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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800971    24 QNITARIGEPLVLKCKgAPKKPPQRLEWKLNTGrteawKVLSPQGGGpwdSVARVLPNGSLFLPAVGIQDEGIFRCQAMN 103
Cdd:smart00410   2 PSVTVKEGESVTLSCE-ASGSPPPEVTWYKQGG-----KLLAESGRF---SVSRSGSTSTLTISNVTPEDSGTYTCAATN 72

                           90
                   ....*....|....
gi 332800971   104 RNGkETKSNYRVRV 117
Cdd:smart00410  73 SSG-SASSGTTLTV 85

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800971    24 QNITARIGEPLVLKCKgAPKKPPQRLEWKLNTGrteawKVLSPQGGGpwdSVARVLPNGSLFLPAVGIQDEGIFRCQAMN 103
Cdd:smart00410   2 PSVTVKEGESVTLSCE-ASGSPPPEVTWYKQGG-----KLLAESGRF---SVSRSGSTSTLTISNVTPEDSGTYTCAATN 72

                           90
                   ....*....|....
gi 332800971   104 RNGkETKSNYRVRV 117
Cdd:smart00410  73 SSG-SASSGTTLTV 85

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 332800971  239 QLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDGLRTRE 280
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISS 44

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 332800971  34 LVLKCKGAPKKPPQrLEWKLNTgrteawkvlSPQGGGPWDSVARVLPNGSLFLPAVGIQDEGIFRCQAMNRNGKETKSN 112
Cdd:cd00096    1 VTLTCSASGNPPPT-ITWYKNG---------KPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69

Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800971 119 QIPGKPEIVdsaseLTAGVPNKVgTCVSEGSYPAGTLSWHLDGKPLvpnEKGVSVKEQTR-RHPEtglfTLQSELMVTPA 197
Cdd:cd05759    3 VIEGGPVIS-----LQAGVPYNL-TCRARGAKPAAEIIWFRDGEQL---EGAVYSKELLKdGKRE----TTVSTLLITPS 69

                         90
                 ....*....|....*....
gi 332800971 198 RGGDPRpTFSC-SFSPGLP 215
Cdd:cd05759   70 DLDTGR-TFTCrARNEAIP 87

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800971    24 QNITARIGEPLVLKCKgAPKKPPQRLEWKLNTGrteawKVLSPQGGGpwdSVARVLPNGSLFLPAVGIQDEGIFRCQAMN 103
Cdd:smart00410   2 PSVTVKEGESVTLSCE-ASGSPPPEVTWYKQGG-----KLLAESGRF---SVSRSGSTSTLTISNVTPEDSGTYTCAATN 72

                           90
                   ....*....|....
gi 332800971   104 RNGkETKSNYRVRV 117
Cdd:smart00410  73 SSG-SASSGTTLTV 85

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 332800971  239 QLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDGLRTRE 280
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISS 44

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 332800971  34 LVLKCKGAPKKPPQrLEWKLNTgrteawkvlSPQGGGPWDSVARVLPNGSLFLPAVGIQDEGIFRCQAMNRNGKETKSN 112
Cdd:cd00096    1 VTLTCSASGNPPPT-ITWYKNG---------KPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69

Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800971 119 QIPGKPEIVdsaseLTAGVPNKVgTCVSEGSYPAGTLSWHLDGKPLvpnEKGVSVKEQTR-RHPEtglfTLQSELMVTPA 197
Cdd:cd05759    3 VIEGGPVIS-----LQAGVPYNL-TCRARGAKPAAEIIWFRDGEQL---EGAVYSKELLKdGKRE----TTVSTLLITPS 69

                         90
                 ....*....|....*....
gi 332800971 198 RGGDPRpTFSC-SFSPGLP 215
Cdd:cd05759   70 DLDTGR-TFTCrARNEAIP 87

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800971  25 NITARIGEPLVLKCKGAPKKPPQrLEWKLN-TGRTeawkvlSPQgggpwdsvarvlpngSLFLPAVGIQDEGIFRCQAMN 103
Cdd:cd20948    4 DTYYLSGENLNLSCHAASNPPAQ-YSWTINgTFQT------SSQ---------------ELFLPAITENNEGTYTCSAHN 61

                         90
                 ....*....|....*
gi 332800971 104 R-NGKETKSNYRVRV 117
Cdd:cd20948   62 SlTGKNISLVLSVTV 76

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 332800971   21 VGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRteawKVLSPQGGGPWDSVArvlpNGSLFLPAVGIQDEGIFRCQ 100
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGT----LIESLKVKHDNGRTT----QSSLLISNVTKEDAGTYTCV 72

                          90
                  ....*....|.
gi 332800971  101 AMNRNGKETKS 111
Cdd:pfam00047  73 VNNPGGSATLS 83

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
                 ....*....|....*....|.
gi 332800971 255 VTLTCEVPAQPSPQIHWMKDG 275
Cdd:cd00096    1 VTLTCSASGNPPPTITWYKNG 21

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        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800971  25 NITARIGEPLVLKCKgAPKKPPQRLEWKLNTGRTEAWKVLSpqgggpwDSVARVLPNGSLFLPAV-----GIQDEGIFRC 99
Cdd:cd07693    9 DLIVSKGDPATLNCK-AEGRPTPTIQWLKNGQPLETDKDDP-------RSHRIVLPSGSLFFLRVvhgrkGRSDEGVYVC 80

                         90
                 ....*....|....*...
gi 332800971 100 QAMNRNGKETKSNYRVRV 117
Cdd:cd07693   81 VAHNSLGEAVSRNASLEV 98

Immunoglobulin I-set domain;

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 332800971  241 VVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDG 275
Cdd:pfam07679   4 TQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDG 38

Seventh 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 seventh 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800971  20 VVGAQNITARIGEPLVLKCKGAPKKPPQrLEWKLNTGRTEA-WKVLSpqgggpWDSVARVLPNGSLFLPAVGIQDEGIFR 98
Cdd:cd20954    5 IVEPVDANVAAGQDVMLHCQADGFPTPT-VTWKKATGSTPGeYKDLL------YDPNVRILPNGTLVFGHVQKENEGHYL 77

                 ....*
gi 332800971  99 CQAMN 103
Cdd:cd20954   78 CEAKN 82

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 332800971 242 VEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDGL 276
Cdd:cd05736    5 VYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGM 39

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332800971 129 SASELTAG-VPNKVGTCVSEGSYPAGTLSWH--LDGKPLVPNEKGvsvkeqtrrhPETGLFTLQSELMVTPAR 198
Cdd:cd07703    6 EAQEVQAGgIPVPVARCVSANGRPPARISWSstLNGNANTTQVPG----------PDSGTVTVTSEYSLVPTP 68

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. 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
                 ....*....|....*....|....
gi 332800971 252 GGTVTLTCEVPAQPSPQIHWMKDG 275
Cdd:cd05893   15 GMPVTFTCRVAGNPKPKIYWFKDG 38