Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530364103  207 RPILMLRAPRAQAAVEDVLELHCEALRGSPPILYWfYHEDITLGSRSAPSGGGASFNLSL-----TEEHSGNYSCEANN 280
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITW-YKNGEPISSGSTRSRSLSGSNSTLtisnvTRSDAGTYTCVASN 78

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530364103  114 SLETQPPGGQVMEGDRLVLICSVAmGTGDITFLWYKG---AVGLNLQSKTQRSLTAEYEIPSVRESDAEQYYCVAEN 187
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEAT-GSPPPTITWYKNgepISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364103 225 LELHCEALRGSPPILYWFY-HEDITLGSRSAPSGGGASFNL---SLTEEHSGNYSCEANNGLGAQRSEAV 290
Cdd:cd00096    1 VTLTCSASGNPPPTITWYKnGKPLPPSSRDSRRSELGNGTLtisNVTLEDSGTYTCVASNSAGGSASASV 70

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530364103   19 LFLIASPSHPTEGSPVTLTCKMPflqsSDAQFQFCFFRDTRALgpgwSSSPKLQIAAMWKEDTGSYWCEAQ 89
Cdd:pfam13895   2 PVLTPSPTVVTEGEPVTLTCSAP----GNPPPSYTWYKDGSAI----SSSPNFFTLSVSAEDSGTYTCVAR 64

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530364103  114 SLETQPPGGQVMEGDRLVLICSVAmGTGDITFLWYKG---AVGLNLQSKTQRSLTAEYEIPSVRESDAEQYYCVAEN 187
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEAT-GSPPPTITWYKNgepISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364103  115 LETQPPGGQVMEGDRLVLICSvAMGTGDITFLWYKGAvglNLQSKTQRSLtaeyeIPSVRESDAEQYYCVAENGYGPSPS 194
Cdd:pfam13895   2 PVLTPSPTVVTEGEPVTLTCS-APGNPPPSYTWYKDG---SAISSSPNFF-----TLSVSAEDSGTYTCVARNGRGGKVS 72

                  ....*..
gi 530364103  195 GLVSITV 201
Cdd:pfam13895  73 NPVELTV 79

Immunoglobulin I-set domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530364103  116 ETQPPGGQVMEGDRLVLICSVaMGTGDITFLWYKGAVGLNLQSK---TQRSLTAEYEIPSVRESDAEQYYCVAENGYG 190
Cdd:pfam07679   4 TQKPKDVEVQEGESARFTCTV-TGTPDPEVSWFKDGQPLRSSDRfkvTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364103   215 PRAQAAVE-DVLELHCEALRGSPPILYWF--YHEDITLGSRSAPSGGGASFNL---SLTEEHSGNYSCEANNGLGAQRSE 288
Cdd:smart00410   1 PPSVTVKEgESVTLSCEASGSPPPEVTWYkqGGKLLAESGRFSVSRSGSTSTLtisNVTPEDSGTYTCAATNSSGSASSG 80

                   .
gi 530364103   289 A 289
Cdd:smart00410  81 T 81

C17orf99 Ig domain; This Ig domain is found in tandem in the uncharacterized human protein C17orf99, which is found across mammalian species.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530364103  226 ELHCEALRGSPPILYWFYHED-ITLGSRSAPSGGGASFNLSLTEEHSG---NYSCEANNGLGAQRSEAV 290
Cdd:pfam17736  20 LISCHASQGSPPITYSLVGSDgIVVAKKIPLHGEPANFSLNITLKSSPdllTYQCQAANTSGTQVSSLR 88

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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530364103 127 GDRLVLICSVAMGTGDITFLWYKGAVGLNLQSKTQRSL----------TAEYEIPSVRESDAEQYYCVAENGYGP 191
Cdd:cd20950   12 GNRAVLTCSEPDGSPPSEYTWFKDGVVMPTNPKSTRAFsnssysldptTGELVFDPLSASDTGEYSCEARNGYGT 86

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 530364103 130 LVLICSVAmGTGDITFLWYKGAVGLNLQSKTQRSL---TAEYEIPSVRESDAEQYYCVAENGYG 190
Cdd:cd00096    1 VTLTCSAS-GNPPPTITWYKNGKPLPPSSRDSRRSelgNGTLTISNVTLEDSGTYTCVASNSAG 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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530364103 227 LHCEALRGSPPILYWFYHEDITLGSRSAPSGGGASFNLSLTEE------------HSGNYSCEANNGLG-AQRSEAVTL 292
Cdd:cd20950   17 LTCSEPDGSPPSEYTWFKDGVVMPTNPKSTRAFSNSSYSLDPTtgelvfdplsasDTGEYSCEARNGYGtPMRSNAVRM 95

Immunoglobulin-like Ig0 domain of basigin-1 (BSG1) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of the collagenase stimulatory factor, basigin-1 (BSG1; also known as Cluster of Differentiation 147 (CD147) and Extracellular Matrix Metalloproteinase Inducer (EMMPRIN)) and similar proteins. CD147 is a transmembrane glycoprotein that belongs to the immunoglobulin superfamily. It is expressed in nearly all cells including platelets and fibroblasts and is involved in inflammatory diseases, and cancer progression. CD147 is highly expressed in several cancers and used as a prognostic marker. The two primary isoforms of CD147 that are related to cancer progression have been identified: CD147 Ig1-Ig2 (also called Basigin-2) that is ubiquitously expressed in most tissues and CD147 Ig0-Ig1-Ig2 (also called Basigin-1) that is retinal specific and implicated in retinoblastoma. Studies showed that CD147 Ig0 domain is a potent stimulator of interleukin-6 and suggest that the CD147 Ig0 dimer is the functional unit required for activity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364103 212 LRAPRAQAA-VEDVLELHCEALrGSP-PILYWFYHE----DITL----GSRSAPSGGGASFNL---------SLTEEHSG 272
Cdd:cd20940    4 IKSPLSQQRlVGDSVELHCEAV-GSPiPEIQWWFEGqepnEICSqlwdGARLDRVHINATYHQhatstisidNLTEEDTG 82

                 ....*...
gi 530364103 273 NYSCEANN 280
Cdd:cd20940   83 TYECRASN 90

First immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The first Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set 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, including vascular (VCAM), intercellular (ICAM), neural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules, as well as junction adhesion molecules (JAM).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364103 115 LETQPPGGQVMEGDRLVLICSVAMGTGDITFLWYKGAVGLNLQSK--TQRSLTAEYEIPSVRESDAEQYYCVAENGYGPS 192
Cdd:cd20979    3 LKEQPAEVLFREGQPTVLECVTEGGDQGVKYSWLKDGKSFNWQEHnvAQRKDEGSLVFLKPQASDEGQYQCFAETPAGVA 82

                 ....*.
gi 530364103 193 PSGLVS 198
Cdd:cd20979   83 SSRVIS 88

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the 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 (Slit-1,Slit-2, Slit-3), 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 Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 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 Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530364103 118 QPPGGQVMEGDRLVLICSVAMGTGDITFLWYKGAVGLNLQSKTQRSLT-AEYEIPSVRESDAEQYYCVAENGYG 190
Cdd:cd05724    3 EPSDTQVAVGEMAVLECSPPRGHPEPTVSWRKDGQPLNLDNERVRIVDdGNLLIAEARKSDEGTYKCVATNMVG 76