTSDYLKEVDVFVSMGYHKKTYGGYQGRVFLKGGSDSDA 122
Cdd:cd05877     1 ETVQAKVFSHRGGNVTLPCRYHYEPEL--SAPRKIRVKWTKLEVDYAKEEDVLVAIGTRHKSYGSYQGRVFLRRADDLDA 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034643639 123 SLVITDLTLEDYGRYKCEVIEGLEDDTVVVALDLQGVVF 161
Cdd:cd05877    79 SLVITDLRLEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 159-253 1.54e-69

Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239595  Cd Length: 95  Bit Score: 212.29  E-value: 1.54e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 159 VVFPYFPRLGRYNLNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGQNTVPGVRNY 238
Cdd:cd03518     1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRTVPGLRSY 80

                          90
                  ....*....|....*
gi 1034643639 239 GFWDKDKSRYDVFCF 253
Cdd:cd03518    81 GERDKMLSRYDAFCF 95
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 260-350 4.24e-57

Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239596  Cd Length: 91  Bit Score: 180.31  E-value: 4.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 260 RFYYLIHPTKLTYDEAVQACLNDGAQIAKVGQIFAAWKILGYDRCDAGWLADGSVRYPISRPRRRCSPTEAAVRFVGFPD 339
Cdd:cd03519     1 GVFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKFHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSFGFPD 80

                          90
                  ....*....|.
gi 1034643639 340 KKHKLYGVYCF 350
Cdd:cd03519    81 KKHKLYGVYCY 91
Xlink pfam00193
Extracellular link domain;
159-253 8.77e-46

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 151.19  E-value: 8.77e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 159 VVFPYFPRlGRYNLNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGqnTVPGVRNY 238
Cdd:pfam00193   1 GVFHLESP-GRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGG--NMPGVRQY 77

                          90
                  ....*....|....*
gi 1034643639 239 GFWDKDKSRYDVFCF 253
Cdd:pfam00193  78 GFRDPLSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
157-254 2.42e-45

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 150.19  E-value: 2.42e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  157 QGVVFPYFPRlGRYNLNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGqnTVPGVR 236
Cdd:smart00445   1 DGGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG--NLPGVR 77

                           90
                   ....*....|....*...
gi 1034643639  237 NYGFWDKDkSRYDVFCFT 254
Cdd:smart00445  78 QYGFPDPT-SRYDAYCFN 94
LINK smart00445
Link (Hyaluronan-binding);
258-351 4.17e-39

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 134.01  E-value: 4.17e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  258 NGRFYYLIH--PTKLTYDEAVQACLNDGAQIAKVGQIFAAWKIlGYDRCDAGWLADGSVRYPISRPRRRCSPTEAAVRFV 335
Cdd:smart00445   1 DGGVFHVEKngRYKLTFAEAREACRAQGATLATVGQLYAAWQD-GFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVRQY 79

                           90
                   ....*....|....*.
gi 1034643639  336 GFPDKKHkLYGVYCFR 351
Cdd:smart00445  80 GFPDPTS-RYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
259-350 1.36e-34

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 122.30  E-value: 1.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 259 GRFYYlIHPT--KLTYDEAVQACLNDGAQIAKVGQIFAAWKiLGYDRCDAGWLADGSVRYPISRPRRRCSPTEAAVRFVG 336
Cdd:pfam00193   1 GVFHL-ESPGryKLTFQEAQAACAALGATLATPEQLYAAWK-AGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVRQYG 78

                          90
                  ....*....|....
gi 1034643639 337 FPDKKHKLYGVYCF 350
Cdd:pfam00193  79 FRDPLSERYDAYCY 92
IGv smart00406
Immunoglobulin V-Type;
56-141 4.48e-10

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 55.47  E-value: 4.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639   56 NVTLPCKFYrdptafGSGIHKIRIKWTKLTSDylKEVDVFVSMGYHKKTYG--GYQGRVFLKG-GSDSDASLVITDLTLE 132
Cdd:smart00406   1 SVTLSCKFS------GSTFSSYYVSWVRQPPG--KGLEWLGYIGSNGSSYYqeSYKGRFTISKdTSKNDVSLTISNLRVE 72


                   ....*....
gi 1034643639  133 DYGRYKCEV 141
Cdd:smart00406  73 DTGTYYCAV 81
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 53-142 7.85e-08

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 50.15  E-value: 7.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  53 RGGNVTLPCKFyrdpTAFGSGIHkIRIKWTKLTSDYLKEVDVFVsmgYHKK-TYGGYQGRV-FLKGGSDSDASLVITDLT 130
Cdd:pfam07686  10 LGGSVTLPCTY----SSSMSEAS-TSVYWYRQPPGKGPTFLIAY---YSNGsEEGVKKGRFsGRGDPSNGDGSLTIQNLT 81

                          90
                  ....*....|..
gi 1034643639 131 LEDYGRYKCEVI 142
Cdd:pfam07686  82 LSDSGTYTCAVI 93
 
Name Accession Description Interval E-value
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 43-161 2.70e-71

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), aggrecan, forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409461  Cd Length: 117  Bit Score: 217.58  E-value: 2.70e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  43 EAEQAKVFSHRGGNVTLPCKFYRDPTAfgSGIHKIRIKWTKLTSDYLKEVDVFVSMGYHKKTYGGYQGRVFLKGGSDSDA 122
Cdd:cd05877     1 ETVQAKVFSHRGGNVTLPCRYHYEPEL--SAPRKIRVKWTKLEVDYAKEEDVLVAIGTRHKSYGSYQGRVFLRRADDLDA 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034643639 123 SLVITDLTLEDYGRYKCEVIEGLEDDTVVVALDLQGVVF 161
Cdd:cd05877    79 SLVITDLRLEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 159-253 1.54e-69

Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239595  Cd Length: 95  Bit Score: 212.29  E-value: 1.54e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 159 VVFPYFPRLGRYNLNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGQNTVPGVRNY 238
Cdd:cd03518     1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRTVPGLRSY 80

                          90
                  ....*....|....*
gi 1034643639 239 GFWDKDKSRYDVFCF 253
Cdd:cd03518    81 GERDKMLSRYDAFCF 95
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 43-161 3.14e-64

Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in chondroitin sulfate proteoglycans (CSPGs) and human cartilage link protein (LP). Included in this group are the CSPGs aggrecan, versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. There is considerable evidence that HA-binding CSPGs are involved in developmental processes in the central nervous system. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409379  Cd Length: 123  Bit Score: 199.74  E-value: 3.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  43 EAEQAKVFSHRGGNVTLPCKFYRDPTAFGSGIHKIRIKWTKLTSD--YLKEVDVFVSMG---YHKKTYGGyQGRVFLKGG 117
Cdd:cd05714     1 EAESAKVFSHLGGNVTLPCKFYRDPTAFGSGIHKIRIKWTKLTSDsgYLKEVDVLVAMGnvvYHKKTYGG-RVSVPLKPG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034643639 118 SDSDASLVITDLTLEDYGRYKCEVIEGLEDDTVVVALDLQGVVF 161
Cdd:cd05714    80 SDSDASLVITDLTASDYGLYRCEVIEGIEDDQDVVALDVQGVVF 123
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 260-350 4.24e-57

Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239596  Cd Length: 91  Bit Score: 180.31  E-value: 4.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 260 RFYYLIHPTKLTYDEAVQACLNDGAQIAKVGQIFAAWKILGYDRCDAGWLADGSVRYPISRPRRRCSPTEAAVRFVGFPD 339
Cdd:cd03519     1 GVFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKFHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSFGFPD 80

                          90
                  ....*....|.
gi 1034643639 340 KKHKLYGVYCF 350
Cdd:cd03519    81 KKHKLYGVYCY 91
Xlink pfam00193
Extracellular link domain;
159-253 8.77e-46

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 151.19  E-value: 8.77e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 159 VVFPYFPRlGRYNLNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGqnTVPGVRNY 238
Cdd:pfam00193   1 GVFHLESP-GRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGG--NMPGVRQY 77

                          90
                  ....*....|....*
gi 1034643639 239 GFWDKDKSRYDVFCF 253
Cdd:pfam00193  78 GFRDPLSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
157-254 2.42e-45

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 150.19  E-value: 2.42e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  157 QGVVFPYFPRlGRYNLNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGqnTVPGVR 236
Cdd:smart00445   1 DGGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG--NLPGVR 77

                           90
                   ....*....|....*...
gi 1034643639  237 NYGFWDKDkSRYDVFCFT 254
Cdd:smart00445  78 QYGFPDPT-SRYDAYCFN 94
LINK smart00445
Link (Hyaluronan-binding);
258-351 4.17e-39

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 134.01  E-value: 4.17e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  258 NGRFYYLIH--PTKLTYDEAVQACLNDGAQIAKVGQIFAAWKIlGYDRCDAGWLADGSVRYPISRPRRRCSPTEAAVRFV 335
Cdd:smart00445   1 DGGVFHVEKngRYKLTFAEAREACRAQGATLATVGQLYAAWQD-GFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVRQY 79

                           90
                   ....*....|....*.
gi 1034643639  336 GFPDKKHkLYGVYCFR 351
Cdd:smart00445  80 GFPDPTS-RYDAYCFN 94
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 159-253 7.52e-35

The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It is found in the CD44 receptor and in human TSG-6. TSG-6 is the protein product of the tumor necrosis factor-stimulated gene-6. TSG-6 has a strong anti-inflammatory effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. This group also contains the link domains of the chondroitin sulfate proteoglycan core proteins (CSPG) including aggrecan, versican, neurocan, and brevican and the link domains of the vertebrate HAPLN (HA and proteoglycan binding link) protein family. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates in which other CSPGs substitute for aggregan might contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN gene family are physically linked adjacent to CSPG genes. TSG-6 contains a single link module which supports high affinity binding with HA. The functional HA-binding domain of CD44 is an extended domain comprised of a link module flanked with N-and C- extensions. These extensions are essential for folding and functional activity. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of the CSPG aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) which contains link modules 3 and 4 which lack HA-binding activity. HAPLNs contain two contiguous link modules.


Pssm-ID: 238534  Cd Length: 92  Bit Score: 122.91  E-value: 7.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 159 VVFPYFPRLGRYNLNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGQNtvPGVRNY 238
Cdd:cd01102     1 VVFHLESQNGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRN--PGVRSY 78

                          90
                  ....*....|....*
gi 1034643639 239 GFWDKdKSRYDVFCF 253
Cdd:cd01102    79 GNPAP-SGRYDAYCF 92
Xlink pfam00193
Extracellular link domain;
259-350 1.36e-34

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 122.30  E-value: 1.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 259 GRFYYlIHPT--KLTYDEAVQACLNDGAQIAKVGQIFAAWKiLGYDRCDAGWLADGSVRYPISRPRRRCSPTEAAVRFVG 336
Cdd:pfam00193   1 GVFHL-ESPGryKLTFQEAQAACAALGATLATPEQLYAAWK-AGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVRQYG 78

                          90
                  ....*....|....
gi 1034643639 337 FPDKKHKLYGVYCF 350
Cdd:pfam00193  79 FRDPLSERYDAYCY 92
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 159-253 5.94e-33

Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan. In addition, it is found in the first link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. In addition, aggrecan contains a second globular domain (G2) which contains link modules 3 and 4. G2 appears to lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 239594  Cd Length: 95  Bit Score: 117.89  E-value: 5.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 159 VVFPYFPRLGRYNLNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPC-GGQNTVPGVRN 237
Cdd:cd03517     1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCyGDMDGFPGVRN 80

                          90
                  ....*....|....*.
gi 1034643639 238 YGFWDKDKSrYDVFCF 253
Cdd:cd03517    81 YGVRDPDEL-YDVYCY 95
Link_domain_CSPGs_modules_2_4 cd03520
Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules ...
 262-350 1.45e-31

Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 239597  Cd Length: 96  Bit Score: 114.33  E-value: 1.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 262 YYLIHPTKLTYDEAVQACLNDGAQIAKVGQIFAAWKiLGYDRCDAGWLADGSVRYPISRPRRRCSPTEAAVRFV------ 335
Cdd:cd03520     3 FYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWR-QGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLyrfpnq 81

                          90
                  ....*....|....*.
gi 1034643639 336 -GFPDkKHKLYGVYCF 350
Cdd:cd03520    82 tGFPD-PHSRFDAYCF 96
Link_domain_CSPGs_modules_2_4 cd03520
Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules ...
 172-253 1.04e-27

Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 239597  Cd Length: 96  Bit Score: 104.32  E-value: 1.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 172 LNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGQntVPGVR-------NYGFWDKD 244
Cdd:cd03520    11 FTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGG--LPGVRtlyrfpnQTGFPDPH 88


                  ....*....
gi 1034643639 245 kSRYDVFCF 253
Cdd:cd03520    89 -SRFDAYCF 96
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 171-253 1.60e-26

Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239596  Cd Length: 91  Bit Score: 100.96  E-value: 1.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 171 NLNFHEAQQACLDQDAVIASFDQLYDAWR-GGLDWCNAGWLSDGSVQYPITKPREPCGGqnTVPGVRNYGFWDKDKSRYD 249
Cdd:cd03519    10 KLTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGP--LEPGVRSFGFPDKKHKLYG 87


                  ....
gi 1034643639 250 VFCF 253
Cdd:cd03519    88 VYCY 91
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 250-350 8.75e-24

The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It is found in the CD44 receptor and in human TSG-6. TSG-6 is the protein product of the tumor necrosis factor-stimulated gene-6. TSG-6 has a strong anti-inflammatory effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. This group also contains the link domains of the chondroitin sulfate proteoglycan core proteins (CSPG) including aggrecan, versican, neurocan, and brevican and the link domains of the vertebrate HAPLN (HA and proteoglycan binding link) protein family. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates in which other CSPGs substitute for aggregan might contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN gene family are physically linked adjacent to CSPG genes. TSG-6 contains a single link module which supports high affinity binding with HA. The functional HA-binding domain of CD44 is an extended domain comprised of a link module flanked with N-and C- extensions. These extensions are essential for folding and functional activity. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of the CSPG aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) which contains link modules 3 and 4 which lack HA-binding activity. HAPLNs contain two contiguous link modules.


Pssm-ID: 238534  Cd Length: 92  Bit Score: 93.64  E-value: 8.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 250 VFCFTSNfNGRFyylihptKLTYDEAVQACLNDGAQIAKVGQIFAAWKIlGYDRCDAGWLADGSVRYPISRPRRRCSPTE 329
Cdd:cd01102     2 VFHLESQ-NGRY-------KLTFAEAALACKARGAHLATPGQLEAAWQD-GFDVCTAGWLADGSVRYPIVTSRPNCGGRN 72

                          90       100
                  ....*....|....*....|.
gi 1034643639 330 AAVRFVGFPDKKhKLYGVYCF 350
Cdd:cd01102    73 PGVRSYGNPAPS-GRYDAYCF 92
Link_domain_TSG_6_like cd03515
This is the extracellular link domain of the type found in human TSG-6. The link domain is a ...
 160-253 7.11e-21

This is the extracellular link domain of the type found in human TSG-6. The link domain is a hyaluronan (HA)-binding domain. TSG-6 is the protein product of tumor necrosis factor-stimulated gene-6. TSG-6 is up-regulated in inflammatory lesions and in the ovary during ovulation. It has a strong anti-inflammatory and chondroprotective effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. Also included in this group are the stabilins: stabilin-1 (FEEL-1, CLEVER-1) and stabilin-2 (FEEL-2). Stabilin-2 functions as the major liver and lymph node-scavenging receptor for HA and related glycosaminoglycans. Stabilin-2 is a scavenger receptor with a broad range of ligands including advanced glycation end (AGE) products, acetylated low density lipoprotein and procollagen peptides. In contrast, stabilin-1 does not bind HA, but binds acetylated low density lipoprotein and AGEs with lower affinity. As AGEs accumulate in vascular tissues during aging and diabetes, these receptors may be implicated in the pathologies of these states. Both stabilins are present in the early endocytic pathway in hepatic sinusoidal epithelium associating with clathrin/AP-2. Stabilin-1 is expressed in macrophages. Stabilin-2 is absent from the latter. In macrophages: stabilin-1 is involved in trafficking between early/sorting endosomes and the trans-Golgi network. Stabilin-1 has also been implicated in angiogenesis and possibly leucocyte trafficking. Both stabilins bind gram-positive and gram-negative bacteria. TSG-6 and stabilins contain a single link module which supports high affinity binding to HA.


Pssm-ID: 239592  Cd Length: 93  Bit Score: 85.98  E-value: 7.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 160 VFPYFPRLGRYNLNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGgqNTVPGVRNYG 239
Cdd:cd03515     2 VFHLRSRSGKYKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCG--FGHVGIVDYG 79

                          90
                  ....*....|....
gi 1034643639 240 FWDKDKSRYDVFCF 253
Cdd:cd03515    80 PRLNLSERWDAYCY 93
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 261-350 4.89e-19

Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan. In addition, it is found in the first link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. In addition, aggrecan contains a second globular domain (G2) which contains link modules 3 and 4. G2 appears to lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 239594  Cd Length: 95  Bit Score: 80.91  E-value: 4.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 261 FYYLIHPTK--LTYDEAVQACLNDGAQIAKVGQIFAAWKIlGYDRCDAGWLADGSVRYPISRPRRRCSP---TEAAVRFV 335
Cdd:cd03517     3 FHYRDATARyaLTFPRAQRACLDISAQIATPEQLLAAYED-GFEQCDAGWLADQTVRYPIQTPREGCYGdmdGFPGVRNY 81

                          90
                  ....*....|....*
gi 1034643639 336 GFPDKKhKLYGVYCF 350
Cdd:cd03517    82 GVRDPD-ELYDVYCY 95
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 55-161 2.23e-17

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Like aggrecan, versican has a wide distribution in connective tissue and extracellular matrices. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409482  Cd Length: 128  Bit Score: 77.31  E-value: 2.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  55 GNVTLPCKFYRDPTAFGS-GIHK--IRIKWTKLTSDY----LKEVDVFVSMGYHKKTYGGYQGRVFLKGGSDS--DASLV 125
Cdd:cd05901    13 GSVVLPCRFSTLPTLPPSyNITSefLRIKWTKIQVDKngkdHKETTVLVAQNGIIKIGQEYMGRVSVPSHPEDqgDASLT 92

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034643639 126 ITDLTLEDYGRYKCEVIEGLEDDTVVVALDLQGVVF 161
Cdd:cd05901    93 IVKLRASDAGVYRCEVMHGIEDTQDTVSLDVSGVVF 128
Ig_Neurocan cd05902
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 55-161 1.02e-16

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Unlike aggrecan which is widely distributed in connective tissue and extracellular matrices, neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409483  Cd Length: 121  Bit Score: 75.26  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  55 GNVTLPCKFYRDPTAfGSGIHKIRIKWTKLTSDYL-KEVDVFVSMGYHKKTYGGYQGRVFLKG--GSDSDASLVITDLTL 131
Cdd:cd05902    13 SSVLLPCVFTLPPSA-SSPPEGPRIKWTKLSTSGGqQQRPVLVARDNVVRVAKAFQGRVSLPGypKNRYNASLVLSRLRY 91

                          90       100       110
                  ....*....|....*....|....*....|
gi 1034643639 132 EDYGRYKCEVIEGLEDDTVVVALDLQGVVF 161
Cdd:cd05902    92 SDSGTYRCEVVLGINDEQDTVPLEVTGVVF 121
Ig_Aggrecan_like cd05878
Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core ...
 54-161 6.70e-16

Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core protein (CSPG); The members here are composed of the immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core proteins (CSPGs). Included in this group are the Ig domains of other CSPGs: versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409462  Cd Length: 125  Bit Score: 73.42  E-value: 6.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  54 GGNVTLPCKFYRDPTAFGSGIHK--IRIKWTKLTSDY--LKEVDVFVSMGYHKKTYGGYQGRVFLKG--GSDSDASLVIT 127
Cdd:cd05878    12 GTSVTLPCYFIDPPHPVTPSTAPlaPRIKWSKVSVDGkkEKEVVLLVATEGRVRVNSAYQGRVSLPNypAIPSDATLEVQ 91

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034643639 128 DLTLEDYGRYKCEVIEGLEDDTVVVALDLQGVVF 161
Cdd:cd05878    92 SLRASDSGLYRCEVMHGIEDSQDTVELVVKGVVF 125
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 54-161 8.67e-15

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggrecan has a wide distribution in connective tissue and extracellular matrices. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409481  Cd Length: 123  Bit Score: 69.97  E-value: 8.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  54 GGNVTLPCKF----YRDPTAFGSGIHKIRIKWTKLTSDylKEVDVFVSMGYHKKTYGGYQGRVFLKG--GSDSDASLVIT 127
Cdd:cd05900    12 GSSLLIPCYFqdpiAKDPGAPTVAPLSPRIKWSFISKE--KESVLLVATEGKVRVNTEYLDRVSLPNypAIPSDATLEIT 89

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034643639 128 DLTLEDYGRYKCEVIEGLEDDTVVVALDLQGVVF 161
Cdd:cd05900    90 ELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 123
Link_domain_TSG_6_like cd03515
This is the extracellular link domain of the type found in human TSG-6. The link domain is a ...
 267-350 9.03e-14

This is the extracellular link domain of the type found in human TSG-6. The link domain is a hyaluronan (HA)-binding domain. TSG-6 is the protein product of tumor necrosis factor-stimulated gene-6. TSG-6 is up-regulated in inflammatory lesions and in the ovary during ovulation. It has a strong anti-inflammatory and chondroprotective effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. Also included in this group are the stabilins: stabilin-1 (FEEL-1, CLEVER-1) and stabilin-2 (FEEL-2). Stabilin-2 functions as the major liver and lymph node-scavenging receptor for HA and related glycosaminoglycans. Stabilin-2 is a scavenger receptor with a broad range of ligands including advanced glycation end (AGE) products, acetylated low density lipoprotein and procollagen peptides. In contrast, stabilin-1 does not bind HA, but binds acetylated low density lipoprotein and AGEs with lower affinity. As AGEs accumulate in vascular tissues during aging and diabetes, these receptors may be implicated in the pathologies of these states. Both stabilins are present in the early endocytic pathway in hepatic sinusoidal epithelium associating with clathrin/AP-2. Stabilin-1 is expressed in macrophages. Stabilin-2 is absent from the latter. In macrophages: stabilin-1 is involved in trafficking between early/sorting endosomes and the trans-Golgi network. Stabilin-1 has also been implicated in angiogenesis and possibly leucocyte trafficking. Both stabilins bind gram-positive and gram-negative bacteria. TSG-6 and stabilins contain a single link module which supports high affinity binding to HA.


Pssm-ID: 239592  Cd Length: 93  Bit Score: 66.33  E-value: 9.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 267 PTKLTYDEAVQACLNDGAQIAKVGQIFAAWKIlGYDRCDAGWLADGSVRYPISRPRRRCSPTEAAVRFVGFPDKKHKLYG 346
Cdd:cd03515    11 KYKLTYTEAKAACEAEGAHLATYSQLSAAQQL-GFHLCAAGWLAKGRVGYPIVFPSANCGFGHVGIVDYGPRLNLSERWD 89


                  ....
gi 1034643639 347 VYCF 350
Cdd:cd03515    90 AYCY 93
IGv smart00406
Immunoglobulin V-Type;
56-141 4.48e-10

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 55.47  E-value: 4.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639   56 NVTLPCKFYrdptafGSGIHKIRIKWTKLTSDylKEVDVFVSMGYHKKTYG--GYQGRVFLKG-GSDSDASLVITDLTLE 132
Cdd:smart00406   1 SVTLSCKFS------GSTFSSYYVSWVRQPPG--KGLEWLGYIGSNGSSYYqeSYKGRFTISKdTSKNDVSLTISNLRVE 72


                   ....*....
gi 1034643639  133 DYGRYKCEV 141
Cdd:smart00406  73 DTGTYYCAV 81
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 168-255 7.00e-09

This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It also plays an important role in arteriogenesis. The functional HA-binding domain of CD44 is an extended domain comprised of a single link module flanked with N-and C- extensions. These extensions are essential for folding and for functional activity. This group also contains the cell surface retention sequence (CRS) binding protein-1 (CRSBP-1) and lymph vessel endothelial receptor-1 (LYVE-1). CRSBP-1 is a cell surface binding protein for the CRS motif of PDGF-BB (platelet-derived growth factor-BB) and is responsible for the cell surface retention of PDGF-BB in SSV-transformed cells. CRSBP-1 may play a role in autocrine regulation of cell growth mediated by CRS containing growth regulators. LYVE-1 is preferentially expressed on the lymphatic endothelium and is used as a molecular marker for the detection and characterization of lymphatic vessels in tumors.


Pssm-ID: 239593  Cd Length: 144  Bit Score: 54.00  E-value: 7.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639 168 GRYNLNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGQNTvpGVrnYGFWDKDKSR 247
Cdd:cd03516    15 GRYSLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCGKNGT--GV--YILNSNLSSR 90


                  ....*...
gi 1034643639 248 YDVFCFTS 255
Cdd:cd03516    91 YDAYCYNS 98
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 53-142 7.85e-08

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 50.15  E-value: 7.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  53 RGGNVTLPCKFyrdpTAFGSGIHkIRIKWTKLTSDYLKEVDVFVsmgYHKK-TYGGYQGRV-FLKGGSDSDASLVITDLT 130
Cdd:pfam07686  10 LGGSVTLPCTY----SSSMSEAS-TSVYWYRQPPGKGPTFLIAY---YSNGsEEGVKKGRFsGRGDPSNGDGSLTIQNLT 81

                          90
                  ....*....|..
gi 1034643639 131 LEDYGRYKCEVI 142
Cdd:pfam07686  82 LSDSGTYTCAVI 93
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 54-141 8.23e-08

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other


Pssm-ID: 409552  Cd Length: 114  Bit Score: 50.14  E-value: 8.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  54 GGNVTLPCKFYRDPTAFGSgihkIRIKWTKLTSDYLKEVDVFVSMGyhkKTYGGY----QGRV-----FLKGgsdsDASL 124
Cdd:cd20960    15 GENVTLPCHHQLGLEDQGT----LDIEWLLLPSDKVEKVVITYSGD---RVYNHYypalKGRVaftsnDLSG----DASL 83

                          90
                  ....*....|....*..
gi 1034643639 125 VITDLTLEDYGRYKCEV 141
Cdd:cd20960    84 NISNLKLSDTGTYQCKV 100
IgV_B7-H6 cd20981
Immunoglobulin variable (IgV) domain of B7-H6; The members here are composed of the ...
 51-142 1.21e-07

Immunoglobulin variable (IgV) domain of B7-H6; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H6 (also known as NCR3LG1). B7-H6 contains one IgV domain and one IgC domain (IgV-IgC) and belongs to the B7-family, which consists of structurally related cell-surface protein ligands which bind to receptors on lymphocytes that regulate immune responses. B7-H6 is a ligand of NKp30, which is a member of CD28 family and an activating receptor of natural killer (NK) cells. The expression of NKp30 has been found in most of NK cells, which is involved in the process of tumor cell killing and interaction with antigen presenting cells (APCs) such as dendritic cells. Studies showed that NK cells eliminate B7-H6-expressing tumor cells either directly via cytotoxicity or indirectly by cytokine secretion. For instance, chimeric NKp30-expressing T cells responded to B7-H6(+) tumor cells and those T cells produced IFN-gamma and killed B7-H6-expressing tumor cells in vivo. B7-H6 mRNA is not found in normal cells, while high expression of B7-H6 is found in certain type tumor cells, such as lymphoma, leukemia, ovarian cancer, brain tumors, breast cancers, and various sarcomas. Since B7-H6 can bind NKp30 to exert anti-tumor effects by NK cells, which are able to recognize the difference between cancer cells and normal cells, B7-H6 may serve as a promising target for cancer immunotherapy.


Pssm-ID: 409573  Cd Length: 114  Bit Score: 49.53  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  51 SHRGGNVTLPCKFyrdptaFGSGIHKIRIK-----WTKLTSDylKEVDVFVSMGYHKKTY--GGYQGRVFLKGGsdsDAS 123
Cdd:cd20981    13 TPLNDNVTIFCNI------FYSQPLNITSMgitwfRKSLTFD--KEVKVFEFFGDHQKAFrpGAIVSPWRLKSG---DAS 81

                          90
                  ....*....|....*....
gi 1034643639 124 LVITDLTLEDYGRYKCEVI 142
Cdd:cd20981    82 LQLPGVQLEEAGEYRCEVV 100
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 54-141 5.26e-06

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).


Pssm-ID: 409383  Cd Length: 113  Bit Score: 44.75  E-value: 5.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  54 GGNVTLPCKFYrdptafGSGIHKI-RIKWTKLTSDYLKEVDVF-VSMGYHKKtyGGYQGRVFLKGGS--DSDASLVITDL 129
Cdd:cd05718    14 GGSVTLPCSLT------SPGTTKItQVTWMKIGAGSSQNVAVFhPQYGPSVP--NPYAERVEFLAARlgLRNATLRIRNL 85

                          90
                  ....*....|..
gi 1034643639 130 TLEDYGRYKCEV 141
Cdd:cd05718    86 RVEDEGNYICEF 97
IgV_VCBP cd20963
Immunoglobulin Variable region-containing chitin-binding proteins; an immunoglobulin V-set ...
 47-151 6.30e-06

Immunoglobulin Variable region-containing chitin-binding proteins; an immunoglobulin V-set domain; The members here are composed of the immunoglobulin variable (IgV) region-containing chitin-binding proteins (VCBPs). VCBPs are secreted, immune-type molecules that have been identified in both amphioxus and sea squirt (Ciona intestinalis). VCBPs, which consist of a leader peptide, two tandem N-terminal immunoglobulin V-type domains and a single C-terminal chitin-binding domain, belong to a multigene family encoding secreted proteins. The VCBPs were identified first in the cephalochordate Branchiostoma floridae and show structural similarities with V-type domains of immunoglobulins and T cell receptors, suggesting that VCBPs represent a unique gut-associated form of innate immune proteins. 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, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, 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. 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. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other.


Pssm-ID: 409555  Cd Length: 123  Bit Score: 44.92  E-value: 6.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  47 AKVFSHRGGNVTLPCKFYRDPTAfgsgiHKIRIKWTKLTSD------YLKEVDVFVSMGYHKKTYGGYQGRVFLKggSDS 120
Cdd:cd20963    10 TRTDPTWGNRVELPCSYTISPAA-----QPPTITWLKGISVdraevvFKGFKYWNETSSSGEVYFGDYAGRASVA--SLT 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034643639 121 DASLVITDLTLEDYGRYKCEVIE-------GLEDDTVV 151
Cdd:cd20963    83 QPTLVLTDLKFDDWGRYWCRVANwsqrdefGTDAESML 120
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 54-141 7.87e-06

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: 43.65  E-value: 7.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639   54 GGNVTLPCKFyrdptafgSGIHKIRIKWTKltsDYLKEVdvfvsmgyhkktygGYQGRVFLKGgSDSDASLVITDLTLED 133
Cdd:smart00410   9 GESVTLSCEA--------SGSPPPEVTWYK---QGGKLL--------------AESGRFSVSR-SGSTSTLTISNVTPED 62


                   ....*...
gi 1034643639  134 YGRYKCEV 141
Cdd:smart00410  63 SGTYTCAA 70
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
 54-142 2.54e-05

First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-4 (also known as poliovirus receptor related protein 4 or LNIR receptor). Nectin-4 belongs to the nectin family, which is comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example nectin-4 trans-interacts with nectin-1. Nectin-4 has also been shown to interact with the actin filament-binding protein, afadin. Unlike the other nectins, which are widely expressed in adult tissues, nectin-4 is mainly expressed during embryogenesis, and is not detected in normal adult tissue or in serum. Nectin-4 is re-expressed in breast carcinoma, and patients having metastatic breast cancer have a circulating form of nectin-4 formed from the ectodomain


Pssm-ID: 409471  Cd Length: 108  Bit Score: 42.96  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  54 GGNVTLPCKFYRDptafgSGIHKIRIKWTKLTSDYLKEVDVFVSMGYHKKTYGGYQGRVFLKGGSD-SDASLVITDLTLE 132
Cdd:cd05888     8 GQDAKLPCFYRGD-----SGEQVGQVAWARVDAGEGAQEIALLHSKYGLHVFPAYEGRVEQPPPPRpADGSVLLRNAVQA 82

                          90
                  ....*....|
gi 1034643639 133 DYGRYKCEVI 142
Cdd:cd05888    83 DEGEYECRVS 92
IgV_CRIg cd16089
Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin ...
 55-141 3.83e-05

Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin superfamily (CRIg); The members here are composed of the immunoglobulin variable (IgV) region of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also known as Z39Ig and V-set and Ig domain-containing 4 (VSIG4) belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. Like all members of this family, the CRIg domain contains two beta-sheets: one composed of strands A', G, F, C, C' and C", and the other of strands B, E and D. The complement system is an important part of the innate immune system and is required for removal of pathogens from the bloodstream. After exposure to pathogens, the third component of the complement system, C3, is cleaved to C3b which, after recruitment of factor B, initiates formation of the alternative pathway convertases. CRIg, a complement receptor expressed on macrophages, binds to C3b and iC3b mediating phagocytosis of the particles. It is also a potent inhibitor of the alternative pathway convertases and a negative regulator of T cell activation. 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, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, 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.


Pssm-ID: 409510  Cd Length: 117  Bit Score: 42.51  E-value: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  55 GNVTLPCKFyrDPTafgSGIHKIRIKWTkLTSDYlKEVDVFV--SMGYHKKTyGGYQGRVFLKGGSDSDASLVITDLTLE 132
Cdd:cd16089    15 GSVNLPCTY--VPE---EGYTQVLVKWL-VQRDS-DPVTIFLrdSSGDHIQQ-AKYRGRLEVSKDTPGDVSLQLDTLEMD 86


                  ....*....
gi 1034643639 133 DYGRYKCEV 141
Cdd:cd16089    87 DRGHYTCQV 95
IgV_1_JAM1-like cd20946
First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of ...
 42-157 1.61e-04

First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of the V-set of IgSF domains; The members here are composed of the first Ig-like domain of Junctional Adhesion Molecule-1 (JAM1)and similar domains. JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. 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 first Ig-like domain of JAM1 is a member of the V-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C'-C" in the other.


Pssm-ID: 409538  Cd Length: 102  Bit Score: 40.21  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  42 VEAEQAKVFSHRGGNVTLPCKFYRDPTAfgsgihkIRIKWTKLTsdylKEVDVFVSmgYHKKTYGGYQGRVflkggSDSD 121
Cdd:cd20946     2 VPSSQQVVTVVENQEVILSCKTPKKTSS-------PRVEWKKLQ----RDVTFVVF--QNNKIQGDYKGRA-----EILG 63

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034643639 122 ASLVITDLTLEDYGRYKCEVI---EGLEDDTVVVALDLQ 157
Cdd:cd20946    64 TNITIKNVTRSDSGKYRCEVSarsDGQNLGEVTVTLEVL 102
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 54-142 3.31e-04

First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor related protein 3), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 (PVRL3) or cluster of differentiation (CD) 113). Nectin-3 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example, during spermatid development, the nectin-3,-2 trans-interaction is required for the formation of Sertoli cell-spermatid junctions in testis, and during morphogenesis of the ciliary body, the nectin-3,-1 trans-interaction is important for apex-apex adhesion between the pigment and non-pigment layers of the ciliary epithelia. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-3 for example, trans-interacts with Necl-5, regulating cell movement and proliferation. Other proteins with which nectin-3 interacts include the actin filament-binding protein, afadin, integrin alpha-beta3, Par-3, and PDGF receptor; its interaction with PDGF receptor regulates the latter's signaling for anti-apoptosis.


Pssm-ID: 409470  Cd Length: 110  Bit Score: 39.53  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  54 GGNVTLPCKFYRDPTAfgsgihkIRIKWTKLTSDYLKEVDVFVSMgYHKKTYGGYQGRVFLKGGSDSDASLVITDLTLED 133
Cdd:cd05887    14 GKNVSLKCLIEVNETI-------TQISWEKIHGKSSQTVAVHHPQ-YGISIQGEYQGRVSFKNYSLNDATITLHNVGFSD 85


                  ....*....
gi 1034643639 134 YGRYKCEVI 142
Cdd:cd05887    86 SGKYICKAV 94
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 57-141 8.41e-04

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: 37.69  E-value: 8.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  57 VTLPCKFYRDPTAfgsgihkiRIKWTKltsdylKEVDVFVSMGYHKKTYGGyqgrvflkggsdsDASLVITDLTLEDYGR 136
Cdd:cd00096     1 VTLTCSASGNPPP--------TITWYK------NGKPLPPSSRDSRRSELG-------------NGTLTISNVTLEDSGT 53


                  ....*
gi 1034643639 137 YKCEV 141
Cdd:cd00096    54 YTCVA 58
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 38-141 1.11e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.55  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  38 PHLLVEAEQAKVFshRGGNVTLPCKFYRDPTAfgsgihkiRIKWTKltsDYLKEVDVFVSMGYHKKTYGgyqgrvflkgg 117
Cdd:pfam13927   2 PVITVSPSSVTVR--EGETVTLTCEATGSPPP--------TITWYK---NGEPISSGSTRSRSLSGSNS----------- 57

                          90       100
                  ....*....|....*....|....
gi 1034643639 118 sdsdaSLVITDLTLEDYGRYKCEV 141
Cdd:pfam13927  58 -----TLTISNVTRSDAGTYTCVA 76
IgV_CD2_like_N cd05775
N-terminal immunoglobulin (Ig)-like domain of T-cell surface antigen CD2, and similar domains; ...
 54-142 1.74e-03

N-terminal immunoglobulin (Ig)-like domain of T-cell surface antigen CD2, and similar domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain (or domain 1) of T-cell surface antigen Clusters of Differentiation (CD) 2 and similar proteins. CD2 is a T-cell specific surface glycoprotein and is critically important for mediating adhesion between T cells and antigen-presenting cells or between cytolytic T cells and target cells. CD2 is located on chromosome 1 at 1p13 in humans and on chromosome 3 in mice. CD2 contains an extracellular domain with two or Ig-like domains, a single transmembrane segment, and a cytoplasmic region rich in proline and basic residues.


Pssm-ID: 409431  Cd Length: 98  Bit Score: 37.33  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  54 GGNVTLpckfyrDPTAFGSGIHkiRIKWTKlTSDylKEVDVFVSMGyhKKTYGGYQGRVFLKGGSdsdASLVITDLTLED 133
Cdd:cd05775    10 GGNVTL------TISSLQDDID--EIKWKK-TKD--KIVEWENNIG--PTYFGSFKDRVLLDKES---GSLTIKNLTKED 73


                  ....*....
gi 1034643639 134 YGRYKCEVI 142
Cdd:cd05775    74 SGTYELEIT 82
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
 56-141 3.44e-03

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 36.60  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  56 NVTLPCKFYRDPTAFgsgIHkirikWTKLTSDYlkevdvFV-SMGYHKKTYGG----YQGR--VFLKGGSDSDASLVITD 128
Cdd:cd16091    14 DCILPCSFTPGSEVV---IH-----WYKQDSDI------KVhSYYYGKDQLESqdqrYRNRtsLFKDQISNGNASLLLRR 79

                          90
                  ....*....|...
gi 1034643639 129 LTLEDYGRYKCEV 141
Cdd:cd16091    80 VQLQDEGRYKCYT 92
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 47-141 9.56e-03

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.


Pssm-ID: 409380  Cd Length: 117  Bit Score: 35.48  E-value: 9.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643639  47 AKVFSHRGGNVTLPCKFyrdpTAFGSGIHKIRIKWTKLTSDYLKEVDVFVsmgYHK-----KTYGGYQGRVFLKGGSD-S 120
Cdd:cd05715     7 RELNVLNGSDVRLTCTF----TSCYTVGDAFSVTWTYQPEGGNTTESMFH---YSKgkpyiLKVGRFKDRVSWAGNPSkK 79

                          90       100
                  ....*....|....*....|.
gi 1034643639 121 DASLVITDLTLEDYGRYKCEV 141
Cdd:cd05715    80 DASIVISNLQFSDNGTYTCDV 100
 
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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