Mucin-2 protein WxxW repeating region; This family is repeating region found on mucins 2 and 5. The function is not known, but the repeat can be present in up to 32 copies, as in Swiss:C3Y5K5, from Branchiostoma floridae. The region carries a highly conserved WxxW sequence motif and also has at least six well conserved cysteine residues.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546287   32 WTTWFNIDYPGG--KGDYERLDAIRFYYgdRVCARPLRLEAR--TTDWTPAGSTGQVVHGSPREGFWCLNREQRPGQnCS 107
Cdd:pfam13330    1 WTPWFDVDNPSGsgGGDFETLENLRAYG--KFCENPTDIECRaePPTGVPASETGQVVTCDVTTGLVCRNADQQPDG-CL 77

                   ....*...
gi 2462546287  108 NYTVRFLC 115
Cdd:pfam13330   78 DYEVRFLC 85

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462546287  285 PYMVMNPETKARRAGQSVSLCCKATGKPRPdKYFWYHNDTLLDP------SLYKHESKLVLRKLQQHQAGEYFCKA 354
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPP-TITWYKNGEPISSgstrsrSLSGSNSTLTISNVTRSDAGTYTCVA 76

Mucin-2 protein WxxW repeating region; This family is repeating region found on mucins 2 and 5. The function is not known, but the repeat can be present in up to 32 copies, as in Swiss:C3Y5K5, from Branchiostoma floridae. The region carries a highly conserved WxxW sequence motif and also has at least six well conserved cysteine residues.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546287   32 WTTWFNIDYPGG--KGDYERLDAIRFYYgdRVCARPLRLEAR--TTDWTPAGSTGQVVHGSPREGFWCLNREQRPGQnCS 107
Cdd:pfam13330    1 WTPWFDVDNPSGsgGGDFETLENLRAYG--KFCENPTDIECRaePPTGVPASETGQVVTCDVTTGLVCRNADQQPDG-CL 77

                   ....*...
gi 2462546287  108 NYTVRFLC 115
Cdd:pfam13330   78 DYEVRFLC 85

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462546287  285 PYMVMNPETKARRAGQSVSLCCKATGKPRPdKYFWYHNDTLLDP------SLYKHESKLVLRKLQQHQAGEYFCKA 354
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPP-TITWYKNGEPISSgstrsrSLSGSNSTLTISNVTRSDAGTYTCVA 76

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 2462546287  302 VSLCCKATGKPRPdKYFWYHNDTLLDPS------LYKHESKLVLRKLQQHQAGEYFCKAQSDAGAVKSKVA 366
Cdd:cd00096      1 VTLTCSASGNPPP-TITWYKNGKPLPPSsrdsrrSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70

Carboxypeptidase regulatory-like domain;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462546287  202 LHGAVSLPGGAPASGAAIYLLTKTPKLL--TQTDSDGRFRIPGLcPDGKSILKITKVKFAPIVLT 264
Cdd:pfam13620    2 ISGTVTDPSGAPVPGATVTVTNTDTGTVrtTTTDADGRYRFPGL-PPGTYTVTVSAPGFKTATRT 65

Mucin-2 protein WxxW repeating region; This family is repeating region found on mucins 2 and 5. The function is not known, but the repeat can be present in up to 32 copies, as in Swiss:C3Y5K5, from Branchiostoma floridae. The region carries a highly conserved WxxW sequence motif and also has at least six well conserved cysteine residues.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546287   32 WTTWFNIDYPGG--KGDYERLDAIRFYYgdRVCARPLRLEAR--TTDWTPAGSTGQVVHGSPREGFWCLNREQRPGQnCS 107
Cdd:pfam13330    1 WTPWFDVDNPSGsgGGDFETLENLRAYG--KFCENPTDIECRaePPTGVPASETGQVVTCDVTTGLVCRNADQQPDG-CL 77

                   ....*...
gi 2462546287  108 NYTVRFLC 115
Cdd:pfam13330   78 DYEVRFLC 85

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462546287  285 PYMVMNPETKARRAGQSVSLCCKATGKPRPdKYFWYHNDTLLDP------SLYKHESKLVLRKLQQHQAGEYFCKA 354
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPP-TITWYKNGEPISSgstrsrSLSGSNSTLTISNVTRSDAGTYTCVA 76

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

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546287   291 PETKARRAGQSVSLCCKATGKPRPdKYFWYHND-TLLDPSL------YKHESKLVLRKLQQHQAGEYFCKAQSDAGAVKS 363
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPP-EVTWYKQGgKLLAESGrfsvsrSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                    ....*..
gi 2462546287   364 KVaQLIV 370
Cdd:smart00410   80 GT-TLTV 85

Thrombospondin type 1 domain;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462546287  129 SPWSPWSKCSAACGQtGVQTRTRIC--LAEMVSLCSEASEEGQHCMGQDC 176
Cdd:pfam00090    1 SPWSPWSPCSVTCGK-GIQVRQRTCksPFPGGEPCTGDDIETQACKMDKC 49

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462546287  129 SPWSPWSKCSAACGqTGVQTRTRICLAemvslcsEASEEGQHC 171
Cdd:pfam19028    4 SEWSEWSECSVTCG-GGVQTRTRTVIV-------EPQNGGRPC 38

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546287  281 RAETPYMvMNPETKARRAGQSVSLCCKATGKPRPDkYFWYHNDTLLDPSLYKHESK----LVLRKLQQHQAGEYFCKAQS 356
Cdd:cd05856      2 RFTQPAK-MRRRVIARPVGSSVRLKCVASGNPRPD-ITWLKDNKPLTPPEIGENKKkkwtLSLKNLKPEDSGKYTCHVSN 79

                   ....*
gi 2462546287  357 DAGAV 361
Cdd:cd05856     80 RAGEI 84

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 2462546287  290 NPETKARRAGQSVSLCCKATGKPRPDkYFWYHNDTLLDPSLYKHESK-----LVLRKLQQHQAGEYFCKAQSDAGAVKSK 364
Cdd:cd20970      8 PSFTVTAREGENATFMCRAEGSPEPE-ISWTRNGNLIIEFNTRYIVRengttLTIRNIRRSDMGIYLCIASNGVPGSVEK 86

                   ....*.
gi 2462546287  365 VAQLIV 370
Cdd:cd20970     87 RITLQV 92

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 2462546287  285 PYMVMNPETKARRAGQSVSLCCKATGKPRPdKYFW----------YHnDTLLDPSLYKHES-KLVLRKLQQHQAGEYFCK 353
Cdd:cd20954      2 PRWIVEPVDANVAAGQDVMLHCQADGFPTP-TVTWkkatgstpgeYK-DLLYDPNVRILPNgTLVFGHVQKENEGHYLCE 79

                           90
                   ....*....|....*..
gi 2462546287  354 AQSDAGAVKSKVAQLIV 370
Cdd:cd20954     80 AKNGIGSGLSKVIFLKV 96

Second immunoglobulin (Ig)-like domain of Axl/Tyro3 family receptor tyrosine kinases (RTKs); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in the Axl/Tyro3 family of receptor tyrosine kinases (RTKs). This family includes Axl (also known as Ark, Ufo, and Tyro7), Tyro3 (also known as Sky, Rse, Brt, Dtk, and Tif), and Mer (also known as Nyk, c-Eyk, and Tyro12). Axl/Tyro3 family receptors have an extracellular portion with two Ig-like domains followed by two fibronectin-types III (FNIII) domains, a membrane-spanning single helix, and a cytoplasmic tyrosine kinase domain. Axl, Tyro3, and Mer are widely expressed in adult tissues, though they show higher expression in the brain, lymphatic and vascular systems, and testis. Axl, Tyro3, and Mer bind the vitamin K dependent protein Gas6 with high affinity, and in doing so activate their tyrosine kinase activity. Axl/Gas6 signaling may play a part in cell adhesion processes, prevention of apoptosis, and cell proliferation.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546287  286 YMVMNPETKARRAGQSVSLCCKATGKPRPDKYFWYHNDTLLDPSLYKHESKLVLRKLqqHQAGEYFCKAQSDAGAVKSKV 365
Cdd:cd05749      1 HFTVEPEDLAVTANTPFNLTCQAVGPPEPVEILWWQGGSPLGGPPAPSPSVLNVPGL--NETTKFSCEAHNAKGLTSSRT 78

                   ...
gi 2462546287  366 AQL 368
Cdd:cd05749     79 ATV 81

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 2462546287  298 AGQSVSLCCKATGKPRPdKYFWYHNDTLLDPSL----YKHESK-----LVLRKLQQHQAGEYFCKAQSDAGAVKSKvAQL 368
Cdd:cd20951     14 EKSDAKLRVEVQGKPDP-EVKWYKNGVPIDPSSipgkYKIESEygvhvLHIRRVTVEDSAVYSAVAKNIHGEASSS-ASV 91

                   ..
gi 2462546287  369 IV 370
Cdd:cd20951     92 VV 93

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        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546287  288 VMNPETKARRAGQSVSLCCKATGKPrPDKYFWYHNDTLL--DP-----------SLYKHESKLVLRKLQQHQAGEYFCKA 354
Cdd:cd20950      2 TVNIPSSATIGNRAVLTCSEPDGSP-PSEYTWFKDGVVMptNPkstrafsnssySLDPTTGELVFDPLSASDTGEYSCEA 80

                   ....*
gi 2462546287  355 QSDAG 359
Cdd:cd20950     81 RNGYG 85

Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546287  285 PYMVMNPETKARRAGQSVSLCCKATGKPRPdKYFWYHNDTLLDPSLYK-----------HESKLVLRKLQQHQAGEYFCK 353
Cdd:cd05734      2 PRFVVQPNDQDGIYGKAVVLNCSADGYPPP-TIVWKHSKGSGVPQFQHivplngriqllSNGSLLIKHVLEEDSGYYLCK 80

                           90
                   ....*....|....*..
gi 2462546287  354 AQSDAGAVKSKVAQLIV 370
Cdd:cd05734     81 VSNDVGADISKSMYLTV 97

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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462546287  297 RAGQSVSLCCKATGKPRPDKYFWYHNDTLL-----DPSLYKHESKLVLRKLQQHQAGEYFCKAQSDAGAVKSKVAQL 368
Cdd:cd20979     13 REGQPTVLECVTEGGDQGVKYSWLKDGKSFnwqehNVAQRKDEGSLVFLKPQASDEGQYQCFAETPAGVASSRVISF 89

Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here are composed of the second immunoglobulin (Ig)-like domain in protein tyrosine kinase (PTK) 7, also known as CCK4. PTK7 is a subfamily of the receptor protein tyrosine kinase family, and is referred to as an RPTK-like molecule. RPTKs transduce extracellular signals across the cell membrane and play important roles in regulating cell proliferation, migration, and differentiation. PTK7 is organized as an extracellular portion having seven Ig-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase-like domain. PTK7 is considered a pseudokinase as it has several unusual residues in some of the highly conserved tyrosine kinase (TK) motifs; it is predicted to lack TK activity. PTK7 may function as a cell-adhesion molecule. PTK7 mRNA is expressed at high levels in placenta, melanocytes, liver, lung, pancreas, and kidney. PTK7 is overexpressed in several cancers, including melanoma and colon cancer lines.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546287  285 PYMVMNPETKARRAGQS-VSLCCKATGKPRPdKYFWYHNDTLL-----DPSLYKHESKLVLRKLQQHQAGEYFCKAQSDA 358
Cdd:cd05760      1 PVVLKHPASAAEIQPSSrVTLRCHIDGHPRP-TYQWFRDGTPLsdgqgNYSVSSKERTLTLRSAGPDDSGLYYCCAHNAF 79

                   ....*
gi 2462546287  359 GAVKS 363
Cdd:cd05760     80 GSVCS 84

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. 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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462546287  306 CKATGKPRPdKYFWYHNDTLLDPSLY---KHESKLVLRKLQQHQAGEYFCKAQSDAGAVKSKvAQLIV 370
Cdd:cd05723     19 CEVTGKPTP-TVKWVKNGDVVIPSDYfkiVKEHNLQVLGLVKSDEGFYQCIAENDVGNAQAS-AQLII 84