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 767910535  38 DVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQELALLHSKYGLHVSPAYEGRVEQPPPPRnPLDGSVLLRNA 117
Cdd:cd05888    1 DVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQEIALLHSKYGLHVFPAYEGRVEQPPPPR-PADGSVLLRNA 79

                         90       100
                 ....*....|....*....|....*....
gi 767910535 118 VQADEGEYECRVSTFPAGSFQARLRLRVL 146
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 767910535 266 AMLKCLSEGQPPPSYNWTRLDGPLPSGVRVDGD------TLGFPPLTTEHSGIYVCHVSNEFSSRDSQVT 329
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 767910535  38 DVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQELALLHSKYGLHVSPAYEGRVEQPPPPRnPLDGSVLLRNA 117
Cdd:cd05888    1 DVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQEIALLHSKYGLHVFPAYEGRVEQPPPPR-PADGSVLLRNA 79

                         90       100
                 ....*....|....*....|....*....
gi 767910535 118 VQADEGEYECRVSTFPAGSFQARLRLRVL 146
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 767910535   35 ETSDVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQELaLLHSKYGLHVsPAYEGRVEQPPPPRNPlDGSVLL 114
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKGPTFL-IAYYSNGSEE-GVKKGRFSGRGDPSNG-DGSLTI 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 767910535  115 RNAVQADEGEYECRVSTFPAGSFQARLRLRVL 146
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 767910535 266 AMLKCLSEGQPPPSYNWTRLDGPLPSGVRVDGD------TLGFPPLTTEHSGIYVCHVSNEFSSRDSQVT 329
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 767910535   259 WHIGREG--AMLKCLSEGQPPPSYNWTRLDGPL---PSGVRVDGD----TLGFPPLTTEHSGIYVCHVSNEFSSRDSQVT 329
Cdd:smart00410   3 SVTVKEGesVTLSCEASGSPPPEVTWYKQGGKLlaeSGRFSVSRSgstsTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                   ...
gi 767910535   330 VDV 332
Cdd:smart00410  83 LTV 85

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 767910535  38 DVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQELALLHSKYGLHVSPAYEGRVEQPPPPRnPLDGSVLLRNA 117
Cdd:cd05888    1 DVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQEIALLHSKYGLHVFPAYEGRVEQPPPPR-PADGSVLLRNA 79

                         90       100
                 ....*....|....*....|....*....
gi 767910535 118 VQADEGEYECRVSTFPAGSFQARLRLRVL 146
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 767910535 149 PLPSLNPGPALEEGQGLTLAASCTAE-GSPAPSVTWDTEVKGTTSSRSFKHS-RSAAVTSEFHLVPSRSMNGQPLTCVVS 226
Cdd:cd05719    1 PTNSLEGGPALLIGGEPTLVATCISAnGKPPASVTWETDLKGEASTTQVRGSnGTVTVTSRYRLVPSREADGQPLTCVVE 80

                         90
                 ....*....|....*.
gi 767910535 227 HPGLLQDQRITHILHV 242
Cdd:cd05719   81 HPSLEKDQRISVTLNV 96

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910535  40 VTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGaQELALLHSKYGLHVSPAYEGRVEQPPPPRNPLDGSVLLRNAVQ 119
Cdd:cd05718    9 VTGFLGGSVTLPCSLTSPGTTKITQVTWMKIGAGSS-QNVAVFHPQYGPSVPNPYAERVEFLAARLGLRNATLRIRNLRV 87

                         90       100
                 ....*....|....*....|....*.
gi 767910535 120 ADEGEYECRVSTFPAGSFQARLRLRV 145
Cdd:cd05718   88 EDEGNYICEFATFPQGNRQGTTWLRV 113

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 767910535  40 VTVVLGQDAKLPCfyRGDSGEQVGQVAWARVdAGEGAQELALLHSKYGLHVSPAYEGRVEQppppRNP--LDGSVLLRNA 117
Cdd:cd05887    9 VTAVWGKNVSLKC--LIEVNETITQISWEKI-HGKSSQTVAVHHPQYGISIQGEYQGRVSF----KNYslNDATITLHNV 81

                         90       100
                 ....*....|....*....|....*....
gi 767910535 118 VQADEGEYECRVSTFPAGSFQARLRLRVL 146
Cdd:cd05887   82 GFSDSGKYICKAVTFPLGNAQSSTTVTVL 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 767910535 162 GQGLTLAASC-TAEGSPAPSVTWDTEVKG--TTSSRSFKHSRSAAVTSEFHLVPSRSMNGQPLTCVVSHPGLLQDQRITH 238
Cdd:cd07703   13 GGIPVPVARCvSANGRPPARISWSSTLNGnaNTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVEHETLEEPQLLPV 92

                 ....
gi 767910535 239 ILHV 242
Cdd:cd07703   93 TLSV 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 767910535  34 LETSDVVTVVLGQDAKLPC-FYRGDSGEQVGQVAWARVDAGEgAQELALLHSKYGLHVSPAYEGRVEQppppRNPL--DG 110
Cdd:cd05886    3 VQVNDSMSGFIGTDVVLHCsFANPLPSVKITQVTWQKSTNGS-KQNVAIYNPSMGVSVLPPYRERVTF----LNPSftDG 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767910535 111 SVLLRNAVQADEGEYECRVSTFPAGSFQARLRLRVL 146
Cdd:cd05886   78 TIRLSRLELEDEGVYICEFATFPTGNRESQLNLTVM 113

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 767910535  36 TSDVVTVVLGQDAKLPCFY----RGDSGEQVGQVAWARVDAGEGAQELALLHSKYG-LHVSPAYEGRVEQPPPPRNPLDG 110
Cdd:cd05902    3 TAPPVRRPLSSSVLLPCVFtlppSASSPPEGPRIKWTKLSTSGGQQQRPVLVARDNvVRVAKAFQGRVSLPGYPKNRYNA 82

                         90
                 ....*....|....*....
gi 767910535 111 SVLLRNAVQADEGEYECRV 129
Cdd:cd05902   83 SLVLSRLRYSDSGTYRCEV 101

First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910535  41 TVVLGQDAKLPCFYRGDsgEQVGQVAWARVdAGEGAQELALLHSKYGLHVSPAYEGRVEQPPPprNPLDGSVLLRNAVQA 120
Cdd:cd05846    9 RAVLGGNATLSCNLTLP--EEVLQVTWQKI-KASSPENIVTYSKKYGVKIQPSYVRRISFTSS--GLNSTSITIWNVTLE 83

                         90       100
                 ....*....|....*....|....*
gi 767910535 121 DEGEYECRVSTFPAGSFQARLRLRV 145
Cdd:cd05846   84 DEGCYKCLFNTFPDGIKSGTACLTV 108

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910535   259 WHIGREG--AMLKCLSEGQPPPSYNWTRLDGPL---PSGVRVDGD----TLGFPPLTTEHSGIYVCHVSNEFSSRDSQVT 329
Cdd:smart00410   3 SVTVKEGesVTLSCEASGSPPPEVTWYKQGGKLlaeSGRFSVSRSgstsTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                   ...
gi 767910535   330 VDV 332
Cdd:smart00410  83 LTV 85

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 767910535 247 EASVRGLEDQnlWHIGREGAMLKCLSEGQP-PPSYNWTRLDGPLPSGVRVDGDTLGFPPLTTEHSGIYVCHVSNEFSSRD 325
Cdd:cd20930    2 EVSISGYDDN--WYLGRNEATLTCDVRSNPePTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGR 79

                 ....*..
gi 767910535 326 SQVTVDV 332
Cdd:cd20930   80 AEQTIFV 86

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. 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. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. 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 hemolymph protein hemolin, 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767910535 264 EGAMLKCLSEGQPPPSYNWTRLDGPLPSG-----VRVDGDTLGFPPLTTEHSGIYVCHVSNEFSSRDSQ 327
Cdd:cd20970   18 ENATFMCRAEGSPEPEISWTRNGNLIIEFntryiVRENGTTLTIRNIRRSDMGIYLCIASNGVPGSVEK 86

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
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767910535 270 CLSEGQPPPSYNWTRLDGPLPSG--VRVDGDTLGFPPLTTEHSGIYVCHVSNEFSS 323
Cdd:cd05728   21 CKASGNPRPAYRWLKNGQPLASEnrIEVEAGDLRITKLSLSDSGMYQCVAENKHGT 76

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 767910535 253 LEDQNLwhigregaMLKCLSEGQPPPSYNWTRLDGPLPSGvrvdgDTLGFPPLTTEHSGIYVCHVSNEFSSRD-SQVTV 330
Cdd:cd20948    8 LSGENL--------NLSCHAASNPPAQYSWTINGTFQTSS-----QELFLPAITENNEGTYTCSAHNSLTGKNiSLVLS 73

Immunoglobulin I-set domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767910535  264 EGAMLKCLSEGQPPPSYNWTRLDGPLPSGVRV------DGDTLGFPPLTTEHSGIYVCHVSNEFSSRDSQVTVDV 332
Cdd:pfam07679  16 ESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFkvtyegGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767910535 268 LKCLSEGQPPPSYNWTrLDG-PLPSGVRV--------DGDTLGFPPLT---TEHSGIYVCHVSNE 320
Cdd:cd20956   21 LKCVASGNPLPQITWT-LDGfPIPESPRFrvgdyvtsDGDVVSYVNISsvrVEDGGEYTCTATND 84

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910535    37 SDVVTVVLGQDAKLPCFYRGDSgeqVGQVAWARvdagegaQELALLHSKYGLHVSpayegrveqppppRNPLDGSVLLRN 116
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSP---PPEVTWYK-------QGGKLLAESGRFSVS-------------RSGSTSTLTISN 57

                           90       100
                   ....*....|....*....|....*....
gi 767910535   117 AVQADEGEYECRVsTFPAGSFQARLRLRV 145
Cdd:smart00410  58 VTPEDSGTYTCAA-TNSSGSASSGTTLTV 85

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 767910535 163 QGLTLAASCTAEGS-PAPSVTW---DTEVKGTTSSRSFkHSRSAAVTSEFHLVPSRSMNGQPLTCVVSHPGL--LQDQR 235
Cdd:cd05883   18 EGEEIELNCTAMASkPAATIRWfkgNKELTGKSEVEEW-YSRMFTVTSQLMLKVTKEDDGVPVICLVDHPAVkdLQTQR 95

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
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767910535 276 PPPSYNWTRLDGPLPSGVRVDGDTLGFPPLTTEHSGIYVCHVSNEFSSRDSQVTV 330
Cdd:cd05754   30 PAYTLVWTRVNGTLPSRAMDFNGILTIRNVQLSDAGTYVCTGSNMLDTDEATATL 84

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767910535 263 REGAMLKCLSEGQPPPSYNWTR-------LDGPLPSgVRVDGDTL------GFPpltTEHSGIYVCHVSNEF 321
Cdd:cd05733   16 RDNITIKCEAKGNPQPTFRWTKdgkffdpAKDPRVS-MRRRSGTLvidnhnGGP---EDYQGEYQCYASNEL 83

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 767910535  38 DVVTVVLGQDAKLPCFYRGDSGEQVGQVA--WARVDAGEGAQELALLHSKyGLHVSPAYEGRVEQPPPPRNPLDGSVLLR 115
Cdd:cd20934    5 DPVVALVGTDATLRCSFSPEPGFSLAQLSvfWQLTDTKQLVHSFTESQDQ-GRDQGSAYANRTALFPDLLAQGNASLRLQ 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 767910535 116 NAVQADEGEYECRVSTFPAGSfqARLRLRVLVP 148
Cdd:cd20934   84 RVRVADEGSYTCFVSVQDFGS--AAVSLQVAAP 114

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 767910535 268 LKCLSEGQPPPSYNWTRLDGPLPSG-----VRVDGDTLGFPPLTTEHSGIYVCHVSNEFSSRDSQ 327
Cdd:cd05760   21 LRCHIDGHPRPTYQWFRDGTPLSDGqgnysVSSKERTLTLRSAGPDDSGLYYCCAHNAFGSVCSS 85

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. 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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767910535 250 VRGLEDQNLwhigregaMLKCLSEGQPPPSYNWTRLDGPLPSG--VRVDGDTLGFPPLTTEHSGIYVCHVSN 319
Cdd:cd05851   11 TYALKGQNV--------TLECFALGNPVPVIRWRKILEPMPATaeISMSGAVLKIFNIQPEDEGTYECEAEN 74

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910535  44 LGQDAKLPC-FYR----GDSGEQVGQVAWARVDAGEGA-QELALLHSKYG-LHVSPAYEGRVEQPPPPRNPLDGSVLLRN 116
Cdd:cd05714   11 LGGNVTLPCkFYRdptaFGSGIHKIRIKWTKLTSDSGYlKEVDVLVAMGNvVYHKKTYGGRVSVPLKPGSDSDASLVITD 90

                         90
                 ....*....|...
gi 767910535 117 AVQADEGEYECRV 129
Cdd:cd05714   91 LTASDYGLYRCEV 103

Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-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
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910535 263 REGAMLKCLSEGQPPPSYNWTRldgplpSGVRVDGDTlgfPPLTT--EHSGIYVCHVSNE 320
Cdd:cd05874   16 RENIVIQCEAKGKPPPSFSWTR------NGTHFDIDK---DPKVTmkPNTGTLVINIMNG 66

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910535  43 VLGQDAKLPCFYR-GDSGEQVGQVAWARVDAgEGAQELALLHSkyGLHV----SPAYEGRVEQPPPPRNPlDGSVLLRNA 117
Cdd:cd20960   13 VAGENVTLPCHHQlGLEDQGTLDIEWLLLPS-DKVEKVVITYS--GDRVynhyYPALKGRVAFTSNDLSG-DASLNISNL 88

                         90
                 ....*....|....*.
gi 767910535 118 VQADEGEYECRVSTFP 133
Cdd:cd20960   89 KLSDTGTYQCKVKKAP 104

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 767910535  42 VVLGQDAKLPCFYRGDSGEQVG---------QVAWARVDAGegaQELALLHSKYG-LHVSPAYEGRVEQPPPPRNPLDGS 111
Cdd:cd05900    9 VVLGSSLLIPCYFQDPIAKDPGaptvaplspRIKWSFISKE---KESVLLVATEGkVRVNTEYLDRVSLPNYPAIPSDAT 85

                         90
                 ....*....|....*...
gi 767910535 112 VLLRNAVQADEGEYECRV 129
Cdd:cd05900   86 LEITELRSNDSGTYRCEV 103