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 1907182748  848 VRFAPQVDHPTPLTKVAAAGDSTSSATLHCRARGVPNIDFTWTKNGVPLDLQDPRYTEHKYHQGVVHSSLLTIANVSAAQ 927
Cdd:cd05773      1 VRFAPDLQKGPQLRKVASRGDGSSDANLVCQAQGVPRVQFRWAKNGVPLDLGNPRYEETTEHTGTVHTSILTIINVSAAL 80

                           90       100
                   ....*....|....*....|....*....
gi 1907182748  928 DYALFKCTATNALGSDHTNIQLVSISRPD 956
Cdd:cd05773     81 DYALFTCTAHNSLGEDSLDIQLVSTSRPD 109

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  358 TILGSTSQSENKN--VTLCCLTKSSRPRVLLRWWLGGRQLLP-TDETVMDGLHGGHISMSNLTLLVKREDNGLSLTCEAF 434
Cdd:pfam08205    2 TIEPPASLLEGEGpeVVATCSSAGGKPAPRITWYLDGKPLEAaETSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQVS 81

                   ....*...
gi 1907182748  435 SDAFSKET 442
Cdd:pfam08205   82 YGALRGSI 89

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  754 PTIRALKDPTEVNVGGSVDIVCTVDANPilPEMFSWERLGEdeEELNLDDMEKMSKGSTGRLRIRQAKLSQAGAYQCIVD 833
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSP--PPTITWYKNGE--PISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77

                   .
gi 1907182748  834 N 834
Cdd:pfam13927   78 N 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        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  251 LFPPGPPVIDwpGLnEGHVRAGENLELPCIARGGNPPATLQWLKN-----GKPVSIAWGTEHAQAVAhSVLVMTVRPEDH 325
Cdd:cd05761      1 LGVPEKPVIT--GF-TSPVVEGDEITLTCTTSGSKPAADIRWFKNdkelkGVKEVQESGAGKTFTVT-STLRFRVDRDDD 76

                           90       100
                   ....*....|....*....|...
gi 1907182748  326 GARLSCQ----SYNSVSAETQER 344
Cdd:cd05761     77 GVAVICRvdheSLTSTPKQTQQV 99

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 1907182748  472 GTRVRLVCLAiGGNPEPSLTWLKDSRPVnDPRQSQEPRRVQLgsveksgstfsrELVLIIGPPDNLAKFSC----KAGQL 547
Cdd:cd05856     19 GSSVRLKCVA-SGNPRPDITWLKDNKPL-TPPEIGENKKKKW------------TLSLKNLKPEDSGKYTChvsnRAGEI 84

                   ....*...
gi 1907182748  548 SASTQLVV 555
Cdd:cd05856     85 NATYKVDV 92

Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain in human nephrin and similar proteins. Nephrin is an integral component of the slit diaphragm and is a central component of the glomerular ultrafilter. Nephrin plays a structural role and has a role in signaling. Nephrin is a transmembrane protein having a short intracellular portion, an extracellular portion comprised of eight Ig-like domains, and one fibronectin type III-like domain. The extracellular portions of nephrin from neighboring foot processes of separate podocyte cells may interact with each other, and in association with other components of the slit diaphragm form a porous molecular sieve within the slit pore. The intracellular portion of nephrin is associated with linker proteins, which connect nephrin to the actin cytoskeleton. The intracellular portion is tyrosine phosphorylated, and mediates signaling from the slit diaphragm into the podocytes.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  848 VRFAPQVDHPTPLTKVAAAGDSTSSATLHCRARGVPNIDFTWTKNGVPLDLQDPRYTEHKYHQGVVHSSLLTIANVSAAQ 927
Cdd:cd05773      1 VRFAPDLQKGPQLRKVASRGDGSSDANLVCQAQGVPRVQFRWAKNGVPLDLGNPRYEETTEHTGTVHTSILTIINVSAAL 80

                           90       100
                   ....*....|....*....|....*....
gi 1907182748  928 DYALFKCTATNALGSDHTNIQLVSISRPD 956
Cdd:cd05773     81 DYALFTCTAHNSLGEDSLDIQLVSTSRPD 109

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  358 TILGSTSQSENKN--VTLCCLTKSSRPRVLLRWWLGGRQLLP-TDETVMDGLHGGHISMSNLTLLVKREDNGLSLTCEAF 434
Cdd:pfam08205    2 TIEPPASLLEGEGpeVVATCSSAGGKPAPRITWYLDGKPLEAaETSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQVS 81

                   ....*...
gi 1907182748  435 SDAFSKET 442
Cdd:pfam08205   82 YGALRGSI 89

Fibronectin type III domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  956 DPPLGLKVVSVSPHSVGLEWKPGFDGGLP-QRFQIRYEALESPGFLYMDVLPAQATTFTLTGLKPSTRYRIWLLASNALG 1034
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPiTGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....*
gi 1907182748 1035 DSGLT 1039
Cdd:pfam00041   81 EGPPS 85

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748   955 PDPPLGLKVVSVSPHSVGLEWKPGFDGGlPQRFQIRYEALESPGFLYMDVL--PAQATTFTLTGLKPSTRYRIWLLASNA 1032
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDG-ITGYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 1907182748  1033 LGDS 1036
Cdd:smart00060   80 AGEG 83

Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, 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 of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  157 EAGSTVTWVAGQEYVVTCVSGDAKPAPDIIFIQGGRTVEDVSSSVNEGSEEKLFFTEAEARVTPQSSDNGQLLVCEGSNP 236
Cdd:cd05759      5 EGGPVISLQAGVPYNLTCRARGAKPAAEIIWFRDGEQLEGAVYSKELLKDGKRETTVSTLLITPSDLDTGRTFTCRARNE 84

                           90
                   ....*....|....
gi 1907182748  237 ALATPIKASFTMNI 250
Cdd:cd05759     85 AIPNGKETSITLDV 98

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  563 TILANSSALRPGDA-LNLTCVSISSNPPVNLSLDKEGERLDDVAAKPQSAPFKGSAASRSVF-LRVSSRDHGHRVTCRAH 640
Cdd:pfam08205    2 TIEPPASLLEGEGPeVVATCSSAGGKPAPRITWYLDGKPLEAAETSSEQDPESGLVTVTSELkLVPSRSDHGQSLTCQVS 81

                   ....*.
gi 1907182748  641 SEALRE 646
Cdd:pfam08205   82 YGALRG 87

Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 or CADM3), Necl-2 (also known as CADM1), Necl-3 (also known as CADM2) and Necl-4 (also known as CADM4). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 and Necl-2 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues, and is a putative tumour suppressor gene, which is downregulated in aggressive neuroblastoma. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system, where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Necl-4 is expressed on Schwann cells, and plays a key part in initiating peripheral nervous system (PNS) myelination. Necl-4 participates in cell-cell adhesion and is proposed to play a role in tumor suppression.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  558 PPTNLTILANSSALRPGDALNLTCVSISSNPPVNLSLDKEGERLDDVAAKPQSAPFKGSAASRSVFLRVSSRDHGHRVTC 637
Cdd:cd05761      3 VPEKPVITGFTSPVVEGDEITLTCTTSGSKPAADIRWFKNDKELKGVKEVQESGAGKTFTVTSTLRFRVDRDDDGVAVIC 82

                           90       100
                   ....*....|....*....|
gi 1907182748  638 RAHSEALRET-VSSFYRLNV 656
Cdd:cd05761     83 RVDHESLTSTpKQTQQVLEV 102

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

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907182748    52 SENLTVVEGSTVKLWCGVRA-PGSVVQWAKDGLLLgpnpkIPGFPRYSLEGDSakGEFHLLIEACDLSDDAEYECQV 127
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGsPPPEVTWYKQGGKL-----LAESGRFSVSRSG--STSTLTISNVTPEDSGTYTCAA 70

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  472 GTRVRLVCLAiGGNPEPSLTWLKDSRPVnDPRQSQEPRRVQLgsveksgstfsrELVLIIGPPDNLAKFSC----KAGQL 547
Cdd:cd05856     19 GSSVRLKCVA-SGNPRPDITWLKDNKPL-TPPEIGENKKKKW------------TLSLKNLKPEDSGKYTChvsnRAGEI 84

                   ....*...
gi 1907182748  548 SASTQLVV 555
Cdd:cd05856     85 NATYKVDV 92

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth 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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  761 DPTEVNVGGSVDIVCTVDANPILPEMFSWERLGE--DEEELNLDDMEKMSKGSTGRLRIRQAKLSQAGAYQCIVDNgVAP 838
Cdd:cd04970     10 SNADITVGENATLQCHASHDPTLDLTFTWSFNGVpiDLEKIEGHYRRRYGKDSNGDLEIVNAQLKHAGRYTCTAQT-VVD 88

                           90
                   ....*....|....
gi 1907182748  839 AARGLVRLVVRFAP 852
Cdd:cd04970     89 SDSASATLVVRGPP 102

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  660 PEFLGEQVRAVTVVEQG-QALLPVSVSANPAPeAFNWTFRGYRLSpaGGPRHRILSGGALQLWNVTRADDGFYQLHCQNS 738
Cdd:cd04969      1 PDFELNPVKKKILAAKGgDVIIECKPKASPKP-TISWSKGTELLT--NSSRICILPDGSLKIKNVTKSDEGKYTCFAVNF 77

                           90
                   ....*....|..
gi 1907182748  739 EGTAEALLKLDV 750
Cdd:cd04969     78 FGKANSTGSLSV 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 1907182748   52 SENLTVVEGSTVKLWC----GVRAPGSVVQWAKDGLLLGPNPKIPGF----------PRYSLEGDSAKGEFHLLIEACDL 117
Cdd:pfam07686    3 PREVTVALGGSVTLPCtyssSMSEASTSVYWYRQPPGKGPTFLIAYYsngseegvkkGRFSGRGDPSNGDGSLTIQNLTL 82

                           90
                   ....*....|.
gi 1907182748  118 SDDAEYECQVG 128
Cdd:pfam07686   83 SDSGTYTCAVI 93

Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 or CADM3), Necl-2 (also known as CADM1), Necl-3 (also known as CADM2) and Necl-4 (also known as CADM4). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 and Necl-2 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues, and is a putative tumour suppressor gene, which is downregulated in aggressive neuroblastoma. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system, where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Necl-4 is expressed on Schwann cells, and plays a key part in initiating peripheral nervous system (PNS) myelination. Necl-4 participates in cell-cell adhesion and is proposed to play a role in tumor suppression.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907182748  357 VTILGSTSQsENKNVTLCCLTKSSRPRVLLRWWLGGRQLLPTDETVMDGLHGGHISMSNLTLLVKREDNGLSLTCEA 433
Cdd:cd05761      9 ITGFTSPVV-EGDEITLTCTTSGSKPAADIRWFKNDKELKGVKEVQESGAGKTFTVTSTLRFRVDRDDDGVAVICRV 84

Immunoglobulin I-set domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  660 PEFLGeQVRAVTVVEQGQALLPVSVSANPAPEaFNWTFRGYRLSPagGPRHRIL-SGGALQLW--NVTRADDGFYQLHCQ 736
Cdd:pfam07679    1 PKFTQ-KPKDVEVQEGESARFTCTVTGTPDPE-VSWFKDGQPLRS--SDRFKVTyEGGTYTLTisNVQPDDSGKYTCVAT 76

                           90
                   ....*....|....
gi 1907182748  737 NSEGTAEALLKLDV 750
Cdd:pfam07679   77 NSAGEAEASAELTV 90

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

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748   464 PEGQSIRTGTRVRLVCLAIGgNPEPSLTWLKdsrpvNDPRQSQEPRRVqlgSVEKSGSTFSrelvLIIGP--PDNLAKFS 541
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASG-SPPPEVTWYK-----QGGKLLAESGRF---SVSRSGSTST----LTISNvtPEDSGTYT 67

                            90
                    ....*....|....*...
gi 1907182748   542 CKA----GQLSASTQLVV 555
Cdd:smart00410   68 CAAtnssGSASSGTTLTV 85

Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain in human nephrin and similar proteins. Nephrin is an integral component of the slit diaphragm and is a central component of the glomerular ultrafilter. Nephrin plays a structural role and has a role in signaling. Nephrin is a transmembrane protein having a short intracellular portion, an extracellular portion comprised of eight Ig-like domains, and one fibronectin type III-like domain. The extracellular portions of nephrin from neighboring foot processes of separate podocyte cells may interact with each other, and in association with other components of the slit diaphragm form a porous molecular sieve within the slit pore. The intracellular portion of nephrin is associated with linker proteins, which connect nephrin to the actin cytoskeleton. The intracellular portion is tyrosine phosphorylated, and mediates signaling from the slit diaphragm into the podocytes.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  848 VRFAPQVDHPTPLTKVAAAGDSTSSATLHCRARGVPNIDFTWTKNGVPLDLQDPRYTEHKYHQGVVHSSLLTIANVSAAQ 927
Cdd:cd05773      1 VRFAPDLQKGPQLRKVASRGDGSSDANLVCQAQGVPRVQFRWAKNGVPLDLGNPRYEETTEHTGTVHTSILTIINVSAAL 80

                           90       100
                   ....*....|....*....|....*....
gi 1907182748  928 DYALFKCTATNALGSDHTNIQLVSISRPD 956
Cdd:cd05773     81 DYALFTCTAHNSLGEDSLDIQLVSTSRPD 109

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  358 TILGSTSQSENKN--VTLCCLTKSSRPRVLLRWWLGGRQLLP-TDETVMDGLHGGHISMSNLTLLVKREDNGLSLTCEAF 434
Cdd:pfam08205    2 TIEPPASLLEGEGpeVVATCSSAGGKPAPRITWYLDGKPLEAaETSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQVS 81

                   ....*...
gi 1907182748  435 SDAFSKET 442
Cdd:pfam08205   82 YGALRGSI 89

Fibronectin type III domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  956 DPPLGLKVVSVSPHSVGLEWKPGFDGGLP-QRFQIRYEALESPGFLYMDVLPAQATTFTLTGLKPSTRYRIWLLASNALG 1034
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPiTGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....*
gi 1907182748 1035 DSGLT 1039
Cdd:pfam00041   81 EGPPS 85

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748   955 PDPPLGLKVVSVSPHSVGLEWKPGFDGGlPQRFQIRYEALESPGFLYMDVL--PAQATTFTLTGLKPSTRYRIWLLASNA 1032
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDG-ITGYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 1907182748  1033 LGDS 1036
Cdd:smart00060   80 AGEG 83

Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, 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 of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  157 EAGSTVTWVAGQEYVVTCVSGDAKPAPDIIFIQGGRTVEDVSSSVNEGSEEKLFFTEAEARVTPQSSDNGQLLVCEGSNP 236
Cdd:cd05759      5 EGGPVISLQAGVPYNLTCRARGAKPAAEIIWFRDGEQLEGAVYSKELLKDGKRETTVSTLLITPSDLDTGRTFTCRARNE 84

                           90
                   ....*....|....
gi 1907182748  237 ALATPIKASFTMNI 250
Cdd:cd05759     85 AIPNGKETSITLDV 98

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. 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. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lacks a C" strand.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  868 DSTSSATLHCRARGVPNIDFTWTKNGVPLDL-QDPRYTEHKyhqgvvHSSLLTI-ANVSAAQDY-ALFKCTATNALGSDH 944
Cdd:cd05733     14 DPRDNITIKCEAKGNPQPTFRWTKDGKFFDPaKDPRVSMRR------RSGTLVIdNHNGGPEDYqGEYQCYASNELGTAI 87

                   ....*..
gi 1907182748  945 TN-IQLV 950
Cdd:cd05733     88 SNeIRLV 94

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  858 TPLTKVAAAGDStssATLHCRARGVPNIDFTWTKNGVPLDLQDPRYTEHkyhqgVVHSSLLTIANVSaAQDYALFKCTAT 937
Cdd:pfam13927    7 SPSSVTVREGET---VTLTCEATGSPPPTITWYKNGEPISSGSTRSRSL-----SGSNSTLTISNVT-RSDAGTYTCVAS 77

                   .
gi 1907182748  938 N 938
Cdd:pfam13927   78 N 78

Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 or CADM3), Necl-2 (also known as CADM1), Necl-3 (also known as CADM2) and Necl-4 (also known as CADM4). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 and Necl-2 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues, and is a putative tumour suppressor gene, which is downregulated in aggressive neuroblastoma. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system, where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Necl-4 is expressed on Schwann cells, and plays a key part in initiating peripheral nervous system (PNS) myelination. Necl-4 participates in cell-cell adhesion and is proposed to play a role in tumor suppression.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  251 LFPPGPPVIDwpGLnEGHVRAGENLELPCIARGGNPPATLQWLKN-----GKPVSIAWGTEHAQAVAhSVLVMTVRPEDH 325
Cdd:cd05761      1 LGVPEKPVIT--GF-TSPVVEGDEITLTCTTSGSKPAADIRWFKNdkelkGVKEVQESGAGKTFTVT-STLRFRVDRDDD 76

                           90       100
                   ....*....|....*....|...
gi 1907182748  326 GARLSCQ----SYNSVSAETQER 344
Cdd:cd05761     77 GVAVICRvdheSLTSTPKQTQQV 99

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  858 TPLTKVAAAGDSTssATLHCRARGVPNIDFTWTKNGVPLDLQDPRYTehkyhqgvVHSSLLTIANVSaAQDYALFKCTAT 937
Cdd:cd20978      6 KPEKNVVVKGGQD--VTLPCQVTGVPQPKITWLHNGKPLQGPMERAT--------VEDGTLTIINVQ-PEDTGYYGCVAT 74

                           90
                   ....*....|....
gi 1907182748  938 NALGSDHTNIQLVS 951
Cdd:cd20978     75 NEIGDIYTETLLHV 88

Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 or CADM3), Necl-2 (also known as CADM1), Necl-3 (also known as CADM2) and Necl-4 (also known as CADM4). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 and Necl-2 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues, and is a putative tumour suppressor gene, which is downregulated in aggressive neuroblastoma. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system, where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Necl-4 is expressed on Schwann cells, and plays a key part in initiating peripheral nervous system (PNS) myelination. Necl-4 participates in cell-cell adhesion and is proposed to play a role in tumor suppression.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182748  558 PPTNLTILANSSALRPGDALNLTCVSISSNPPVNLSLDKEGERLDDVAAKPQSAPFKGSAASRSVFLRVSSRDHGHRVTC 637
Cdd:cd05761      3 VPEKPVITGFTSPVVEGDEITLTCTTSGSKPAADIRWFKNDKELKGVKEVQESGAGKTFTVTSTLRFRVDRDDDGVAVIC 82

                           90       100
                   ....*....|....*....|
gi 1907182748  638 RAHSEALRET-VSSFYRLNV 656
Cdd:cd05761     83 RVDHESLTSTpKQTQQVLEV 102