CNTN4_HUMAN
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 03-AUG-2022, entry version 159.
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; 5.
DR STRING; 9606.ENSP00000380602; -.
DR GlyConnect; 1156; 25 N-Linked glycans (7 sites).
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; Q8IWV2; -.
DR PeptideAtlas; Q8IWV2; -.
DR PRIDE; Q8IWV2; -.
DR ProteomicsDB; 3420; -.
DR ProteomicsDB; 70904; -. [Q8IWV2-1]
DR ProteomicsDB; 70905; -. [Q8IWV2-2]
DR ProteomicsDB; 70906; -. [Q8IWV2-3]
DR Antibodypedia; 9906; 200 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 CTD; 152330; -.
DR DisGeNET; 152330; -.
DR GeneCards; CNTN4; -.
DR HGNC; HGNC:2174; CNTN4.
DR HPA; ENSG00000144619; Tissue enhanced (parathyroid).
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; KICKAYT; -.
DR OrthoDB; 655902at2759; -.
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 1068 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 153 other tissues.
DR ExpressionAtlas; Q8IWV2; baseline and differential.
DR Genevisible; Q8IWV2; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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: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 Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR043204; Basigin-like.
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; PTHR10075; PTHR10075; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 3.
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 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
