Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804476980  31 FAVLGPPGPILAMVGEDADLPCHLVPTMSAETMELRWVSSSLRQVVSVYADGKEVEDRQSAEYRGRTSILQDGIAAGKAA 110
Cdd:cd05713     1 FSVIGPTEPILALVGEDAELPCHLSPKMSAEHMEVRWFRSQFSPVVHLYRDGQDQEEEQMPEYRGRTELLKDAIAEGSVA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1804476980 111 LRIHNVTASDSGKY*CYFQDGDFCEKALVELKVA 144
Cdd:cd05713    81 LRIHNVRPSDEGQYTCFFRSGSFYEEATLELKVA 114

Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804476980  31 FAVLGPPGPILAMVGEDADLPCHLVPTMSAETMELRWVSSSLRQVVSVYADGKEVEDRQSAEYRGRTSILQDGIAAGKAA 110
Cdd:cd05713     1 FSVIGPTEPILALVGEDAELPCHLSPKMSAEHMEVRWFRSQFSPVVHLYRDGQDQEEEQMPEYRGRTELLKDAIAEGSVA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1804476980 111 LRIHNVTASDSGKY*CYFQDGDFCEKALVELKVA 144
Cdd:cd05713    81 LRIHNVRPSDEGQYTCFFRSGSFYEEATLELKVA 114

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804476980   37 PGPILAMVGEDADLPCHlvptmsaetmelrwVSSSLRQVVSVYADGKEVedrqsAEYRGRTSILQDGiaaGKAALRIHNV 116
Cdd:smart00410   1 PPSVTVKEGESVTLSCE--------------ASGSPPPEVTWYKQGGKL-----LAESGRFSVSRSG---STSTLTISNV 58

                           90       100
                   ....*....|....*....|....*..
gi 1804476980  117 TASDSGKY*CYFQDGDFCEKALVELKV 143
Cdd:smart00410  59 TPEDSGTYTCAATNSSGSASSGTTLTV 85

Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804476980  31 FAVLGPPGPILAMVGEDADLPCHLVPTMSAETMELRWVSSSLRQVVSVYADGKEVEDRQSAEYRGRTSILQDGIAAGKAA 110
Cdd:cd05713     1 FSVIGPTEPILALVGEDAELPCHLSPKMSAEHMEVRWFRSQFSPVVHLYRDGQDQEEEQMPEYRGRTELLKDAIAEGSVA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1804476980 111 LRIHNVTASDSGKY*CYFQDGDFCEKALVELKVA 144
Cdd:cd05713    81 LRIHNVRPSDEGQYTCFFRSGSFYEEATLELKVA 114

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 1804476980  36 PPGPILAMVGEDADLPCHL--VPTMSAETMELRWVSSSLRQVVSVYADGKEVEDRQSAEYRGRTSILQDGIAAGKAALRI 113
Cdd:cd20934     3 PEDPVVALVGTDATLRCSFspEPGFSLAQLSVFWQLTDTKQLVHSFTESQDQGRDQGSAYANRTALFPDLLAQGNASLRL 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1804476980 114 HNVTASDSGKY*CYFQDGDFcEKALVELKVA 144
Cdd:cd20934    83 QRVRVADEGSYTCFVSVQDF-GSAAVSLQVA 112

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 1804476980  36 PPGPILAMVGEDADLPCHLVPTMSAETMELRWV----SSSLRQVVSVYADGKEVEdrqsaEYRGRTSILQDgIAAGKAAL 111
Cdd:pfam07686   2 TPREVTVALGGSVTLPCTYSSSMSEASTSVYWYrqppGKGPTFLIAYYSNGSEEG-----VKKGRFSGRGD-PSNGDGSL 75

                          90
                  ....*....|....*
gi 1804476980 112 RIHNVTASDSGKY*C 126
Cdd:pfam07686  76 TIQNLTLSDSGTYTC 90

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 1804476980  36 PPGPILAMVGEDADLPCHLV--PTMSAET-MELRWV---SSSLRQVVSVYADGKEveDRQSAEYRGRTSILQDGiaAGKA 109
Cdd:cd05877     3 VQAKVFSHRGGNVTLPCRYHyePELSAPRkIRVKWTkleVDYAKEEDVLVAIGTR--HKSYGSYQGRVFLRRAD--DLDA 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1804476980 110 ALRIHNVTASDSGKY*CYFQDGDFCEKALVELKVAG 145
Cdd:cd05877    79 SLVITDLRLEDYGRYRCEVIDGLEDESVVVALRLRG 114

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 1804476980  38 GPILAMVGEDADLPCH--LVPTMSAETME---LRW----VSSSLRQVVSVY-ADGKEVEDRQSaeYRGRTSILQDGIAAG 107
Cdd:cd05714     5 AKVFSHLGGNVTLPCKfyRDPTAFGSGIHkirIKWtkltSDSGYLKEVDVLvAMGNVVYHKKT--YGGRVSVPLKPGSDS 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1804476980 108 KAALRIHNVTASDSGKY*CYFQDGDFCEKALVELKVAG 145
Cdd:cd05714    83 DASLVITDLTASDYGLYRCEVIEGIEDDQDVVALDVQG 120

Immunoglobulin I-set domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804476980  33 VLGPPGPILAMVGEDADLPCHlvpTMSAETMELRWvssslrqvvsvYADGKEVedRQSAEYRgrtsILQDGiaaGKAALR 112
Cdd:pfam07679   3 FTQKPKDVEVQEGESARFTCT---VTGTPDPEVSW-----------FKDGQPL--RSSDRFK----VTYEG---GTYTLT 59

                          90
                  ....*....|....
gi 1804476980 113 IHNVTASDSGKY*C 126
Cdd:pfam07679  60 ISNVQPDDSGKYTC 73

Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 86). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. The CTLA-4 and B7-2 monomers are both two-layer beta-sandwiches that display the chain topology characteristic of the immunoglobulin variable (V-type) domains present in antigen receptors. The front and back sheets of B7-2 are composed of AGFCC'C" and BED strands, respectively. Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804476980  40 ILAMVGEDADLPCHL--VPTMSAETMELRWVSSSLRQVVSVYAdGKEVEDRQSAEYRGRTSILQDgiaagKAALRIHNVT 117
Cdd:cd16087     3 IQAYFNETAYLPCQFknPQNISLSELVVFWQDQKKLVLYELYL-GKEKLDNVNSKYIGRTSFDQE-----NWTLQLHNVQ 76

                          90
                  ....*....|..
gi 1804476980 118 ASDSGKY*CYFQ 129
Cdd:cd16087    77 IKDQGTYQCFIH 88

Immunoglobulin Variable (IgV) domain of T cell Immunoglobulin Domain and Mucin Domain 3 (Tim-3), and similar domains; The members here are composed of the immunoglobulin variable (IgV) domain of T cell immunoglobulin domain and mucin domain 3 (Tim-3; also known as Hepatitis A virus cellular receptor 2 (HAVcr-2) and Cluster of Differentiation 366 (CD366)) and similar proteins. TIM-3 is a checkpoint inhibitor in immune responses to tumors, as well as involved in chronic viral infections. Thus, Tim-3 has emerged as one of most promising immune checkpoint targets for cancer immunotherapy. Tim-3 is highly expressed on Th1 lymphocytes and CD11b(+) macrophages and is upregulated on activated T and myeloid cells. TIM-3 regulates macrophage, activation and inhibits Th1 mediated immune responses to promote immunological tolerance. There are three TIM family members in humans (TIM-1, TIM-3, and TIM-4) and eight members in mice (TIM-1 to TIM-8). The IgV domain of human TIM-3 has been shown to bind ligands such as carcinoembryonic antigen cell adhesion molecule 1 (CEACAM1), high mobility group protein B1 (HMGB1)and galectin-9 (GAL9). The binding of GAL9 to TIM-3 can negatively regulate Th1 immune response, enhance immune tolerance and inhibit anti#tumor immunity. Dysregulation of the TIM-3/GAL9 pathway is implicated in numerous chronic autoimmune diseases, such as multiple sclerosis and systemic lupus erythematosus.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804476980  42 AMVGEDADLPCHLVPTMSAETMELRW----VSSSLRQVVSVYADGKEVEDRQSAEYRgrtsiLQDGIAAGKAALRIHNVT 117
Cdd:cd20982     5 AEVGHNAYLPCSYTTAAPGNLVPVCWgkgaCPVSYCGNVLLRTDERDVTYQKSSRYQ-----LKGDFSKGDVSLTIENVT 79

                          90       100
                  ....*....|....*....|....*...
gi 1804476980 118 ASDSGKY*CYFQ-DGDFC-EKALVELKV 143
Cdd:cd20982    80 LADSGIYCCRIQiPGIMNdEKFNLKLVI 107

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804476980  34 LGPPGPILAMVGEDADLPCHL--VPTM------SAETMELRWV-------SSSLRQVVSVYADGKEVEDRQsaEYRGRTS 98
Cdd:cd05901     1 VRKSSRVHGSLSGSVVLPCRFstLPTLppsyniTSEFLRIKWTkiqvdknGKDHKETTVLVAQNGIIKIGQ--EYMGRVS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1804476980  99 ILQDGIAAGKAALRIHNVTASDSGKY*CYFQDGDFCEKALVELKVAG 145
Cdd:cd05901    79 VPSHPEDQGDASLTIVKLRASDAGVYRCEVMHGIEDTQDTVSLDVSG 125

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 1804476980  33 VLGPPgPILAMVGEDADLPCHL-VPTMSAETMELRWVSSSLRQVVSVY-----ADGKE------VEDRQSAEYRgrtsil 100
Cdd:cd20989     3 VQVPP-EVRGFLGGSVTLPCHLlPPNMVTHVSQVTWQRHDEHGSVAVFhpkqgPSFPEserlsfVAARLGAELR------ 75

                          90       100
                  ....*....|....*....|....*...
gi 1804476980 101 qdgiaagKAALRIHNVTASDSGKY*CYF 128
Cdd:cd20989    76 -------NASLAMFGLRVEDEGNYTCEF 96

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 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" strands in the other.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804476980  36 PPGPILAMVGEDADLPCHLvpTMSAETMELRWV----SSSLRQVVSVYADGKEVEDRQSAEYRGRTSilqdgiAAGKAAL 111
Cdd:cd00099     4 SPRSLSVQEGESVTLSCEV--SSSFSSTYIYWYrqkpGQGPEFLIYLSSSKGKTKGGVPGRFSGSRD------GTSSFSL 75

                          90
                  ....*....|....*
gi 1804476980 112 RIHNVTASDSGKY*C 126
Cdd:cd00099    76 TISNLQPEDSGTYYC 90

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804476980  36 PPGPILAMVGEDADLPCHlvptmsaetmelrwVSSSLRQVVSVYADGKEVEDrqsaeyrgrTSILQDGIAAGKAALRIHN 115
Cdd:pfam13927   7 SPSSVTVREGETVTLTCE--------------ATGSPPPTITWYKNGEPISS---------GSTRSRSLSGSNSTLTISN 63

                          90
                  ....*....|.
gi 1804476980 116 VTASDSGKY*C 126
Cdd:pfam13927  64 VTRSDAGTYTC 74

IL-1 receptor-like protein; Provisional

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1804476980  88 RQSAEYRGRTSILQDGIAAGKAALRIHNVTASDSGKY*CYFQDGDFCEKALVELKVAGEPLGF 150
Cdd:PHA02826   77 RDSGARTKIKKITHNEIGDRSENLWIGNVINIDEGIYICTISSGNICEESTIRLTFDSGTINY 139