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 1519313775   56 WTTWFNIDYPGG--KGDYERLDAIRFYYgdRVCARPLRLEAR--TTDWTPAGSTGQVVHGSPREGFWCLNREQRPGQnCS 131
Cdd:pfam13330    1 WTPWFDVDNPSGsgGGDFETLENLRAYG--KFCENPTDIECRaePPTGVPASETGQVVTCDVTTGLVCRNADQQPDG-CL 77

                   ....*...
gi 1519313775  132 NYTVRFLC 139
Cdd:pfam13330   78 DYEVRFLC 85

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519313775  309 PYMVMNPETKARRAGQSVSLCCKATGKPRPdKYFWYHNDTLLDP------SLYKHESKLVLRKLQQHQAGEYFCKA 378
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 1519313775   56 WTTWFNIDYPGG--KGDYERLDAIRFYYgdRVCARPLRLEAR--TTDWTPAGSTGQVVHGSPREGFWCLNREQRPGQnCS 131
Cdd:pfam13330    1 WTPWFDVDNPSGsgGGDFETLENLRAYG--KFCENPTDIECRaePPTGVPASETGQVVTCDVTTGLVCRNADQQPDG-CL 77

                   ....*...
gi 1519313775  132 NYTVRFLC 139
Cdd:pfam13330   78 DYEVRFLC 85

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519313775  309 PYMVMNPETKARRAGQSVSLCCKATGKPRPdKYFWYHNDTLLDP------SLYKHESKLVLRKLQQHQAGEYFCKA 378
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 1519313775  326 VSLCCKATGKPRPdKYFWYHNDTLLDPS------LYKHESKLVLRKLQQHQAGEYFCKAQSDAGAVKSKVA 390
Cdd:cd00096      1 VTLTCSASGNPPP-TITWYKNGKPLPPSsrdsrrSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70

Carboxypeptidase regulatory-like domain;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519313775  226 LHGAVSLPGGAPASGAAIYLLTKTPKLL--TQTDSDGRFRIPGLcPDGKSILKITKVKFAPIVLT 288
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 1519313775   56 WTTWFNIDYPGG--KGDYERLDAIRFYYgdRVCARPLRLEAR--TTDWTPAGSTGQVVHGSPREGFWCLNREQRPGQnCS 131
Cdd:pfam13330    1 WTPWFDVDNPSGsgGGDFETLENLRAYG--KFCENPTDIECRaePPTGVPASETGQVVTCDVTTGLVCRNADQQPDG-CL 77

                   ....*...
gi 1519313775  132 NYTVRFLC 139
Cdd:pfam13330   78 DYEVRFLC 85

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519313775  309 PYMVMNPETKARRAGQSVSLCCKATGKPRPdKYFWYHNDTLLDP------SLYKHESKLVLRKLQQHQAGEYFCKA 378
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 1519313775   315 PETKARRAGQSVSLCCKATGKPRPdKYFWYHND-TLLDPSL------YKHESKLVLRKLQQHQAGEYFCKAQSDAGAVKS 387
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPP-EVTWYKQGgKLLAESGrfsvsrSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                    ....*..
gi 1519313775   388 KVaQLIV 394
Cdd:smart00410   80 GT-TLTV 85

Thrombospondin type 1 domain;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1519313775  153 SPWSPWSKCSAACGQtGVQTRTRIC--LAEMVSLCSEASEEGQHCMGQDC 200
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 1519313775  153 SPWSPWSKCSAACGqTGVQTRTRICLAemvslcsEASEEGQHC 195
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 1519313775  305 RAETPYMvMNPETKARRAGQSVSLCCKATGKPRPDkYFWYHNDTLLDPSLYKHESK----LVLRKLQQHQAGEYFCKAQS 380
Cdd:cd05856      2 RFTQPAK-MRRRVIARPVGSSVRLKCVASGNPRPD-ITWLKDNKPLTPPEIGENKKkkwtLSLKNLKPEDSGKYTCHVSN 79

                   ....*
gi 1519313775  381 DAGAV 385
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 1519313775  314 NPETKARRAGQSVSLCCKATGKPRPDkYFWYHNDTLLDPSLYKHESK-----LVLRKLQQHQAGEYFCKAQSDAGAVKSK 388
Cdd:cd20970      8 PSFTVTAREGENATFMCRAEGSPEPE-ISWTRNGNLIIEFNTRYIVRengttLTIRNIRRSDMGIYLCIASNGVPGSVEK 86

                   ....*.
gi 1519313775  389 VAQLIV 394
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 1519313775  309 PYMVMNPETKARRAGQSVSLCCKATGKPRPdKYFW----------YHnDTLLDPSLYKHES-KLVLRKLQQHQAGEYFCK 377
Cdd:cd20954      2 PRWIVEPVDANVAAGQDVMLHCQADGFPTP-TVTWkkatgstpgeYK-DLLYDPNVRILPNgTLVFGHVQKENEGHYLCE 79

                           90
                   ....*....|....*..
gi 1519313775  378 AQSDAGAVKSKVAQLIV 394
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 1519313775  310 YMVMNPETKARRAGQSVSLCCKATGKPRPDKYFWYHNDTLLDPSLYKHESKLVLRKLqqHQAGEYFCKAQSDAGAVKSKV 389
Cdd:cd05749      1 HFTVEPEDLAVTANTPFNLTCQAVGPPEPVEILWWQGGSPLGGPPAPSPSVLNVPGL--NETTKFSCEAHNAKGLTSSRT 78

                   ...
gi 1519313775  390 AQL 392
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 1519313775  322 AGQSVSLCCKATGKPRPdKYFWYHNDTLLDPSL----YKHESK-----LVLRKLQQHQAGEYFCKAQSDAGAVKSKvAQL 392
Cdd:cd20951     14 EKSDAKLRVEVQGKPDP-EVKWYKNGVPIDPSSipgkYKIESEygvhvLHIRRVTVEDSAVYSAVAKNIHGEASSS-ASV 91

                   ..
gi 1519313775  393 IV 394
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 1519313775  312 VMNPETKARRAGQSVSLCCKATGKPrPDKYFWYHNDTLL--DP-----------SLYKHESKLVLRKLQQHQAGEYFCKA 378
Cdd:cd20950      2 TVNIPSSATIGNRAVLTCSEPDGSP-PSEYTWFKDGVVMptNPkstrafsnssySLDPTTGELVFDPLSASDTGEYSCEA 80

                   ....*
gi 1519313775  379 QSDAG 383
Cdd:cd20950     81 RNGYG 85

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 1519313775  321 RAGQSVSLCCKATGKPRPDKYFWYHNDTLLDPSLYKHESK-------LVLRKLQQHQAGEYFCKAQ 379
Cdd:pfam00047    9 LEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVKHDNgrttqssLLISNVTKEDAGTYTCVVN 74

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 1519313775  321 RAGQSVSLCCKATGKPRPDKYFWYHNDTLL-----DPSLYKHESKLVLRKLQQHQAGEYFCKAQSDAGAVKSKVAQL 392
Cdd:cd20979     13 REGQPTVLECVTEGGDQGVKYSWLKDGKSFnwqehNVAQRKDEGSLVFLKPQASDEGQYQCFAETPAGVASSRVISF 89

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth 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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313775  323 GQSVSLCCKATGKPRPD-KYFWYHNDTLLDPS--------LYKHES--KLVLRKLQQHQAGEYFCKAQSDAGAVKSKvAQ 391
Cdd:cd04970     17 GENATLQCHASHDPTLDlTFTWSFNGVPIDLEkieghyrrRYGKDSngDLEIVNAQLKHAGRYTCTAQTVVDSDSAS-AT 95

                   ...
gi 1519313775  392 LIV 394
Cdd:cd04970     96 LVV 98

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 1519313775  330 CKATGKPRPdKYFWYHNDTLLDPSLY---KHESKLVLRKLQQHQAGEYFCKAQSDAGAVKSKvAQLIV 394
Cdd:cd05723     19 CEVTGKPTP-TVKWVKNGDVVIPSDYfkiVKEHNLQVLGLVKSDEGFYQCIAENDVGNAQAS-AQLII 84