ID   CNTN4_HUMAN             Reviewed;        1026 AA.
AC   Q8IWV2; B2RAX3; Q8IX14; Q8TC35;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Contactin-4;
DE   AltName: Full=Brain-derived immunoglobulin superfamily protein 2;
DE            Short=BIG-2;
DE   Flags: Precursor;
GN   Name=CNTN4;
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] (ISOFORMS 1 AND 2).
RX   PubMed=12202991; DOI=10.1007/s100380200073;
RA   Zeng L., Zhang C., Xu J., Ye X., Wu Q., Dai J., Ji C., Gu S., Xie Y.,
RA   Mao Y.;
RT   "A novel splice variant of the cell adhesion molecule contactin 4 (CNTN4)
RT   is mainly expressed in human brain.";
RL   J. Hum. Genet. 47:497-499(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=14571131; DOI=10.1159/000073412;
RA   Hansford L.M., Smith S.A., Haber M., Norris M.D., Cheung B., Marshall G.M.;
RT   "Cloning and characterization of the human neural cell adhesion molecule,
RT   CNTN4 (alias BIG-2).";
RL   Cytogenet. Genome Res. 101:17-23(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Testis;
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 GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Testis;
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   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=11013081; DOI=10.1006/geno.2000.6310;
RA   Kamei Y., Takeda Y., Teramoto K., Tsutsumi O., Taketani Y., Watanabe K.;
RT   "Human NB-2 of the contactin subgroup molecules: chromosomal localization
RT   of the gene (CNTN5) and distinct expression pattern from other subgroup
RT   members.";
RL   Genomics 69:113-119(2000).
RN   [8]
RP   CHROMOSOMAL TRANSLOCATION, AND INVOLVEMENT IN 3PDS.
RX   PubMed=15106122; DOI=10.1086/421474;
RA   Fernandez T., Morgan T., Davis N., Klin A., Morris A., Farhi A.,
RA   Lifton R.P., State M.W.;
RT   "Disruption of contactin 4 (CNTN4) results in developmental delay and other
RT   features of 3p deletion syndrome.";
RL   Am. J. Hum. Genet. 74:1286-1293(2004).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65.
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   [10]
RP   INTERACTION WITH PTPRG.
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   [11]
RP   VARIANTS [LARGE SCALE ANALYSIS] PRO-176 AND ASN-420.
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).
CC   -!- FUNCTION: Contactins mediate cell surface interactions during nervous
CC       system development. Has some neurite outgrowth-promoting activity. May
CC       be involved in synaptogenesis.
CC   -!- SUBUNIT: Interacts with PTPRG. {ECO:0000269|PubMed:20133774}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Secreted
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8IWV2-1; Sequence=Displayed;
CC       Name=2; Synonyms=CNTN4A;
CC         IsoId=Q8IWV2-2; Sequence=VSP_011961;
CC       Name=3;
CC         IsoId=Q8IWV2-3; Sequence=VSP_044270, VSP_011962;
CC       Name=4;
CC         IsoId=Q8IWV2-4; Sequence=VSP_044270;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in brain. Highly expressed in
CC       cerebellum and weakly expressed in corpus callosum, caudate nucleus,
CC       amygdala and spinal cord. Also expressed in testis, pancreas, thyroid,
CC       uterus, small intestine and kidney. Not expressed in skeletal muscle.
CC       Isoform 2 is weakly expressed in cerebral cortex.
CC       {ECO:0000269|PubMed:11013081, ECO:0000269|PubMed:14571131}.
CC   -!- INDUCTION: By retinoic acid, suggesting that it may act in response to
CC       differentiating agents. {ECO:0000269|PubMed:14571131}.
CC   -!- DISEASE: Note=A chromosomal aberration involving CNTN4 has been found
CC       in a boy with characteristic physical features of 3p deletion syndrome
CC       (3PDS). Translocation t(3;10)(p26;q26). 3PDS is a rare contiguous gene
CC       disorder involving the loss of the telomeric portion of the short arm
CC       of chromosome 3 and characterized by developmental delay, growth
CC       retardation, and dysmorphic features. {ECO:0000269|PubMed:15106122}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC       family. {ECO:0000305}.
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DR   EMBL; AF464063; AAN86141.1; -; mRNA.
DR   EMBL; AY090737; AAM00025.1; -; mRNA.
DR   EMBL; AF549455; AAP05786.1; -; mRNA.
DR   EMBL; AK314396; BAG37020.1; -; mRNA.
DR   EMBL; AC018842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC022002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC022008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC024057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC026882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC066608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC087094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC087427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471055; EAW63874.1; -; Genomic_DNA.
DR   EMBL; BC026119; AAH26119.1; -; mRNA.
DR   CCDS; CCDS2558.1; -. [Q8IWV2-4]
DR   CCDS; CCDS43041.1; -. [Q8IWV2-1]
DR   RefSeq; NP_001193884.1; NM_001206955.1. [Q8IWV2-1]
DR   RefSeq; NP_001193885.1; NM_001206956.1. [Q8IWV2-3]
DR   RefSeq; NP_783200.1; NM_175607.2. [Q8IWV2-1]
DR   RefSeq; NP_783302.1; NM_175613.2. [Q8IWV2-4]
DR   RefSeq; XP_011531727.1; XM_011533425.2. [Q8IWV2-1]
DR   RefSeq; XP_011531728.1; XM_011533426.2.
DR   RefSeq; XP_011531729.1; XM_011533427.2. [Q8IWV2-1]
DR   RefSeq; XP_011531730.1; XM_011533428.2. [Q8IWV2-1]
DR   RefSeq; XP_011531731.1; XM_011533429.2. [Q8IWV2-1]
DR   RefSeq; XP_011531732.1; XM_011533430.2. [Q8IWV2-1]
DR   RefSeq; XP_016861271.1; XM_017005782.1. [Q8IWV2-1]
DR   RefSeq; XP_016861272.1; XM_017005783.1. [Q8IWV2-1]
DR   RefSeq; XP_016861273.1; XM_017005784.1. [Q8IWV2-1]
DR   AlphaFoldDB; Q8IWV2; -.
DR   SMR; Q8IWV2; -.
DR   BioGRID; 127444; 5.
DR   IntAct; Q8IWV2; 6.
DR   STRING; 9606.ENSP00000380602; -.
DR   GlyConnect; 1156; 25 N-Linked glycans (7 sites).
DR   GlyCosmos; Q8IWV2; 14 sites, 27 glycans.
DR   GlyGen; Q8IWV2; 14 sites, 27 N-linked glycans (7 sites).
DR   iPTMnet; Q8IWV2; -.
DR   PhosphoSitePlus; Q8IWV2; -.
DR   BioMuta; CNTN4; -.
DR   DMDM; 55976529; -.
DR   jPOST; Q8IWV2; -.
DR   MassIVE; Q8IWV2; -.
DR   PaxDb; 9606-ENSP00000380602; -.
DR   PeptideAtlas; Q8IWV2; -.
DR   ProteomicsDB; 3420; -.
DR   ProteomicsDB; 70904; -. [Q8IWV2-1]
DR   ProteomicsDB; 70905; -. [Q8IWV2-2]
DR   ProteomicsDB; 70906; -. [Q8IWV2-3]
DR   Antibodypedia; 9906; 249 antibodies from 31 providers.
DR   DNASU; 152330; -.
DR   Ensembl; ENST00000397459.6; ENSP00000380600.2; ENSG00000144619.15. [Q8IWV2-4]
DR   Ensembl; ENST00000397461.5; ENSP00000380602.1; ENSG00000144619.15. [Q8IWV2-1]
DR   Ensembl; ENST00000418658.6; ENSP00000396010.1; ENSG00000144619.15. [Q8IWV2-1]
DR   Ensembl; ENST00000427331.5; ENSP00000413642.1; ENSG00000144619.15. [Q8IWV2-1]
DR   GeneID; 152330; -.
DR   KEGG; hsa:152330; -.
DR   MANE-Select; ENST00000418658.6; ENSP00000396010.1; NM_175607.3; NP_783200.1.
DR   UCSC; uc003bpc.4; human. [Q8IWV2-1]
DR   AGR; HGNC:2174; -.
DR   CTD; 152330; -.
DR   DisGeNET; 152330; -.
DR   GeneCards; CNTN4; -.
DR   HGNC; HGNC:2174; CNTN4.
DR   HPA; ENSG00000144619; Tissue enhanced (parathyroid gland, retina).
DR   MIM; 607280; gene.
DR   neXtProt; NX_Q8IWV2; -.
DR   OpenTargets; ENSG00000144619; -.
DR   PharmGKB; PA26688; -.
DR   VEuPathDB; HostDB:ENSG00000144619; -.
DR   eggNOG; KOG3513; Eukaryota.
DR   GeneTree; ENSGT00940000155198; -.
DR   HOGENOM; CLU_005756_0_0_1; -.
DR   InParanoid; Q8IWV2; -.
DR   OMA; EESIFWE; -.
DR   OrthoDB; 3073820at2759; -.
DR   PhylomeDB; Q8IWV2; -.
DR   TreeFam; TF351103; -.
DR   PathwayCommons; Q8IWV2; -.
DR   Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   SignaLink; Q8IWV2; -.
DR   BioGRID-ORCS; 152330; 12 hits in 1146 CRISPR screens.
DR   ChiTaRS; CNTN4; human.
DR   GeneWiki; CNTN4; -.
DR   GenomeRNAi; 152330; -.
DR   Pharos; Q8IWV2; Tbio.
DR   PRO; PR:Q8IWV2; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q8IWV2; Protein.
DR   Bgee; ENSG00000144619; Expressed in sperm and 154 other cell types or tissues.
DR   ExpressionAtlas; Q8IWV2; baseline and differential.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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:0007413; P:axonal fasciculation; TAS:UniProtKB.
DR   GO; GO:0007409; P:axonogenesis; TAS:UniProtKB.
DR   GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR   GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR   GO; GO:0007158; P:neuron cell-cell adhesion; TAS:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; TAS:UniProtKB.
DR   CDD; cd00063; FN3; 4.
DR   CDD; cd05853; Ig6_Contactin-4; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 10.
DR   InterPro; IPR033007; CNTN4_Ig6.
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:SF18; CONTACTIN 4-RELATED; 1.
DR   PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF13927; Ig_3; 3.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 6.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 6.
DR   Genevisible; Q8IWV2; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane;
KW   Chromosomal rearrangement; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..1000
FT                   /note="Contactin-4"
FT                   /id="PRO_0000014711"
FT   PROPEP          1001..1026
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000014712"
FT   DOMAIN          32..117
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          122..207
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          225..311
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          316..400
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          406..493
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          497..586
FT                   /note="Ig-like C2-type 6"
FT   DOMAIN          599..697
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          702..799
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          804..899
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          900..995
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          685..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           1000
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        466
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        705
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        764
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        858
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        893
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        911
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        929
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        954
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        144..194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        247..295
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        337..384
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        429..477
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        519..576
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         1..744
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12202991"
FT                   /id="VSP_011961"
FT   VAR_SEQ         1..328
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_044270"
FT   VAR_SEQ         555
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_011962"
FT   VARIANT         176
FT                   /note="T -> P (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035507"
FT   VARIANT         420
FT                   /note="K -> N (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035508"
SQ   SEQUENCE   1026 AA;  113454 MW;  2B53D15665B4287B CRC64;
     MRLPWELLVL QSFILCLADD STLHGPIFIQ EPSPVMFPLD SEEKKVKLNC EVKGNPKPHI
     RWKLNGTDVD TGMDFRYSVV EGSLLINNPN KTQDAGTYQC TATNSFGTIV SREAKLQFAY
     LDNFKTRTRS TVSVRRGQGM VLLCGPPPHS GELSYAWIFN EYPSYQDNRR FVSQETGNLY
     IAKVEKSDVG NYTCVVTNTV TNHKVLGPPT PLILRNDGVM GEYEPKIEVQ FPETVPTAKG
     ATVKLECFAL GNPVPTIIWR RADGKPIARK ARRHKSNGIL EIPNFQQEDA GLYECVAENS
     RGKNVARGQL TFYAQPNWIQ KINDIHVAME ENVFWECKAN GRPKPTYKWL KNGEPLLTRD
     RIQIEQGTLN ITIVNLSDAG MYQCLAENKH GVIFSNAELS VIAVGPDFSR TLLKRVTLVK
     VGGEVVIECK PKASPKPVYT WKKGRDILKE NERITISEDG NLRIINVTKS DAGSYTCIAT
     NHFGTASSTG NLVVKDPTRV MVPPSSMDVT VGESIVLPCQ VTHDHSLDIV FTWSFNGHLI
     DFDRDGDHFE RVGGQDSAGD LMIRNIQLKH AGKYVCMVQT SVDRLSAAAD LIVRGPPGPP
     EAVTIDEITD TTAQLSWRPG PDNHSPITMY VIQARTPFSV GWQAVSTVPE LIDGKTFTAT
     VVGLNPWVEY EFRTVAANVI GIGEPSRPSE KRRTEEALPE VTPANVSGGG GSKSELVITW
     ETVPEELQNG RGFGYVVAFR PYGKMIWMLT VLASADASRY VFRNESVHPF SPFEVKVGVF
     NNKGEGPFSP TTVVYSAEEE PTKPPASIFA RSLSATDIEV FWASPLEKNR GRIQGYEVKY
     WRHEDKEENA RKIRTVGNQT STKITNLKGS VLYHLAVKAY NSAGTGPSSA TVNVTTRKPP
     PSQPPGNIIW NSSDSKIILN WDQVKALDNE SEVKGYKVLY RWNRQSSTSV IETNKTSVEL
     SLPFDEDYII EIKPFSDGGD GSSSEQIRIP KISNAYARGS GASTSNACTL SAISTIMISL
     TARSSL
//