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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116014342   117 SEGELAKLVCKSDASYPPITDWFWfktsdTGEEEAITNsteanGKYVVVSTPEKSQLTISNLDVNvDPGTYVCNATNAQG 196
Cdd:smart00410   7 KEGESVTLSCEASGSPPPEVTWYK-----QGGKLLAES-----GRFSVSRSGSTSTLTISNVTPE-DSGTYTCAATNSSG 75

                           90
                   ....*....|
gi 116014342   197 TTRETISLRV 206
Cdd:smart00410  76 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 116014342   117 SEGELAKLVCKSDASYPPITDWFWfktsdTGEEEAITNsteanGKYVVVSTPEKSQLTISNLDVNvDPGTYVCNATNAQG 196
Cdd:smart00410   7 KEGESVTLSCEASGSPPPEVTWYK-----QGGKLLAES-----GRFSVSRSGSTSTLTISNVTPE-DSGTYTCAATNSSG 75

                           90
                   ....*....|
gi 116014342   197 TTRETISLRV 206
Cdd:smart00410  76 SASSGTTLTV 85

First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116014342 114 EHSSEGELAkLVCKSDASYPPITDWfwfkTSDTGEEEAITNSTEANGKYVVVSTPEKSQltisnldvnvDPGTYVCNATN 193
Cdd:cd05849   15 EESTEGKVS-VNCRARANPFPIYKW----RKNNLDIDLTNDRYSMVGGNLVINNPDKYK----------DAGRYVCIVSN 79

                 ....*...
gi 116014342 194 AQGTTRET 201
Cdd:cd05849   80 IYGKVRSR 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 116014342   117 SEGELAKLVCKSDASYPPITDWFWfktsdTGEEEAITNsteanGKYVVVSTPEKSQLTISNLDVNvDPGTYVCNATNAQG 196
Cdd:smart00410   7 KEGESVTLSCEASGSPPPEVTWYK-----QGGKLLAES-----GRFSVSRSGSTSTLTISNVTPE-DSGTYTCAATNSSG 75

                           90
                   ....*....|
gi 116014342   197 TTRETISLRV 206
Cdd:smart00410  76 SASSGTTLTV 85

Immunoglobulin I-set domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116014342  117 SEGELAKLVCKSDASYPP-ITdwfWFKtsdtgEEEAITNSteanGKYVVVSTPEKSQLTISNLDVNvDPGTYVCNATNAQ 195
Cdd:pfam07679  13 QEGESARFTCTVTGTPDPeVS---WFK-----DGQPLRSS----DRFKVTYEGGTYTLTISNVQPD-DSGKYTCVATNSA 79

                          90
                  ....*....|.
gi 116014342  196 GTTRETISLRV 206
Cdd:pfam07679  80 GEAEASAELTV 90

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. 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. 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 structures of the titin-A168169 lacks this strand and thus it 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116014342 119 GELAKLVCKSDASYPPITDWFWFKTSDTGEEEAITNSTEANGKYVVvstpeksqltISNLDVNVDPGTYVCNATNAQG 196
Cdd:cd20971   16 QSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRIQEFKGGYHQL----------IIASVTDDDATVYQVRATNQGG 83

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-nonNCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). 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 116014342 117 SEGELAKLVCKSdASYPPITDWFwfktSDTGEEeAITNSTEangKYVVVSTPEKSQLTISNLDVNvDPGTYVCNATNAQG 196
Cdd:cd04977   13 SVGESKFFLCKV-SGDAKNINWV----SPNGEK-VLTKHGN---LKVVNHGSVLSSLTIYNANIN-DAGIYKCVATNGKG 82

                         90
                 ....*....|.
gi 116014342 197 TTRE-TISLRV 206
Cdd:cd04977   83 TESEaTVKLDI 93

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2 (OCAM/mamFas II, RNCAM). NCAM-2 is organized similarly to NCAM-1, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. 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
                 ....*....|....*....|....*....|....*...
gi 116014342 170 KSQLTISNLDVNvDPGTYVCNATNAQGTTRE-TISLRV 206
Cdd:cd05866   55 RSRLTIYNANIE-DAGIYRCQATDAKGQTQEaTVVLEI 91

First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116014342 114 EHSSEGELAkLVCKSDASYPPITDWfwfktsdtgeeeaITNSTE----ANGKYVVVStpekSQLTISNLDVNVDPGTYVC 189
Cdd:cd04967   15 EDSDEKKVA-LNCRARANPVPSYRW-------------LMNGTEidleSDYRYSLVD----GTLVISNPSKAKDAGHYQC 76

                         90       100
                 ....*....|....*....|....
gi 116014342 190 NATNAQGTtretislrVRSRMAAL 213
Cdd:cd04967   77 LATNTVGS--------VLSREATL 92

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116014342 118 EGELAKLVCKSDASYPPITDWFwfktsdtGEEEAITNSTEAnGKYVVVSTPEKSQLTISNLDVNvDPGTYVCNATNAQGT 197
Cdd:cd20951   14 EKSDAKLRVEVQGKPDPEVKWY-------KNGVPIDPSSIP-GKYKIESEYGVHVLHIRRVTVE-DSAVYSAVAKNIHGE 84

                         90
                 ....*....|
gi 116014342 198 TRETISLRVR 207
Cdd:cd20951   85 ASSSASVVVE 94

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. 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 the MuSK lacks this strand and thus it 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 116014342 118 EGELAKLVCKSDASYPPITDWFwfktSDTGEEEAItnsteaNGKYVVVStpEKSQLTISNLDvNVDPGTYVCNATN-AQG 196
Cdd:cd20970   16 EGENATFMCRAEGSPEPEISWT----RNGNLIIEF------NTRYIVRE--NGTTLTIRNIR-RSDMGIYLCIASNgVPG 82

                         90
                 ....*....|
gi 116014342 197 TTRETISLRV 206
Cdd:cd20970   83 SVEKRITLQV 92