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
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907201124 142 PVCRIPAAVPVGKTATLQCQESEGYPRPHYSWYRNDVPLPTDSRANPRFQNSSFHVNSETGTL 204
Cdd:cd20950     1 PTVNIPSSATIGNRAVLTCSEPDGSPPSEYTWFKDGVVMPTNPKSTRAFSNSSYSLDPTTGEL 63

Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF domains; The members here are composed of the second Ig-like domain of Junctional adhesion molecule-1 (JAM1). JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. 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 second Ig-like domain of JAM1 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, the A strand of the I-set is discontinuous but lacks 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907201124 142 PVCRIPAAVPVGKTATLQCQESEGYPRPHYSWYRNDVPLPTDSRANPRFQNSSFHVNSETGTL 204
Cdd:cd20950     1 PTVNIPSSATIGNRAVLTCSEPDGSPPSEYTWFKDGVVMPTNPKSTRAFSNSSYSLDPTTGEL 63

Immunoglobulin I-set domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907201124  39 RNPVVHEFESVELSCIITDsqTSDPRIEWKKiqDGQttyvyfdnKIQGDLAGRTDVFGKT-SLRIWNVTRSDSAIYRCev 117
Cdd:pfam07679   8 KDVEVQEGESARFTCTVTG--TPDPEVSWFK--DGQ--------PLRSSDRFKVTYEGGTyTLTISNVQPDDSGKYTC-- 73

                          90
                  ....*....|....*...
gi 1907201124 118 VALNDRKEvDEITIELIV 135
Cdd:pfam07679  74 VATNSAGE-AEASAELTV 90

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

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1907201124  150 VPVGKTATLQCqESEGYPRPHYSWYRND-VPLPTDSRANPRFQNSSFH 196
Cdd:smart00410   6 VKEGESVTLSC-EASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTST 52

Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF domains; The members here are composed of the second Ig-like domain of Junctional adhesion molecule-1 (JAM1). JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. 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 second Ig-like domain of JAM1 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, the A strand of the I-set is discontinuous but lacks 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907201124 142 PVCRIPAAVPVGKTATLQCQESEGYPRPHYSWYRNDVPLPTDSRANPRFQNSSFHVNSETGTL 204
Cdd:cd20950     1 PTVNIPSSATIGNRAVLTCSEPDGSPPSEYTWFKDGVVMPTNPKSTRAFSNSSYSLDPTTGEL 63

Immunoglobulin I-set domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907201124  39 RNPVVHEFESVELSCIITDsqTSDPRIEWKKiqDGQttyvyfdnKIQGDLAGRTDVFGKT-SLRIWNVTRSDSAIYRCev 117
Cdd:pfam07679   8 KDVEVQEGESARFTCTVTG--TPDPEVSWFK--DGQ--------PLRSSDRFKVTYEGGTyTLTISNVQPDDSGKYTC-- 73

                          90
                  ....*....|....*...
gi 1907201124 118 VALNDRKEvDEITIELIV 135
Cdd:pfam07679  74 VATNSAGE-AEASAELTV 90

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907201124  34 LKSSNRNPVVHEFESVELSCIITDSQTsdPRIEWKKiqDGQTTyvyfdnkIQGDLAGRTDVFGKTSLRIWNVTRSDSAIY 113
Cdd:pfam13927   4 ITVSPSSVTVREGETVTLTCEATGSPP--PTITWYK--NGEPI-------SSGSTRSRSLSGSNSTLTISNVTRSDAGTY 72

                  ....
gi 1907201124 114 RCEV 117
Cdd:pfam13927  73 TCVA 76

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third 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, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907201124  47 ESVELSCIITDSQTsdPRIEWkkiqdgqttyvyfdNKIQGDL-AGRT--DVFGKTsLRIWNVTRSDSAIYRC 115
Cdd:cd05731    11 GVLLLECIAEGLPT--PDIRW--------------IKLGGELpKGRTkfENFNKT-LKIENVSEADSGEYQC 65

Immunoglobulin I-set domain;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907201124 147 PAAVPVGKTATLQCQESeGYPRPHYSWYRNDVPLPTDSRAnprfqnsSFHVNSETGTLMI 206
Cdd:pfam07679   9 DVEVQEGESARFTCTVT-GTPDPEVSWFKDGQPLRSSDRF-------KVTYEGGTYTLTI 60

Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H4 (also known as B7-S1, B7x, or Vtcn1). B7-H4 is one of the B7 family of immune-regulatory ligands that act as negative regulators of T cell function; it contains one IgV domain and one IgC domain. The B7-family consists of structurally related cell-surface protein ligands, which bind to receptors on lymphocytes that regulate immune responses. The binding of B7-H4 to unidentified receptors results in the inhibition of TCR-mediated T cell proliferation, cell-cycle progression and IL-2 production. As a co-inhibitory molecule, B7-H4 is widely expressed in tumor tissues and its expression is significantly associated with poor prognosis in human cancers such as glioma, pancreatic cancer, oral squamous cell carcinoma, renal cell carcinoma, and lung cancer.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907201124  32 VNLKSSnrnpVVHEFESVELSCIIT-DSQTSDPRIEWKKIQDGQTTYVYFDNKIQ-----GDLAGRTDVF------GKTS 99
Cdd:cd20984     2 VTAKHL----AGNIGEDGILSCTFTpDIKLSDIVIQWLKEGDSGLVHEFKEGKDElsrqsPMFRGRTSLFadqvhvGNAS 77

                          90
                  ....*....|....*...
gi 1907201124 100 LRIWNVTRSDSAIYRCEV 117
Cdd:cd20984    78 LRLKNVQLTDAGTYLCII 95

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.

                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907201124 150 VPVGKTATLQCQeSEGYPRPHYSWYRNDVPLPTD 183
Cdd:cd07693    12 VSKGDPATLNCK-AEGRPTPTIQWLKNGQPLETD 44

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

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1907201124  150 VPVGKTATLQCqESEGYPRPHYSWYRND-VPLPTDSRANPRFQNSSFH 196
Cdd:smart00410   6 VKEGESVTLSC-EASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTST 52

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
                  ....*....|....*....|....*....|....*....|.
gi 1907201124 156 ATLQCqESEGYPRPHYSWYRNDVPLPTDSRANPRFQNSSFH 196
Cdd:cd00096     1 VTLTC-SASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGT 40

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the gamma chain of gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigens as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain the standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907201124  47 ESVELSCIITDSQTSDPRIEWKKIQDGQ-----------TTYVYFDNKIQGDLAGRTDVFGKTS-LRIWNVTRSDSAIYR 114
Cdd:cd04982    14 KSVTISCKVSGIDFSTTYIHWYRQKPGQalerllyvsstSAVRKDSGKTKNKFEARKDVGKSTStLTITNLEKEDSATYY 93

                  .
gi 1907201124 115 C 115
Cdd:cd04982    94 C 94

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 1907201124  44 HEFESVELSCIIT-----DSQTSD-PRIEWKKIQDGQ------TTYVYFDN--KIQGDLAGRTDVF------GKTSLRIW 103
Cdd:cd05714    10 HLGGNVTLPCKFYrdptaFGSGIHkIRIKWTKLTSDSgylkevDVLVAMGNvvYHKKTYGGRVSVPlkpgsdSDASLVIT 89

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907201124 104 NVTRSDSAIYRCEVV-ALNDRKEVDEITIELIV 135
Cdd:cd05714    90 DLTASDYGLYRCEVIeGIEDDQDVVALDVQGVV 122

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
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907201124 147 PAAVPVGKTATLQCQESEGYPRPHYSWYRNDVPLPTDSRANPRFQ---NSSFHVNSET 201
Cdd:pfam00047   5 TVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVKHDNGrttQSSLLISNVT 62

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. 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 Ig I1 domain of the titin I-band 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. 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 1907201124 147 PAAVPVGKTATLQCqESEGYPRPHYSWYRNDVPLptDSRANPRfqNSSFHVNSETGTLMI 206
Cdd:cd20951     9 SHTVWEKSDAKLRV-EVQGKPDPEVKWYKNGVPI--DPSSIPG--KYKIESEYGVHVLHI 63

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third 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. 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, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907201124 150 VPVGKTATLQCQESeGYPRPHYSWYRNDVPLPTDSR 185
Cdd:cd20957    13 VDFGRTAVFNCSVT-GNPIHTVLWMKDGKPLGHSSR 47

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907201124  64 RIEWKKIQD-------GQTTYVYFDN---KIQGDLAGRTDV------FGKTSLRIWNVTRSDSAIYRCEVV 118
Cdd:cd05901    39 RIKWTKIQVdkngkdhKETTVLVAQNgiiKIGQEYMGRVSVpshpedQGDASLTIVKLRASDAGVYRCEVM 109

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 1907201124  36 SSNRNPVV-HEFESVELSCII-TDSQTSDP---RIEWKKIQDGQTTYVY------FDNKIQGDLAGRTDVFGKT----SL 100
Cdd:cd05877     1 ETVQAKVFsHRGGNVTLPCRYhYEPELSAPrkiRVKWTKLEVDYAKEEDvlvaigTRHKSYGSYQGRVFLRRADdldaSL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907201124 101 RIWNVTRSDSAIYRCEVV-ALNDRKEVDEITIELIVQ 136
Cdd:cd05877    81 VITDLRLEDYGRYRCEVIdGLEDESVVVALRLRGVVF 117

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 1907201124  47 ESVELSCIITDSQTS-DPRIEWKKIQDGQTTYVYFDNKIQGDL-----AGRTDVF------GKTSLRIWNVTRSDSAIYR 114
Cdd:cd05713    16 EDAELPCHLSPKMSAeHMEVRWFRSQFSPVVHLYRDGQDQEEEqmpeyRGRTELLkdaiaeGSVALRIHNVRPSDEGQYT 95

                          90       100
                  ....*....|....*....|.
gi 1907201124 115 CEVvalNDRKEVDEITIELIV 135
Cdd:cd05713    96 CFF---RSGSFYEEATLELKV 113