CNTN1_HUMAN
ID CNTN1_HUMAN Reviewed; 1018 AA.
AC Q12860; A8K0H9; A8K0Y3; Q12861; Q14030; Q7M4P0; Q8N466;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Contactin-1;
DE AltName: Full=Glycoprotein gp135;
DE AltName: Full=Neural cell surface protein F3;
DE Flags: Precursor;
GN Name=CNTN1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Neuroblastoma;
RX PubMed=8164510; DOI=10.1016/0169-328x(94)90372-7;
RA Reid R.A., Bronson D.D., Young K.M., Hemperly J.J.;
RT "Identification and characterization of the human cell adhesion molecule
RT contactin.";
RL Brain Res. Mol. Brain Res. 21:1-8(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=7959734; DOI=10.1006/geno.1994.1316;
RA Berglund E.O., Ranscht B.;
RT "Molecular cloning and in situ localization of the human contactin gene
RT (CNTN1) on chromosome 12q11-q12.";
RL Genomics 21:571-582(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Amygdala, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 21-40 AND 679-693 (ISOFORM 1), SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain cortex;
RX PubMed=2026173; DOI=10.1111/j.1432-1033.1991.tb15943.x;
RA Berglund E., Stigbrand T., Carlsson S.R.;
RT "Isolation and characterization of a membrane glycoprotein from human brain
RT with sequence similarities to cell adhesion proteins from chicken and
RT mouse.";
RL Eur. J. Biochem. 197:549-554(1991).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-494.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [7]
RP GLYCOSYLATION AT ASN-494.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [8]
RP INTERACTION WITH PTPRZ1.
RX PubMed=20133774; DOI=10.1073/pnas.0911235107;
RA Bouyain S., Watkins D.J.;
RT "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members
RT of the contactin family of neural recognition molecules.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010).
RN [9]
RP STRUCTURE BY NMR OF 791-903.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the FN3 domain of human contactin 1.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-794.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [11]
RP INVOLVEMENT IN MYPCN.
RX PubMed=19026398; DOI=10.1016/j.ajhg.2008.10.022;
RA Compton A.G., Albrecht D.E., Seto J.T., Cooper S.T., Ilkovski B.,
RA Jones K.J., Challis D., Mowat D., Ranscht B., Bahlo M., Froehner S.C.,
RA North K.N.;
RT "Mutations in contactin-1, a neural adhesion and neuromuscular junction
RT protein, cause a familial form of lethal congenital myopathy.";
RL Am. J. Hum. Genet. 83:714-724(2008).
CC -!- FUNCTION: Contactins mediate cell surface interactions during nervous
CC system development. Involved in the formation of paranodal axo-glial
CC junctions in myelinated peripheral nerves and in the signaling between
CC axons and myelinating glial cells via its association with CNTNAP1.
CC Participates in oligodendrocytes generation by acting as a ligand of
CC NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through
CC the released notch intracellular domain (NICD) and subsequent
CC translocation to the nucleus. Interaction with TNR induces a repulsion
CC of neurons and an inhibition of neurite outgrowth (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer (PubMed:2026173). Interacts with CNTNAP1 in cis form
CC (By similarity). Binds to the carbonic-anhydrase like domain of PTPRZ1
CC (PubMed:20133774). Interacts with NOTCH1 and TNR. Detected in a complex
CC with NRCAM and PTPRB (By similarity). Interacts with TASOR (By
CC similarity). {ECO:0000250|UniProtKB:P12960,
CC ECO:0000250|UniProtKB:Q63198, ECO:0000269|PubMed:20133774,
CC ECO:0000269|PubMed:2026173}.
CC -!- INTERACTION:
CC Q12860; Q9UHC6: CNTNAP2; NbExp=5; IntAct=EBI-5564336, EBI-310892;
CC Q12860; P23471: PTPRZ1; NbExp=3; IntAct=EBI-5564336, EBI-2263175;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Lipid-anchor, GPI-
CC anchor; Extracellular side.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Lipid-anchor, GPI-
CC anchor; Extracellular side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q12860-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12860-2; Sequence=VSP_002500;
CC Name=3;
CC IsoId=Q12860-3; Sequence=VSP_011959, VSP_011960;
CC -!- TISSUE SPECIFICITY: Strongly expressed in brain and in neuroblastoma
CC and retinoblastoma cell lines. Lower levels of expression in lung,
CC pancreas, kidney and skeletal muscle. {ECO:0000269|PubMed:2026173,
CC ECO:0000269|PubMed:8164510}.
CC -!- DISEASE: Myopathy, congenital, Compton-North (MYPCN) [MIM:612540]: A
CC lethal, autosomal recessive, congenital myopathy characterized by fetal
CC akinesia, neonatal hypotonia, severe muscle weakness, loss of beta2-
CC syntrophin and alpha-dystrobrevin from the muscle sarcolemma and
CC disruption of sarcomeres with disorganization of the Z band.
CC {ECO:0000269|PubMed:19026398}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; Z21488; CAA79696.1; -; mRNA.
DR EMBL; U07819; AAA67920.1; -; mRNA.
DR EMBL; U07820; AAA67921.1; -; mRNA.
DR EMBL; AK289544; BAF82233.1; -; mRNA.
DR EMBL; AK289698; BAF82387.1; -; mRNA.
DR EMBL; BC036569; AAH36569.1; -; mRNA.
DR CCDS; CCDS58225.1; -. [Q12860-3]
DR CCDS; CCDS8737.1; -. [Q12860-1]
DR CCDS; CCDS8738.1; -. [Q12860-2]
DR PIR; A54744; A54744.
DR PIR; S15394; S15394.
DR RefSeq; NP_001242992.1; NM_001256063.1. [Q12860-3]
DR RefSeq; NP_001242993.1; NM_001256064.1. [Q12860-3]
DR RefSeq; NP_001834.2; NM_001843.3. [Q12860-1]
DR RefSeq; NP_778203.1; NM_175038.2. [Q12860-2]
DR RefSeq; XP_005268708.1; XM_005268651.2. [Q12860-1]
DR RefSeq; XP_006719304.1; XM_006719241.2. [Q12860-1]
DR RefSeq; XP_011536228.1; XM_011537926.2. [Q12860-1]
DR RefSeq; XP_011536229.1; XM_011537927.2. [Q12860-1]
DR RefSeq; XP_016874314.1; XM_017018825.1.
DR RefSeq; XP_016874315.1; XM_017018826.1. [Q12860-3]
DR RefSeq; XP_016874316.1; XM_017018827.1. [Q12860-3]
DR PDB; 2EE2; NMR; -; A=798-903.
DR PDB; 3S97; X-ray; 2.30 A; C/D=133-329.
DR PDBsum; 2EE2; -.
DR PDBsum; 3S97; -.
DR AlphaFoldDB; Q12860; -.
DR SMR; Q12860; -.
DR BioGRID; 107672; 40.
DR DIP; DIP-59714N; -.
DR IntAct; Q12860; 28.
DR MINT; Q12860; -.
DR STRING; 9606.ENSP00000447006; -.
DR GlyConnect; 1930; 6 N-Linked glycans (6 sites).
DR GlyGen; Q12860; 11 sites, 6 N-linked glycans (6 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q12860; -.
DR PhosphoSitePlus; Q12860; -.
DR SwissPalm; Q12860; -.
DR BioMuta; CNTN1; -.
DR DMDM; 2497301; -.
DR EPD; Q12860; -.
DR jPOST; Q12860; -.
DR MassIVE; Q12860; -.
DR MaxQB; Q12860; -.
DR PaxDb; Q12860; -.
DR PeptideAtlas; Q12860; -.
DR PRIDE; Q12860; -.
DR ProteomicsDB; 58988; -. [Q12860-1]
DR ProteomicsDB; 58989; -. [Q12860-2]
DR ProteomicsDB; 58990; -. [Q12860-3]
DR TopDownProteomics; Q12860-3; -. [Q12860-3]
DR ABCD; Q12860; 1 sequenced antibody.
DR Antibodypedia; 25021; 344 antibodies from 40 providers.
DR DNASU; 1272; -.
DR Ensembl; ENST00000347616.5; ENSP00000325660.3; ENSG00000018236.15. [Q12860-1]
DR Ensembl; ENST00000348761.2; ENSP00000261160.3; ENSG00000018236.15. [Q12860-2]
DR Ensembl; ENST00000547702.5; ENSP00000448004.1; ENSG00000018236.15. [Q12860-3]
DR Ensembl; ENST00000547849.5; ENSP00000448653.1; ENSG00000018236.15. [Q12860-3]
DR Ensembl; ENST00000551295.7; ENSP00000447006.1; ENSG00000018236.15. [Q12860-1]
DR GeneID; 1272; -.
DR KEGG; hsa:1272; -.
DR MANE-Select; ENST00000551295.7; ENSP00000447006.1; NM_001843.4; NP_001834.2.
DR UCSC; uc001rmm.3; human. [Q12860-1]
DR CTD; 1272; -.
DR DisGeNET; 1272; -.
DR GeneCards; CNTN1; -.
DR HGNC; HGNC:2171; CNTN1.
DR HPA; ENSG00000018236; Tissue enhanced (brain).
DR MalaCards; CNTN1; -.
DR MIM; 600016; gene.
DR MIM; 612540; phenotype.
DR neXtProt; NX_Q12860; -.
DR OpenTargets; ENSG00000018236; -.
DR Orphanet; 210163; Congenital lethal myopathy, Compton-North type.
DR PharmGKB; PA26685; -.
DR VEuPathDB; HostDB:ENSG00000018236; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000155915; -.
DR HOGENOM; CLU_005756_0_1_1; -.
DR InParanoid; Q12860; -.
DR OMA; PNHEVRM; -.
DR PhylomeDB; Q12860; -.
DR TreeFam; TF351103; -.
DR PathwayCommons; Q12860; -.
DR Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR Reactome; R-HSA-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus.
DR Reactome; R-HSA-373760; L1CAM interactions.
DR Reactome; R-HSA-447043; Neurofascin interactions.
DR SignaLink; Q12860; -.
DR BioGRID-ORCS; 1272; 40 hits in 1072 CRISPR screens.
DR ChiTaRS; CNTN1; human.
DR EvolutionaryTrace; Q12860; -.
DR GeneWiki; CNTN1; -.
DR GenomeRNAi; 1272; -.
DR Pharos; Q12860; Tbio.
DR PRO; PR:Q12860; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q12860; protein.
DR Bgee; ENSG00000018236; Expressed in cortical plate and 163 other tissues.
DR ExpressionAtlas; Q12860; baseline and differential.
DR Genevisible; Q12860; HS.
DR GO; GO:0099025; C:anchored component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:Ensembl.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0032289; P:central nervous system myelin formation; IEA:Ensembl.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; IEA:Ensembl.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR036992; Contactin-1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR PANTHER; PTHR44170:SF10; PTHR44170:SF10; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Notch signaling pathway;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..20
FT CHAIN 21..?993
FT /note="Contactin-1"
FT /id="PRO_0000014685"
FT PROPEP ?994..1018
FT /note="Removed in mature form"
FT /id="PRO_0000014686"
FT DOMAIN 41..131
FT /note="Ig-like C2-type 1"
FT DOMAIN 137..223
FT /note="Ig-like C2-type 2"
FT DOMAIN 241..326
FT /note="Ig-like C2-type 3"
FT DOMAIN 331..407
FT /note="Ig-like C2-type 4"
FT DOMAIN 413..500
FT /note="Ig-like C2-type 5"
FT DOMAIN 504..601
FT /note="Ig-like C2-type 6"
FT DOMAIN 606..704
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 709..806
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 811..906
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 907..1000
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 693..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 993
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 933
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 65..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 158..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 263..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 352..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 436..484
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 526..583
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 21..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7959734"
FT /id="VSP_002500"
FT VAR_SEQ 603..627
FT /note="PPGPPGGLRIEDIRATSVALTWSRG -> KNRKGGEKNMVDSFLPVCASLPP
FT TW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011959"
FT VAR_SEQ 628..1018
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011960"
FT VARIANT 794
FT /note="P -> H (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035506"
FT VARIANT 798
FT /note="V -> L (in dbSNP:rs1056020)"
FT /id="VAR_011722"
FT VARIANT 824
FT /note="E -> G (in dbSNP:rs11553341)"
FT /id="VAR_049866"
FT CONFLICT 682
FT /note="V -> I (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="L -> P (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="R -> I (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 692
FT /note="P -> F (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:3S97"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:3S97"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:3S97"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 259..269
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3S97"
FT TURN 290..293
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:3S97"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 306..314
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 317..328
FT /evidence="ECO:0007829|PDB:3S97"
FT STRAND 816..821
FT /evidence="ECO:0007829|PDB:2EE2"
FT STRAND 824..828
FT /evidence="ECO:0007829|PDB:2EE2"
FT STRAND 839..849
FT /evidence="ECO:0007829|PDB:2EE2"
FT HELIX 851..853
FT /evidence="ECO:0007829|PDB:2EE2"
FT STRAND 855..860
FT /evidence="ECO:0007829|PDB:2EE2"
FT STRAND 864..868
FT /evidence="ECO:0007829|PDB:2EE2"
FT STRAND 876..884
FT /evidence="ECO:0007829|PDB:2EE2"
FT STRAND 886..888
FT /evidence="ECO:0007829|PDB:2EE2"
FT STRAND 896..899
FT /evidence="ECO:0007829|PDB:2EE2"
FT CONFLICT Q12860-3:610
FT /note="K -> I (in Ref. 3; BAF82233)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1018 AA; 113320 MW; 4B8FDC5BFD434ED5 CRC64;
MKMWLLVSHL VIISITTCLA EFTWYRRYGH GVSEEDKGFG PIFEEQPINT IYPEESLEGK
VSLNCRARAS PFPVYKWRMN NGDVDLTSDR YSMVGGNLVI NNPDKQKDAG IYYCLASNNY
GMVRSTEATL SFGYLDPFPP EERPEVRVKE GKGMVLLCDP PYHFPDDLSY RWLLNEFPVF
ITMDKRRFVS QTNGNLYIAN VEASDKGNYS CFVSSPSITK SVFSKFIPLI PIPERTTKPY
PADIVVQFKD VYALMGQNVT LECFALGNPV PDIRWRKVLE PMPSTAEIST SGAVLKIFNI
QLEDEGIYEC EAENIRGKDK HQARIYVQAF PEWVEHINDT EVDIGSDLYW PCVATGKPIP
TIRWLKNGYA YHKGELRLYD VTFENAGMYQ CIAENTYGAI YANAELKILA LAPTFEMNPM
KKKILAAKGG RVIIECKPKA APKPKFSWSK GTEWLVNSSR ILIWEDGSLE INNITRNDGG
IYTCFAENNR GKANSTGTLV ITDPTRIILA PINADITVGE NATMQCAASF DPALDLTFVW
SFNGYVIDFN KENIHYQRNF MLDSNGELLI RNAQLKHAGR YTCTAQTIVD NSSASADLVV
RGPPGPPGGL RIEDIRATSV ALTWSRGSDN HSPISKYTIQ TKTILSDDWK DAKTDPPIIE
GNMEAARAVD LIPWMEYEFR VVATNTLGRG EPSIPSNRIK TDGAAPNVAP SDVGGGGGRN
RELTITWAPL SREYHYGNNF GYIVAFKPFD GEEWKKVTVT NPDTGRYVHK DETMSPSTAF
QVKVKAFNNK GDGPYSLVAV INSAQDAPSE APTEVGVKVL SSSEISVHWE HVLEKIVESY
QIRYWAAHDK EEAANRVQVT SQEYSARLEN LLPDTQYFIE VGACNSAGCG PPSDMIEAFT
KKAPPSQPPR IISSVRSGSR YIITWDHVVA LSNESTVTGY KVLYRPDGQH DGKLYSTHKH
SIEVPIPRDG EYVVEVRAHS DGGDGVVSQV KISGAPTLSP SLLGLLLPAF GILVYLEF
