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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364105   119 PPGGQVMEGDRLVLICSVAmGTGDITFLWYKGAVGLNLQSK----TQRSLTAEYEIPSVRESDAEQYYCVAENGYGpSPS 194
Cdd:smart00410   1 PPSVTVKEGESVTLSCEAS-GSPPPEVTWYKQGGKLLAESGrfsvSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SAS 78

                   ....*..
gi 530364105   195 GLVSITV 201
Cdd:smart00410  79 SGTTLTV 85

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530364105   19 LFLIASPSHPTEGSPVTLTCKMPflqsSDAQFQFCFFRDTRALgpgwSSSPKLQIAAMWKEDTGSYWCEAQ 89
Cdd:pfam13895   2 PVLTPSPTVVTEGEPVTLTCSAP----GNPPPSYTWYKDGSAI----SSSPNFFTLSVSAEDSGTYTCVAR 64

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364105   119 PPGGQVMEGDRLVLICSVAmGTGDITFLWYKGAVGLNLQSK----TQRSLTAEYEIPSVRESDAEQYYCVAENGYGpSPS 194
Cdd:smart00410   1 PPSVTVKEGESVTLSCEAS-GSPPPEVTWYKQGGKLLAESGrfsvSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SAS 78

                   ....*..
gi 530364105   195 GLVSITV 201
Cdd:smart00410  79 SGTTLTV 85

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530364105  207 RPILMLRAPRAQAAVEDVLELHCEALRGSPPILYWfYHEDITLGSRSAPSGGGASFNLSL-----TEEHSGNYSCEANN 280
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITW-YKNGEPISSGSTRSRSLSGSNSTLtisnvTRSDAGTYTCVASN 78

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364105   215 PRAQAAVE-DVLELHCEALRGSPPILYWF--YHEDITLGSRSAPSGGGASFNL---SLTEEHSGNYSCEANNGLGAQRSE 288
Cdd:smart00410   1 PPSVTVKEgESVTLSCEASGSPPPEVTWYkqGGKLLAESGRFSVSRSGSTSTLtisNVTPEDSGTYTCAATNSSGSASSG 80

                   .
gi 530364105   289 A 289
Cdd:smart00410  81 T 81

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 530364105 127 GDRLVLICSVAMGTGDITFLWYKGAVGLNLQSKTQRSL----------TAEYEIPSVRESDAEQYYCVAENGYGP 191
Cdd:cd20950   12 GNRAVLTCSEPDGSPPSEYTWFKDGVVMPTNPKSTRAFsnssysldptTGELVFDPLSASDTGEYSCEARNGYGT 86

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364105   119 PPGGQVMEGDRLVLICSVAmGTGDITFLWYKGAVGLNLQSK----TQRSLTAEYEIPSVRESDAEQYYCVAENGYGpSPS 194
Cdd:smart00410   1 PPSVTVKEGESVTLSCEAS-GSPPPEVTWYKQGGKLLAESGrfsvSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SAS 78

                   ....*..
gi 530364105   195 GLVSITV 201
Cdd:smart00410  79 SGTTLTV 85

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530364105  207 RPILMLRAPRAQAAVEDVLELHCEALRGSPPILYWfYHEDITLGSRSAPSGGGASFNLSL-----TEEHSGNYSCEANN 280
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITW-YKNGEPISSGSTRSRSLSGSNSTLtisnvTRSDAGTYTCVASN 78

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364105  119 PPGGQVMEGDRLVLICSVAMGTGDITFLWYKGAVGLNLQSKTQ----RSLTAEYEIPSVRESDAEQYYCVAENGYGPSPS 194
Cdd:pfam00047   3 PPTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVKhdngRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATL 82

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 530364105 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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364105  210 LMLRAPRAQAAVEDVLELHCEALrGSPPILYWFYHEDitlgsrSAPSGGGASFNLSLTEEHSGNYSCEANNGLGAQRSEA 289
Cdd:pfam13895   2 PVLTPSPTVVTEGEPVTLTCSAP-GNPPPSYTWYKDG------SAISSSPNFFTLSVSAEDSGTYTCVARNGRGGKVSNP 74

                  ....
gi 530364105  290 VTLN 293
Cdd:pfam13895  75 VELT 78

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530364105   19 LFLIASPSHPTEGSPVTLTCKMPflqsSDAQFQFCFFRDTRALgpgwSSSPKLQIAAMWKEDTGSYWCEAQ 89
Cdd:pfam13895   2 PVLTPSPTVVTEGEPVTLTCSAP----GNPPPSYTWYKDGSAI----SSSPNFFTLSVSAEDSGTYTCVAR 64

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 530364105 130 LVLICSVAmGTGDITFLWYKGAVGLNLQSKTQRSL---TAEYEIPSVRESDAEQYYCVAENGYG 190
Cdd:cd00096    1 VTLTCSAS-GNPPPTITWYKNGKPLPPSSRDSRRSelgNGTLTISNVTLEDSGTYTCVASNSAG 63

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364105 124 VMEGDRLVLICSVAMGTGDITFLWYKGAVGLN--------LQSKTQRSltaEYEIPSVRESDAEQYYCVAENGYGpSPSG 195
Cdd:cd05750   11 VQEGSKLVLKCEATSENPSPRYRWFKDGKELNrkrpknikIRNKKKNS---ELQINKAKLEDSGEYTCVVENILG-KDTV 86

                 ....*.
gi 530364105 196 LVSITV 201
Cdd:cd05750   87 TGNVTV 92

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530364105  225 LELHCEALRGSP-PILYWF----YHEDITLGSRSAPSGGGASFNLS-LTEEHSGNYSCEANNGLG 283
Cdd:pfam00047  14 ATLTCSASTGSPgPDVTWSkeggTLIESLKVKHDNGRTTQSSLLISnVTKEDAGTYTCVVNNPGG 78

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. 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 this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364105 114 SLETQPPGGQVMEGDRLVLICSVAmGTGDITFLWYKGAVGLNLQSK--TQRSLTAEYEIPSVRESDAEQYYCVAENGygp 191
Cdd:cd20976    3 SFSSVPKDLEAVEGQDFVAQCSAR-GKPVPRITWIRNAQPLQYAADrsTCEAGVGELHIQDVLPEDHGTYTCLAKNA--- 78

                         90
                 ....*....|....
gi 530364105 192 spSGLVSITVRIPV 205
Cdd:cd20976   79 --AGQVSCSAWVTV 90

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364105 218 QAAVEDVLELHCEALRGSP-PILYWfYHEDITL---GSRSAPSGGGasfNLSLTE---EHSGNYSCEANNGLGAQRSEAV 290
Cdd:cd05724    8 QVAVGEMAVLECSPPRGHPePTVSW-RKDGQPLnldNERVRIVDDG---NLLIAEarkSDEGTYKCVATNMVGERESRAA 83

                 ..
gi 530364105 291 TL 292
Cdd:cd05724   84 RL 85