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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673043  37 DLVTVVLGQDAKLPCFYRGDPDEQVGQVAWARVDPNEGTRELALLHSKYGLHVSPAYEDRVEQPPPPrDPLDGSILLRNA 116
Cdd:cd05888     1 DVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQEIALLHSKYGLHVFPAYEGRVEQPPPP-RPADGSVLLRNA 79

                          90       100
                  ....*....|....*....|....*....
gi 1958673043 117 VQADEGEYECRVSTFPAGSFQARMRLRVL 145
Cdd:cd05888    80 VQADEGEYECRVSTFPAGNFQAELRLRVL 108

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 1958673043 265 ATLKCLSEGQPPPKYNWTRLDGPLPSGVRVKGD------TLGFPPLTTEHSGVYVCHVSNELSSRASQVT 328
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRselgngTLTISNVTLEDSGTYTCVASNSAGGSASASV 70

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673043  37 DLVTVVLGQDAKLPCFYRGDPDEQVGQVAWARVDPNEGTRELALLHSKYGLHVSPAYEDRVEQPPPPrDPLDGSILLRNA 116
Cdd:cd05888     1 DVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQEIALLHSKYGLHVFPAYEGRVEQPPPP-RPADGSVLLRNA 79

                          90       100
                  ....*....|....*....|....*....
gi 1958673043 117 VQADEGEYECRVSTFPAGSFQARMRLRVL 145
Cdd:cd05888    80 VQADEGEYECRVSTFPAGNFQAELRLRVL 108

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 1958673043  34 ETSDLVTVVLGQDAKLPCFYRGDPDEQVGQVAWARVDPNEGTRELaLLHSKYGLHVsPAYEDRVEQPPPPRDPlDGSILL 113
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKGPTFL-IAYYSNGSEE-GVKKGRFSGRGDPSNG-DGSLTI 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958673043 114 RNAVQADEGEYECRVSTFPAGSFQARMRLRVL 145
Cdd:pfam07686  78 QNLTLSDSGTYTCAVIPSGEGVFGKGTRLTVL 109

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 1958673043 265 ATLKCLSEGQPPPKYNWTRLDGPLPSGVRVKGD------TLGFPPLTTEHSGVYVCHVSNELSSRASQVT 328
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRselgngTLTISNVTLEDSGTYTCVASNSAGGSASASV 70

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958673043 255 QNLWHVGREG--ATLKCLSEGQPPPKYNWTRLDGPLPSGVRVKGD------TLGFPPLTTEHSGVYVCHVSN 318
Cdd:pfam13927   7 SPSSVTVREGetVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSlsgsnsTLTISNVTRSDAGTYTCVASN 78

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673043  37 DLVTVVLGQDAKLPCFYRGDPDEQVGQVAWARVDPNEGTRELALLHSKYGLHVSPAYEDRVEQPPPPrDPLDGSILLRNA 116
Cdd:cd05888     1 DVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQEIALLHSKYGLHVFPAYEGRVEQPPPP-RPADGSVLLRNA 79

                          90       100
                  ....*....|....*....|....*....
gi 1958673043 117 VQADEGEYECRVSTFPAGSFQARMRLRVL 145
Cdd:cd05888    80 VQADEGEYECRVSTFPAGNFQAELRLRVL 108

Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (Necl-5)) and similar proteins. 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), these result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted, while 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" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the second Ig-like domain of nectin-1, also known as poliovirus receptor related protein(PVRL)1 or CD111.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673043 148 PLPSLNPGPPLEEGQGLTLAASCTAE-GSPAPSVTWDTEVKGTQSSRSFKHS-RSAAVTSEFHLVPSRSMNGQPLTCVVS 225
Cdd:cd05719     1 PTNSLEGGPALLIGGEPTLVATCISAnGKPPASVTWETDLKGEASTTQVRGSnGTVTVTSRYRLVPSREADGQPLTCVVE 80

                          90
                  ....*....|....*.
gi 1958673043 226 HPGLLQDQRITHTLQV 241
Cdd:cd05719    81 HPSLEKDQRISVTLNV 96

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 1958673043  34 ETSDLVTVVLGQDAKLPCFYRGDPDEQVGQVAWARVDPNEGTRELaLLHSKYGLHVsPAYEDRVEQPPPPRDPlDGSILL 113
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKGPTFL-IAYYSNGSEE-GVKKGRFSGRGDPSNG-DGSLTI 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958673043 114 RNAVQADEGEYECRVSTFPAGSFQARMRLRVL 145
Cdd:pfam07686  78 QNLTLSDSGTYTCAVIPSGEGVFGKGTRLTVL 109

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673043  39 VTVVLGQDAKLPCfyRGDPDEQVGQVAWARVDPNeGTRELALLHSKYGLHVSPAYEDRVEQPPPprDPLDGSILLRNAVQ 118
Cdd:cd05887     9 VTAVWGKNVSLKC--LIEVNETITQISWEKIHGK-SSQTVAVHHPQYGISIQGEYQGRVSFKNY--SLNDATITLHNVGF 83

                          90       100
                  ....*....|....*....|....*..
gi 1958673043 119 ADEGEYECRVSTFPAGSFQARMRLRVL 145
Cdd:cd05887    84 SDSGKYICKAVTFPLGNAQSSTTVTVL 110

Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; member of the C1-set of the Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673043 157 PLEEGQGLTLAASC-TAEGSPAPSVTWDTEVKGTQSSRSFKHSRSAAVT--SEFHLVPSRSMNGQPLTCVVSHPGLLQDQ 233
Cdd:cd07703     9 EVQAGGIPVPVARCvSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTvtSEYSLVPTPEANGKEVTCKVEHETLEEPQ 88

                  ....*...
gi 1958673043 234 RITHTLQV 241
Cdd:cd07703    89 LLPVTLSV 96

First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-1 (also known as poliovirus receptor related protein 1 (PVRL1) or cluster of differentiation (CD) 111). Nectin-1 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. In addition nectins heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls), nectin-1 for example, has been shown to trans-interact with Necl-1. Nectins also interact with various other proteins, including the actin filament (F-actin)-binding protein, afadin. Mutation in the human nectin-1 gene is associated with cleft lip/palate ectodermal dysplasia syndrome (CLPED1). Nectin-1 is a major receptor for herpes simplex virus through interaction with the viral envelope glycoprotein D.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673043  33 LETSDLVTVVLGQDAKLPC-FYRGDPDEQVGQVAWARVdPNEGTRELALLHSKYGLHVSPAYEDRVEQPPPPRDplDGSI 111
Cdd:cd05886     3 VQVNDSMSGFIGTDVVLHCsFANPLPSVKITQVTWQKS-TNGSKQNVAIYNPSMGVSVLPPYRERVTFLNPSFT--DGTI 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958673043 112 LLRNAVQADEGEYECRVSTFPAGSFQARMRLRVL 145
Cdd:cd05886    80 RLSRLELEDEGVYICEFATFPTGNRESQLNLTVM 113

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958673043 255 QNLWHVGREG--ATLKCLSEGQPPPKYNWTRLDGPLPSGVRVKGD------TLGFPPLTTEHSGVYVCHVSN 318
Cdd:pfam13927   7 SPSSVTVREGetVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSlsgsnsTLTISNVTRSDAGTYTCVASN 78

First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673043  39 VTVVLGQDAKLPCFYR-GDPDEQVGQVAWARVDPNEgtrELALLHSKYGLHVSPAyeDRVE--QPPPPRDPLDGSILLRN 115
Cdd:cd20989     9 VRGFLGGSVTLPCHLLpPNMVTHVSQVTWQRHDEHG---SVAVFHPKQGPSFPES--ERLSfvAARLGAELRNASLAMFG 83

                          90       100
                  ....*....|....*....|....*....
gi 1958673043 116 AVQADEGEYECRVSTFPAGSFQARMRLRV 144
Cdd:cd20989    84 LRVEDEGNYTCEFATFPQGSRSGDTWLRV 112

Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here are composed of the third immunoglobulin domain of Nectin-like Protein-5 (also known as Cluster of Differentiation 155 (CD155)). Nectin-like Protein-5 mediates NK (Natural Killer) cell adhesion and triggers NK cell effector functions. CD155 binds two different NK cell receptors: CD96 and CD226. These interactions accumulate at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. CD155 may also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Moreover, CD155 plays a role in mediating tumor cell invasion and migration.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673043 246 EASVRGLEDQnlWHVGREGATLKCLSEGQPPPK-YNWTRLDGPLPSGVRVKGDTLGFPPLTTEHSGVYVCHVSNELSSRA 324
Cdd:cd20930     2 EVSISGYDDN--WYLGRNEATLTCDVRSNPEPTgYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGR 79

                  ....*..
gi 1958673043 325 SQVTVEV 331
Cdd:cd20930    80 AEQTIFV 86

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 1958673043 263 EGATLKCLSEGQPPPKYNWtRLDG------PLPSGVRVKGDTLGFPPLTTEHSGVYVCHVSNELSSRASQVTVEVL 332
Cdd:cd04978    15 ETGELICEAEGNPQPTITW-RLNGvpiepaPEDMRRTVDGRTLIFSNLQPNDTAVYQCNASNVHGYLLANAFLHVL 89

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 1958673043 157 PLEEGQGLTLaaSCTAEGS-PAPSVTW---DTEVKGTQSSRSFKHSRSAAVTSEFHLVPSRSMNGQPLTCVVSHPGLLQD 232
Cdd:cd05761    15 PVVEGDEITL--TCTTSGSkPAADIRWfknDKELKGVKEVQESGAGKTFTVTSTLRFRVDRDDDGVAVICRVDHESLTST 92

                  ....
gi 1958673043 233 QRIT 236
Cdd:cd05761    93 PKQT 96

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 1958673043 252 LEDQNLwhvgregaTLKCLSEGQPPPKYNWTrldgpLPSGVRVKGDTLGFPPLTTEHSGVYVCHVSNELSSR-ASQVTV 329
Cdd:cd20948     8 LSGENL--------NLSCHAASNPPAQYSWT-----INGTFQTSSQELFLPAITENNEGTYTCSAHNSLTGKnISLVLS 73

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673043  35 TSDLVTVVLGQDAKLPCFY----RGDPDEQVGQVAWARVDPNEGTRELALLHSKYG-LHVSPAYEDRVEQPPPPRDPLDG 109
Cdd:cd05902     3 TAPPVRRPLSSSVLLPCVFtlppSASSPPEGPRIKWTKLSTSGGQQQRPVLVARDNvVRVAKAFQGRVSLPGYPKNRYNA 82

                          90
                  ....*....|....*....
gi 1958673043 110 SILLRNAVQADEGEYECRV 128
Cdd:cd05902    83 SLVLSRLRYSDSGTYRCEV 101

Immunoglobulin I-set domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958673043 263 EGATLKCLSEGQPPPKYNWTRLDGPLPSGVRVK------GDTLGFPPLTTEHSGVYVCHVSNELSSRASQVTVEV 331
Cdd:pfam07679  16 ESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKvtyeggTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90

Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The members here are composed of the fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule). NrCAM 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. NrCAM is primarily expressed in the nervous system.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958673043 263 EGATLKCLSEGQPPPKYNWTrLDG------PLPSGVRVKGDTLGFPPLTTEHSGVYVCHVSNELSSRASQVTVEVL 332
Cdd:cd05868    15 EDGTLICRANGNPKPSISWL-TNGvpieiaPTDPSRKVDGDTIIFSKVQERSSAVYQCNASNEYGYLLANAFVNVL 89

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673043  39 VTVVLGQDAKLPCFYRGDPDEQVGQVA-------WARVDPNEGTR-ELALLHSKYG-LHVSPAYEDRVEQPPPPRDPLDG 109
Cdd:cd05878     7 VRVLLGTSVTLPCYFIDPPHPVTPSTAplaprikWSKVSVDGKKEkEVVLLVATEGrVRVNSAYQGRVSLPNYPAIPSDA 86

                          90
                  ....*....|....*....
gi 1958673043 110 SILLRNAVQADEGEYECRV 128
Cdd:cd05878    87 TLEVQSLRASDSGLYRCEV 105

Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here are composed of the second immunoglobulin (Ig)-like domain in protein tyrosine kinase (PTK) 7, also known as CCK4. PTK7 is a subfamily of the receptor protein tyrosine kinase family, and is referred to as an RPTK-like molecule. RPTKs transduce extracellular signals across the cell membrane and play important roles in regulating cell proliferation, migration, and differentiation. PTK7 is organized as an extracellular portion having seven Ig-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase-like domain. PTK7 is considered a pseudokinase as it has several unusual residues in some of the highly conserved tyrosine kinase (TK) motifs; it is predicted to lack TK activity. PTK7 may function as a cell-adhesion molecule. PTK7 mRNA is expressed at high levels in placenta, melanocytes, liver, lung, pancreas, and kidney. PTK7 is overexpressed in several cancers, including melanoma and colon cancer lines.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958673043 266 TLKCLSEGQPPPKYNWTRLDGPLPSG-----VRVKGDTLGFPPLTTEHSGVYVCHVSNELSSRASQ 326
Cdd:cd05760    20 TLRCHIDGHPRPTYQWFRDGTPLSDGqgnysVSSKERTLTLRSAGPDDSGLYYCCAHNAFGSVCSS 85

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673043 264 GATLK--CLSEGQPPPKYNWTRLDGPLPSG--VRVKGDTLGFPPLTTEHSGVYVCHVSNE 319
Cdd:cd05728    14 GSSLRweCKASGNPRPAYRWLKNGQPLASEnrIEVEAGDLRITKLSLSDSGMYQCVAENK 73

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958673043 262 REGATLK--CLSEGQPP-PKYNWTRLDGPLPSGVRVKGDTLGFPPLTTEHSGVYVCHVSNEL 320
Cdd:cd05754    14 RPGADVSfiCRAKSKSPaYTLVWTRVNGTLPSRAMDFNGILTIRNVQLSDAGTYVCTGSNML 75

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673043  41 VVLGQDAKLPCFYRgDPDEQVG----------QVAWARVdpNEGTRELALLHSKYGLHVSPAYEDRVEQPPPPRDPLDGS 110
Cdd:cd05900     9 VVLGSSLLIPCYFQ-DPIAKDPgaptvaplspRIKWSFI--SKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAIPSDAT 85

                          90
                  ....*....|....*...
gi 1958673043 111 ILLRNAVQADEGEYECRV 128
Cdd:cd05900    86 LEITELRSNDSGTYRCEV 103

Second immunoglobulin (Ig)-like domain of nectin-like molecule 2 (Necl-2); member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of nectin-like molecule 2 (Necl-2; also known as cell adhesion molecule 1 (CADM1)). Nectin-like molecules (Necls) 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. Necl-2 has Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is expressed in a wide variety of tissues and is a putative tumour suppressor gene which is downregulated in aggressive neuroblastoma. Ig domains are likely to participate in ligand binding and recognition.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958673043 162 QGLTLAASCTAEGS-PAPSVTW---DTEVKGtQSSRSFKHSRSAAVTSEFHLVPSRSMNGQPLTCVVSHPGL--LQDQR 234
Cdd:cd05883    18 EGEEIELNCTAMASkPAATIRWfkgNKELTG-KSEVEEWYSRMFTVTSQLMLKVTKEDDGVPVICLVDHPAVkdLQTQR 95

First 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 first 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 1958673043 264 GATLKCLSEGQPPPKYNWTRLDGP----LPSGVRVKGD-TLGFPPLTTE------HSGVYVCHVSNELSSRASQ 326
Cdd:cd20955    19 GAEIECKASGNPMPEIIWIRSDGTavgdVPGLRQISSDgKLVFPPFRAEdyrqevHAQVYACLARNQFGSIISR 92

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 1958673043 153 NPGPPLEEGQGLTLaaSCTA-EGSPAPSVTWdtEVKGTQSSRSFKHSRSAAVT--SEFHLVPSRSMNGQPLTCVVSHPG 228
Cdd:pfam00047   3 PPTVTVLEGDSATL--TCSAsTGSPGPDVTW--SKEGGTLIESLKVKHDNGRTtqSSLLISNVTKEDAGTYTCVVNNPG 77

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 1958673043 259 HVGREG--ATLKC-LSEGQPPPKYNWTRLDGPLPSGVRVKGD-------TLGFPPLTTEHSGVYVCHVSNELSS 322
Cdd:pfam00047   6 VTVLEGdsATLTCsASTGSPGPDVTWSKEGGTLIESLKVKHDngrttqsSLLISNVTKEDAGTYTCVVNNPGGS 79

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958673043 260 VGREGATLKCLSEGQPPPKYNWT----RLDGPLPSgVRVKGDTLGFPPLTTEHSGVYVCHVSNELSSRASQVTVEV 331
Cdd:cd20978    14 KGGQDVTLPCQVTGVPQPKITWLhngkPLQGPMER-ATVEDGTLTIINVQPEDTGYYGCVATNEIGDIYTETLLHV 88

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673043  44 GQDAKLPCFYRGDPDEQVG---QVAWARVDPNEGTRELALL-----HSKYGlhvspAYEDRV--EQppppRDPLDGSILL 113
Cdd:cd05877    12 GGNVTLPCRYHYEPELSAPrkiRVKWTKLEVDYAKEEDVLVaigtrHKSYG-----SYQGRVflRR----ADDLDASLVI 82

                          90
                  ....*....|....*.
gi 1958673043 114 RNAVQADEGEYECRVS 129
Cdd:cd05877    83 TDLRLEDYGRYRCEVI 98

Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint molecules; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H3 also known as CD276), a member of the B7 family of immune checkpoint molecules. B7-H3 is an important immune checkpoint member of the B7 family and shares homology with other B7 ligands such as programmed death ligand 1 (PD-L1). The B7 family molecules interact with CD28 on T-cells to provide co-stimulatory signals that regulate T-cell activation and T-helper cell differentiation. Although B7-H3 has been shown to have both co-stimulatory and co-inhibitory effects on T-cell responses, the most current studies describe B7-H3 as a T cell inhibitor that promotes tumor aggressiveness and proliferation. Moreover, B7-H3 is highly overexpressed on a wide range of human solid cancers and promotes tumor growth, metastasis, and drug resistance. Thus, B7-H3 expression in tumors often correlates with both negative prognosis and poor clinical outcome in cancer patients. B7-H3 protein contains a predicted signal peptide, V- and C-like Ig domains (IgV and IgC), a transmembrane region, and an intracellular tail.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673043  37 DLVTVVLGQDAKLPCFYRGDPDEQVGQVA--WARVDPNEGTRELALLHSKyGLHVSPAYEDRVEQPPPPRDPLDGSILLR 114
Cdd:cd20934     5 DPVVALVGTDATLRCSFSPEPGFSLAQLSvfWQLTDTKQLVHSFTESQDQ-GRDQGSAYANRTALFPDLLAQGNASLRLQ 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958673043 115 NAVQADEGEYECRVSTFPAGSfqARMRLRVLVP 147
Cdd:cd20934    84 RVRVADEGSYTCFVSVQDFGS--AAVSLQVAAP 114