First immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM); The members here are composed of the immunoglobulin (Ig)-like domain 1 in carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) proteins. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions: it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two (D1, D4) or four (D1-D4) Ig-like domains on the cell surface.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195  36 LTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQATPGPANSGRETIYPNASLLIQNVTQN 115
Cdd:cd05774   1 LTIELVPPQVAEGENVLLLVHNLPENLLAYAWYKGKTVSPNFLIASYIISTNSSTPGPAYSGRETIYPNGSLLIQNVTQK 80

                        90       100
                ....*....|....*....|....*
gi 19923195 116 DTGFYTLQVIKSDLVNEEATGQFHV 140
Cdd:cd05774  81 DTGFYTLQTITADLQTEQASVHLQV 105

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195 327 KPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWFFKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQ 406
Cdd:cd05740   1 KPFISSNNSNPVEDKDAVTLTCEPETQNTSYLWWFNGQSLPVTPRLTLSNGNRTLTLLNVTREDAGAYQCEISNPVSANR 80

                ....*....
gi 19923195 407 SDPIMLNVN 415
Cdd:cd05740  81 SDPVTLDVI 89

First immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM); The members here are composed of the immunoglobulin (Ig)-like domain 1 in carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) proteins. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions: it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two (D1, D4) or four (D1-D4) Ig-like domains on the cell surface.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195  36 LTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQATPGPANSGRETIYPNASLLIQNVTQN 115
Cdd:cd05774   1 LTIELVPPQVAEGENVLLLVHNLPENLLAYAWYKGKTVSPNFLIASYIISTNSSTPGPAYSGRETIYPNGSLLIQNVTQK 80

                        90       100
                ....*....|....*....|....*
gi 19923195 116 DTGFYTLQVIKSDLVNEEATGQFHV 140
Cdd:cd05774  81 DTGFYTLQTITADLQTEQASVHLQV 105

Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) domains 2, 4, and 6, and similar domains; The members here are composed of the second, fourth, and sixth immunoglobulin (Ig)-like domains in human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) protein subfamily. The CEA family is a group of anchored or secreted glycoproteins expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions; it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two [D1, D4] or four [D1-D4] Ig-like domains on the cell surface.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195 327 KPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWFFKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQ 406
Cdd:cd05740   1 KPFISSNNSNPVEDKDAVTLTCEPETQNTSYLWWFNGQSLPVTPRLTLSNGNRTLTLLNVTREDAGAYQCEISNPVSANR 80

                ....*....
gi 19923195 407 SDPIMLNVN 415
Cdd:cd05740  81 SDPVTLDVI 89

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195    38 TESMPFNVAEGKEVLLLVHNLPQ---QLFGYSWYKGERVDGNRQ-IVGYAIGTQQATPGPANSGRETI-YPNASLLIQNV 112
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSmseASTSVYWYRQPPGKGPTFlIAYYSNGSEEGVKKGRFSGRGDPsNGDGSLTIQNL 80

                          90       100
                  ....*....|....*....|....*....
gi 19923195   113 TQNDTGFYTLQVIKSDLVNEEATGQFHVY 141
Cdd:pfam07686  81 TLSDSGTYTCAVIPSGEGVFGKGTRLTVL 109

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195   331 KASKTTVTGDKDSVNLTCS--TNDTGISIRWFFKNQSLPSSERMKLS---QGNTTLSINPVKREDAGTYWCEVFNPISKN 405
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSasTGSPGPDVTWSKEGGTLIESLKVKHDngrTTQSSLLISNVTKEDAGTYTCVVNNPGGSA 80

                  ....*.
gi 19923195   406 QSDPIM 411
Cdd:pfam00047  81 TLSTSL 86

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

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19923195    342 DSVNLTCS-TNDTGISIRWFF-KNQSLPSSERMKLSQ--GNTTLSINPVKREDAGTYWCEVFNPiSKNQSDPIMLNV 414
Cdd:smart00410  10 ESVTLSCEaSGSPPPEVTWYKqGGKLLAESGRFSVSRsgSTSTLTISNVTPEDSGTYTCAATNS-SGSASSGTTLTV 85

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195    157 VEDKDAVAFTCEPETQDTTYLWWINN--QSLPVSPRLQLSN--GNRTLTLLSVTRNDTGPYECEIQNPvSANRSDPVTLN 232
Cdd:smart00410   6 VKEGESVTLSCEASGSPPPEVTWYKQggKLLAESGRFSVSRsgSTSTLTISNVTPEDSGTYTCAATNS-SGSASSGTTLT 84

                   .
gi 19923195    233 V 233
Cdd:smart00410  85 V 85

IL-1 receptor-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195  106 SLLIQNVTQNDTGFYTLQvIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFtcEPETQDTTYLWWINNQSL 185
Cdd:PHA02826  99 NLWIGNVINIDEGIYICT-ISSGNICEESTIRLTFDSGTINYQFNSGKDSKLHCYGTDGI--SSTFKDYTLTWYKNGNIV 175

                         90       100       110
                 ....*....|....*....|....*....|..
gi 19923195  186 PVSPRLQLSNGNRTLTLLSVTRNDTGPYECEI 217
Cdd:PHA02826 176 LYTDRIQLRNNNSTLVIKSATHDDSGIYTCNL 207

First immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM); The members here are composed of the immunoglobulin (Ig)-like domain 1 in carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) proteins. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions: it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two (D1, D4) or four (D1-D4) Ig-like domains on the cell surface.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195  36 LTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQATPGPANSGRETIYPNASLLIQNVTQN 115
Cdd:cd05774   1 LTIELVPPQVAEGENVLLLVHNLPENLLAYAWYKGKTVSPNFLIASYIISTNSSTPGPAYSGRETIYPNGSLLIQNVTQK 80

                        90       100
                ....*....|....*....|....*
gi 19923195 116 DTGFYTLQVIKSDLVNEEATGQFHV 140
Cdd:cd05774  81 DTGFYTLQTITADLQTEQASVHLQV 105

Immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) and related domains. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions: it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two (D1, D4) or four (D1-D4) Ig-like domains on the cell surface. This family corresponds to the D1 Ig-like domain. Also belonging to this group is the N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule (SLAM) family, CD84-like family. The SLAM family is a group of immune-cell specific receptors that can regulate both adaptive and innate immune responses. SLAM family proteins are organized as an extracellular domain with having two or four Ig-like domains, a single transmembrane segment, and a cytoplasmic region having Tyr-based motifs. The extracellular domain is organized as a membrane-distal Ig variable (IgV) domain that is responsible for ligand recognition and a membrane-proximal truncated Ig constant-2 (IgC2) domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195  40 SMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQATPGPANSGRETIYPNASLLIQNVTQNDTGF 119
Cdd:cd05741   2 SEQFYGAEGKNVLLLVPNLQTPLKSVSWYKGKQVSRNDEIAEYENSSDEFRAGSAFSGREYIYTNGSLLIQNITLSDTGF 81

                        90       100
                ....*....|....*....|.
gi 19923195 120 YTLQVIKSDLVNEEATGQFHV 140
Cdd:cd05741  82 YTLESTNIGGKTESATFQLHV 102

Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains; member of the C2-set IgSF domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), also known as CD66e (Cluster of Differentiation 66e), is a cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression. Diseases associated with CEACAM5 include lung cancer and rectum cancer. 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 C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923195 243 SPSDTYYRPGANLSLSCYAASNPPAQYSWLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIV 318
Cdd:cd20948   1 SPSDTYYLSGENLNLSCHAASNPPAQYSWTINGTFQTSSQELFLPAITENNEGTYTCSAHNSLTGKNISLVLSVTV 76

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19923195   240 PTISPSDTYYRPGANLSLSCYAASNPPAQYSWLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVkTIIV 318
Cdd:pfam13895   2 PVLTPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNFFTLSVSAEDSGTYTCVARNGRGGKVSNPV-ELTV 79

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923195   241 TISPSDTYYRPGANLSLSCYAASNPPAQYSWLINGT-----------FQQSTQELFIPNITVNNSGSYTCHANN 303
Cdd:pfam13927   5 TVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEpissgstrsrsLSGSNSTLTISNVTRSDAGTYTCVASN 78

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195 344 VNLTCS-TNDTGISIRWFFKNQSLPSS--ERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPI 410
Cdd:cd00096   1 VTLTCSaSGNPPPTITWYKNGKPLPPSsrDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70

Immunoglobulin I-set domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195   317 IVTELSPVVAKPQikaskttvtgdkDSVNLTCSTndTG---ISIRWFFKNQSLPSSERMKLSQ--GNTTLSINPVKREDA 391
Cdd:pfam07679   3 FTQKPKDVEVQEG------------ESARFTCTV--TGtpdPEVSWFKDGQPLRSSDRFKVTYegGTYTLTISNVQPDDS 68

                          90
                  ....*....|....*..
gi 19923195   392 GTYWCEVFNPISKNQSD 408
Cdd:pfam07679  69 GKYTCVATNSAGEAEAS 85

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195 255 LSLSCYAASNPPAQYSWLING-----------TFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTV 313
Cdd:cd00096   1 VTLTCSASGNPPPTITWYKNGkplppssrdsrRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195    157 VEDKDAVAFTCEPETQDTTYLWWINN--QSLPVSPRLQLSN--GNRTLTLLSVTRNDTGPYECEIQNPvSANRSDPVTLN 232
Cdd:smart00410   6 VKEGESVTLSCEASGSPPPEVTWYKQggKLLAESGRFSVSRsgSTSTLTISNVTPEDSGTYTCAATNS-SGSASSGTTLT 84

                   .
gi 19923195    233 V 233
Cdd:smart00410  85 V 85

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group 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 Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19923195 250 RPGANLSLSCYAASNPPAQYSWLINGT-------FQQS---TQE------LFIPNITVNNSGSYTCHANNSV 305
Cdd:cd20956  14 QPGPSVSLKCVASGNPLPQITWTLDGFpipesprFRVGdyvTSDgdvvsyVNISSVRVEDGGEYTCTATNDV 85

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19923195 242 ISPSDTYYRPGANLSLSCYAASNPPAQYSWLING-----------TFQQSTQELFIPNITVNNSGSYTCHANNSV 305
Cdd:cd05736   5 VYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGmdinpklskqlTLIANGSELHISNVRYEDTGAYTCIAKNEG 79

Immunoglobulin I-set domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923195   241 TISPSDTYYRPGANLSLSCYAASNPPAQYSWLING-----------TFQQSTQELFIPNITVNNSGSYTCHANNSV 305
Cdd:pfam07679   4 TQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGqplrssdrfkvTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group 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 Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 19923195 356 SIRWFFKNQSLPSSERMKLSQgNTTLSINPV-KREDAGTYWCEVFNPisKNQSD 408
Cdd:cd20958  31 SITWEKDGRRLPLNHRQRVFP-NGTLVIENVqRSSDEGEYTCTARNQ--QGQSA 81

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third 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. This group belongs to the I-set of IgSF domains.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923195 244 PSDTYYRPGANLSLSCYAASNPPAQYSWLINGTFQQSTQE-------LFIPNITVNNSGSYTCHANNS 304
Cdd:cd04968   8 PADTYALKGQTVTLECFALGNPVPQIKWRKVDGSPSSQWEittsepvLEIPNVQFEDEGTYECEAENS 75

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19923195   157 VEDKDAVAFTCEPETQD--TTYLWWINNQSLPVSPRLQLSNGNRT---LTLLSVTRNDTGPYECEIQNPVS 222
Cdd:pfam00047   8 VLEGDSATLTCSASTGSpgPDVTWSKEGGTLIESLKVKHDNGRTTqssLLISNVTKEDAGTYTCVVNNPGG 78

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19923195 241 TISPSDTYYRPGANLSLSCYAASNPPAQYSWLINGTFQQST----------QELFIPNITVNNSGSYTCHANN 303
Cdd:cd04978   3 IIEPPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPApedmrrtvdgRTLIFSNLQPNDTAVYQCNASN 75

Third immunoglobulin domain in Cluster of Differentiation (CD) 22; member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain in Cluster of Differentiation (CD) 22 (also known as Siglec-2). CD22, a sialic-acid binding immunoglobulin type-lectin (Siglec) family member, is an inhibitory co-receptor of the B-cell receptor (BCR). The inhibitory function of CD22 and its restricted expression on B cells makes CD22 an attractive target against dysregulated B cells that cause autoimmune diseases and B-cell-derived cancers. CD22 plays a vital role in establishing a baseline level of B-cell inhibition, and thus is an important determinant of homeostasis in humoral immunity. Siglecs are primarily expressed on immune cells and recognize sialic acid-containing glycan ligands. Siglecs are organized as an extracellular module composed of Ig-like domains (an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains), followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG (Siglec-4, myelin-associated glycoprotein), the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11. 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 C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923195 242 ISPSDTYYRPGANLSLSCYAASNPP--AQYSWLINGTF--QQSTQELFIPNITVNNSGSYTCHANNSV 305
Cdd:cd20937   7 VTPSDAIVREGDSVTMTCEVSSSNPeyTTVSWLKDGTSlkKQNTFTLNLREVTKDQSGKYCCQVSNDV 74

IL-1 receptor-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195  213 YECEIQNPVSANRSDPVTLNVT--------YGPDTPTISPSDTYYRPGanlSLSCYAASNPPAQYSWLINGTFQQSTQEL 284
Cdd:PHA02826  24 YRGGDLTPVYAKFGDPMVLLCTgkhykksiFFDKTFITSYNVTWSKTD---SLAFVRDSGARTKIKKITHNEIGDRSENL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195  285 FIPNITVNNSGSYTCHANNSvTGCNRTTVKTIIVTELSPVvakpQIKASKttvtgdkdSVNLTCSTNDtGIS-------I 357
Cdd:PHA02826 101 WIGNVINIDEGIYICTISSG-NICEESTIRLTFDSGTINY----QFNSGK--------DSKLHCYGTD-GISstfkdytL 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195  358 RWFFKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFnpISKNqsdpimlNVNYN 417
Cdd:PHA02826 167 TWYKNGNIVLYTDRIQLRNNNSTLVIKSATHDDSGIYTCNLR--FNKN-------SNNYN 217

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195   146 KPSISSNNSNpVEDKDAVAFTCE-PETQDTTYLWWINNQSLPVSPRLQLSNgnrtltllsVTRNDTGPYECEIQNPVSAN 224
Cdd:pfam13895   1 KPVLTPSPTV-VTEGEPVTLTCSaPGNPPPSYTWYKDGSAISSSPNFFTLS---------VSAEDSGTYTCVARNGRGGK 70

                  ....*....
gi 19923195   225 RSDPVTLNV 233
Cdd:pfam13895  71 VSNPVELTV 79

IL-1 receptor-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195  106 SLLIQNVTQNDTGFYTLQvIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFtcEPETQDTTYLWWINNQSL 185
Cdd:PHA02826  99 NLWIGNVINIDEGIYICT-ISSGNICEESTIRLTFDSGTINYQFNSGKDSKLHCYGTDGI--SSTFKDYTLTWYKNGNIV 175

                         90       100       110
                 ....*....|....*....|....*....|..
gi 19923195  186 PVSPRLQLSNGNRTLTLLSVTRNDTGPYECEI 217
Cdd:PHA02826 176 LYTDRIQLRNNNSTLVIKSATHDDSGIYTCNL 207

First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-5. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains, anchored to the membrane by glycosylphosphatidylinositol. The different contactins show different expression patterns in the central nervous system. In rats, a lack of contactin-5 (NB-2) results in an impairment of the neuronal activity in the auditory system. Contactin-5 is expressed specifically in the postnatal nervous system, peaking at about 3 weeks postnatal. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala; lower levels of expression have been detected in the corpus callosum, caudate nucleus, and spinal cord. This group belongs to the I-set of IgSF domains.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19923195 255 LSLSCYAASNPPAQYSWLINGT-------FQQSTQE--LFIPNIT-VNNSGSYTCHANNSV 305
Cdd:cd05848  22 VILNCEARGNPVPTYRWLRNGTeidtesdYRYSLIDgnLIISNPSeVKDSGRYQCLATNSI 82

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup 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. 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. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin 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. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923195 241 TISPSDTYYRPGANLSLSCYAASNPPAQYSWLING--TFQQSTQ----------ELFIPNITVNNSGSYTCHANNS 304
Cdd:cd05763   3 TKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGgtDFPAARErrmhvmpeddVFFIVDVKIEDTGVYSCTAQNS 78

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923195 326 AKPQIKASKTTVTGDKDSVNLTC-STNDTGISIRWFFKNQSLPSSER-------MKLSQGNTTLSINPVKREDAGTYWCE 397
Cdd:cd05732   1 VQPKITYLENQTAVELEQITLTCeAEGDPIPEITWRRATRGISFEEGdldgrivVRGHARVSSLTLKDVQLTDAGRYDCE 80

                ....*....
gi 19923195 398 VFNPISKNQ 406
Cdd:cd05732  81 ASNRIGGDQ 89

First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 19923195 263 SNPPAQYS--WLINGTFQQSTQE-LFIPNITVNNSGSYTCHANNS 304
Cdd:cd05752  25 FYSPEQNStqWYHNGTLISSTSSsYRIVAATVNDSGEYRCQTQGS 69