EPCAM_HUMAN
ID EPCAM_HUMAN Reviewed; 314 AA.
AC P16422; P18180; Q6FG26; Q6FG49; Q96C47; Q9UCD0;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Epithelial cell adhesion molecule;
DE Short=Ep-CAM;
DE AltName: Full=Adenocarcinoma-associated antigen;
DE AltName: Full=Cell surface glycoprotein Trop-1;
DE AltName: Full=Epithelial cell surface antigen;
DE AltName: Full=Epithelial glycoprotein;
DE Short=EGP;
DE AltName: Full=Epithelial glycoprotein 314;
DE Short=EGP314;
DE Short=hEGP314;
DE AltName: Full=KS 1/4 antigen;
DE AltName: Full=KSA;
DE AltName: Full=Major gastrointestinal tumor-associated protein GA733-2;
DE AltName: Full=Tumor-associated calcium signal transducer 1;
DE AltName: CD_antigen=CD326;
DE Flags: Precursor;
GN Name=EPCAM; Synonyms=GA733-2, M1S2, M4S1, MIC18, TACSTD1, TROP1;
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], AND VARIANT THR-115.
RC TISSUE=Lung adenocarcinoma;
RX PubMed=2463074;
RA Strnad J., Hamilton A.E., Beavers L.S., Gamboa G.C., Apelgren L.D.,
RA Taber L.D., Sportsman J.R., Bumol T.F., Sharp J.D., Gadski R.A.;
RT "Molecular cloning and characterization of a human
RT adenocarcinoma/epithelial cell surface antigen complementary DNA.";
RL Cancer Res. 49:314-317(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-115.
RX PubMed=2469722;
RA Perez M.S., Walker L.E.;
RT "Isolation and characterization of a cDNA encoding the KS1/4 epithelial
RT carcinoma marker.";
RL J. Immunol. 142:3662-3667(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-115.
RX PubMed=2108441; DOI=10.1073/pnas.87.7.2755;
RA Simon B., Podolsky D.K., Moldenhauer G., Isselbacher K.J.,
RA Gattoni-Celli S., Brand S.J.;
RT "Epithelial glycoprotein is a member of a family of epithelial cell surface
RT antigens homologous to nidogen, a matrix adhesion protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2755-2759(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon carcinoma;
RX PubMed=2333300; DOI=10.1073/pnas.87.9.3542;
RA Szala S., Froehlich M., Scollon M., Kasai Y., Steplewski Z., Koprowski H.,
RA Linnenbach A.J.;
RT "Molecular cloning of cDNA for the carcinoma-associated antigen GA733-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3542-3546(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lymphoma;
RX PubMed=8382772; DOI=10.1128/mcb.13.3.1507-1515.1993;
RA Linnenbach A.J., Seng B.A., Wu S., Robbins S., Scollon M., Pyrc J.J.,
RA Druck T., Huebner K.;
RT "Retroposition in a family of carcinoma-associated antigen genes.";
RL Mol. Cell. Biol. 13:1507-1515(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-115.
RC TISSUE=Ovary;
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 [10]
RP PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-126.
RC TISSUE=Placenta;
RX PubMed=2911574; DOI=10.1073/pnas.86.1.27;
RA Linnenbach A.J., Wojcierowski J., Wu S., Pyrc J.J., Ross A.H.,
RA Dietzschold B., Speicher D., Koprowski H.;
RT "Sequence investigation of the major gastrointestinal tumor-associated
RT antigen gene family, GA733.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:27-31(1989).
RN [11]
RP PROTEIN SEQUENCE OF 82-100, AND SUBUNIT.
RX PubMed=7693697; DOI=10.1016/s0021-9258(20)80515-8;
RA Bjoerk P., Joensson U., Svedberg H., Larsson K., Lind P., Dillner J.,
RA Hedlund G., Dohlsten M., Kalland T.;
RT "Isolation, partial characterization, and molecular cloning of a human
RT colon adenocarcinoma cell-surface glycoprotein recognized by the C215 mouse
RT monoclonal antibody.";
RL J. Biol. Chem. 268:24232-24241(1993).
RN [12]
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-74 AND ASN-111.
RX PubMed=11080501; DOI=10.1074/jbc.m008839200;
RA Chong J.M., Speicher D.W.;
RT "Determination of disulfide bond assignments and N-glycosylation sites of
RT the human gastrointestinal carcinoma antigen GA733-2 (CO17-1A, EGP, KS1-4,
RT KSA, and Ep-CAM).";
RL J. Biol. Chem. 276:5804-5813(2001).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15195135; DOI=10.1038/sj.onc.1207610;
RA Muenz M., Kieu C., Mack B., Schmitt B., Zeidler R., Gires O.;
RT "The carcinoma-associated antigen EpCAM upregulates c-myc and induces cell
RT proliferation.";
RL Oncogene 23:5748-5758(2004).
RN [14]
RP FUNCTION.
RX PubMed=15922867; DOI=10.1016/j.canlet.2004.11.048;
RA Muenz M., Zeidler R., Gires O.;
RT "The tumour-associated antigen EpCAM upregulates the fatty acid binding
RT protein E-FABP.";
RL Cancer Lett. 225:151-157(2005).
RN [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CLDN7.
RX PubMed=16054130; DOI=10.1016/j.yexcr.2005.06.013;
RA Ladwein M., Pape U.F., Schmidt D.S., Schnoelzer M., Fiedler S.,
RA Langbein L., Franke W.W., Moldenhauer G., Zoeller M.;
RT "The cell-cell adhesion molecule EpCAM interacts directly with the tight
RT junction protein claudin-7.";
RL Exp. Cell Res. 309:345-357(2005).
RN [16]
RP GLYCOSYLATION AT ASN-74; ASN-111 AND ASN-198, AND MUTAGENESIS OF ASN-74;
RP ASN-111 AND ASN-198.
RX PubMed=18508581; DOI=10.2741/3075;
RA Munz M., Fellinger K., Hofmann T., Schmitt B., Gires O.;
RT "Glycosylation is crucial for stability of tumour and cancer stem cell
RT antigen EpCAM.";
RL Front. Biosci. 13:5195-5201(2008).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [18]
RP INVOLVEMENT IN HNPCC8.
RX PubMed=19098912; DOI=10.1038/ng.283;
RA Ligtenberg M.J., Kuiper R.P., Chan T.L., Goossens M., Hebeda K.M.,
RA Voorendt M., Lee T.Y., Bodmer D., Hoenselaar E., Hendriks-Cornelissen S.J.,
RA Tsui W.Y., Kong C.K., Brunner H.G., van Kessel A.G., Yuen S.T.,
RA van Krieken J.H., Leung S.Y., Hoogerbrugge N.;
RT "Heritable somatic methylation and inactivation of MSH2 in families with
RT Lynch syndrome due to deletion of the 3' exons of TACSTD1.";
RL Nat. Genet. 41:112-117(2009).
RN [19]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20064925; DOI=10.1074/jbc.m109.077081;
RA Lu T.Y., Lu R.M., Liao M.Y., Yu J., Chung C.H., Kao C.F., Wu H.C.;
RT "Epithelial cell adhesion molecule regulation is associated with the
RT maintenance of the undifferentiated phenotype of human embryonic stem
RT cells.";
RL J. Biol. Chem. 285:8719-8732(2010).
RN [20]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19785009; DOI=10.1002/stem.221;
RA Ng V.Y., Ang S.N., Chan J.X., Choo A.B.;
RT "Characterization of epithelial cell adhesion molecule as a surface marker
RT on undifferentiated human embryonic stem cells.";
RL Stem Cells 28:29-35(2010).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP VARIANT DIAR5 TYR-66.
RX PubMed=18572020; DOI=10.1053/j.gastro.2008.05.036;
RA Sivagnanam M., Mueller J.L., Lee H., Chen Z., Nelson S.F., Turner D.,
RA Zlotkin S.H., Pencharz P.B., Ngan B.Y., Libiger O., Schork N.J.,
RA Lavine J.E., Taylor S., Newbury R.O., Kolodner R.D., Hoffman H.M.;
RT "Identification of EpCAM as the gene for congenital tufting enteropathy.";
RL Gastroenterology 135:429-437(2008).
CC -!- FUNCTION: May act as a physical homophilic interaction molecule between
CC intestinal epithelial cells (IECs) and intraepithelial lymphocytes
CC (IELs) at the mucosal epithelium for providing immunological barrier as
CC a first line of defense against mucosal infection. Plays a role in
CC embryonic stem cells proliferation and differentiation. Up-regulates
CC the expression of FABP5, MYC and cyclins A and E.
CC {ECO:0000269|PubMed:15195135, ECO:0000269|PubMed:15922867,
CC ECO:0000269|PubMed:19785009, ECO:0000269|PubMed:20064925}.
CC -!- SUBUNIT: Monomer. Interacts with phosphorylated CLDN7.
CC {ECO:0000269|PubMed:16054130, ECO:0000269|PubMed:7693697}.
CC -!- INTERACTION:
CC P16422; P27797: CALR; NbExp=3; IntAct=EBI-1171184, EBI-1049597;
CC P16422; P12830: CDH1; NbExp=3; IntAct=EBI-1171184, EBI-727477;
CC P16422; Q15078: CDK5R1; NbExp=3; IntAct=EBI-1171184, EBI-746189;
CC P16422; P36957: DLST; NbExp=3; IntAct=EBI-1171184, EBI-351007;
CC P16422; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-1171184, EBI-1055945;
CC -!- SUBCELLULAR LOCATION: Lateral cell membrane
CC {ECO:0000269|PubMed:15195135, ECO:0000269|PubMed:16054130,
CC ECO:0000269|PubMed:19785009}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16054130}. Cell junction, tight junction
CC {ECO:0000269|PubMed:16054130}. Note=Colocalizes with CLDN7 at the
CC lateral cell membrane and tight junction.
CC {ECO:0000269|PubMed:16054130}.
CC -!- TISSUE SPECIFICITY: Highly and selectively expressed by
CC undifferentiated rather than differentiated embryonic stem cells (ESC).
CC Levels rapidly diminish as soon as ESC's differentiate (at protein
CC levels). Expressed in almost all epithelial cell membranes but not on
CC mesodermal or neural cell membranes. Found on the surface of
CC adenocarcinoma. {ECO:0000269|PubMed:20064925}.
CC -!- PTM: Hyperglycosylated in carcinoma tissue as compared with autologous
CC normal epithelia. Glycosylation at Asn-198 is crucial for protein
CC stability. {ECO:0000269|PubMed:11080501, ECO:0000269|PubMed:18508581,
CC ECO:0000269|PubMed:19159218}.
CC -!- DISEASE: Diarrhea 5, with tufting enteropathy, congenital (DIAR5)
CC [MIM:613217]: An intractable diarrhea of infancy characterized by
CC villous atrophy and absence of inflammation, with intestinal epithelial
CC cell dysplasia manifesting as focal epithelial tufts in the duodenum
CC and jejunum. {ECO:0000269|PubMed:18572020}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Hereditary non-polyposis colorectal cancer 8 (HNPCC8)
CC [MIM:613244]: An autosomal dominant disease associated with marked
CC increase in cancer susceptibility. It is characterized by a familial
CC predisposition to early-onset colorectal carcinoma (CRC) and extra-
CC colonic tumors of the gastrointestinal, urological and female
CC reproductive tracts. HNPCC is reported to be the most common form of
CC inherited colorectal cancer in the Western world. Clinically, HNPCC is
CC often divided into two subgroups. Type I is characterized by hereditary
CC predisposition to colorectal cancer, a young age of onset, and
CC carcinoma observed in the proximal colon. Type II is characterized by
CC increased risk for cancers in certain tissues such as the uterus,
CC ovary, breast, stomach, small intestine, skin, and larynx in addition
CC to the colon. Diagnosis of classical HNPCC is based on the Amsterdam
CC criteria: 3 or more relatives affected by colorectal cancer, one a
CC first degree relative of the other two; 2 or more generation affected;
CC 1 or more colorectal cancers presenting before 50 years of age;
CC exclusion of hereditary polyposis syndromes. The term 'suspected HNPCC'
CC or 'incomplete HNPCC' can be used to describe families who do not or
CC only partially fulfill the Amsterdam criteria, but in whom a genetic
CC basis for colon cancer is strongly suspected.
CC {ECO:0000269|PubMed:19098912}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. HNPCC8 results from
CC heterozygous deletion of 3-prime exons of EPCAM and intergenic regions
CC directly upstream of MSH2, resulting in transcriptional read-through
CC and epigenetic silencing of MSH2 in tissues expressing EPCAM.
CC -!- SIMILARITY: Belongs to the EPCAM family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TACSTD1ID42459ch2p21.html";
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DR EMBL; M32325; AAA36151.1; -; mRNA.
DR EMBL; X14758; CAA32870.1; -; mRNA.
DR EMBL; M26481; AAA59543.1; -; mRNA.
DR EMBL; M32306; AAA35723.1; -; mRNA.
DR EMBL; M33011; AAA35861.1; -; mRNA.
DR EMBL; M93036; AAB00775.1; -; Genomic_DNA.
DR EMBL; M93029; AAB00775.1; JOINED; Genomic_DNA.
DR EMBL; M93030; AAB00775.1; JOINED; Genomic_DNA.
DR EMBL; M93031; AAB00775.1; JOINED; Genomic_DNA.
DR EMBL; M93032; AAB00775.1; JOINED; Genomic_DNA.
DR EMBL; M93033; AAB00775.1; JOINED; Genomic_DNA.
DR EMBL; M93034; AAB00775.1; JOINED; Genomic_DNA.
DR EMBL; M93035; AAB00775.1; JOINED; Genomic_DNA.
DR EMBL; CR542259; CAG47055.1; -; mRNA.
DR EMBL; CR542283; CAG47078.1; -; mRNA.
DR EMBL; AC079775; AAY15095.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00218.1; -; Genomic_DNA.
DR EMBL; BC014785; AAH14785.1; -; mRNA.
DR CCDS; CCDS1833.1; -.
DR PIR; B48149; B48149.
DR RefSeq; NP_002345.2; NM_002354.2.
DR PDB; 4MZV; X-ray; 1.86 A; A=24-265.
DR PDB; 6I07; X-ray; 2.35 A; C/D=24-265.
DR PDBsum; 4MZV; -.
DR PDBsum; 6I07; -.
DR AlphaFoldDB; P16422; -.
DR SMR; P16422; -.
DR BioGRID; 110250; 18.
DR CORUM; P16422; -.
DR IntAct; P16422; 11.
DR MINT; P16422; -.
DR STRING; 9606.ENSP00000263735; -.
DR ChEMBL; CHEMBL3580493; -.
DR DrugBank; DB06607; Catumaxomab.
DR DrugBank; DB11075; Hypromellose.
DR DrugBank; DB05831; ING-1.
DR DrugBank; DB05319; Oportuzumab monatox.
DR DrugBank; DB09336; Technetium Tc-99m nofetumomab merpentan.
DR GlyConnect; 1217; 34 N-Linked glycans (3 sites).
DR GlyGen; P16422; 4 sites, 34 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P16422; -.
DR MetOSite; P16422; -.
DR PhosphoSitePlus; P16422; -.
DR BioMuta; EPCAM; -.
DR DMDM; 160266056; -.
DR CPTAC; CPTAC-502; -.
DR CPTAC; CPTAC-503; -.
DR EPD; P16422; -.
DR jPOST; P16422; -.
DR MassIVE; P16422; -.
DR MaxQB; P16422; -.
DR PaxDb; P16422; -.
DR PeptideAtlas; P16422; -.
DR PRIDE; P16422; -.
DR ProteomicsDB; 53359; -.
DR ABCD; P16422; 18 sequenced antibodies.
DR Antibodypedia; 3539; 4504 antibodies from 59 providers.
DR DNASU; 4072; -.
DR Ensembl; ENST00000263735.9; ENSP00000263735.4; ENSG00000119888.11.
DR GeneID; 4072; -.
DR KEGG; hsa:4072; -.
DR MANE-Select; ENST00000263735.9; ENSP00000263735.4; NM_002354.3; NP_002345.2.
DR UCSC; uc002rvx.4; human.
DR CTD; 4072; -.
DR DisGeNET; 4072; -.
DR GeneCards; EPCAM; -.
DR GeneReviews; EPCAM; -.
DR HGNC; HGNC:11529; EPCAM.
DR HPA; ENSG00000119888; Tissue enhanced (intestine).
DR MalaCards; EPCAM; -.
DR MIM; 185535; gene.
DR MIM; 613217; phenotype.
DR MIM; 613244; phenotype.
DR neXtProt; NX_P16422; -.
DR OpenTargets; ENSG00000119888; -.
DR Orphanet; 92050; Congenital tufting enteropathy.
DR Orphanet; 144; Lynch syndrome.
DR PharmGKB; PA35493; -.
DR VEuPathDB; HostDB:ENSG00000119888; -.
DR eggNOG; ENOG502QVSU; Eukaryota.
DR GeneTree; ENSGT00390000018245; -.
DR HOGENOM; CLU_075326_0_0_1; -.
DR InParanoid; P16422; -.
DR OMA; NGTTTCW; -.
DR OrthoDB; 1017141at2759; -.
DR PhylomeDB; P16422; -.
DR TreeFam; TF332767; -.
DR BRENDA; 2.4.1.37; 2681.
DR BRENDA; 2.4.1.40; 2681.
DR PathwayCommons; P16422; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR SignaLink; P16422; -.
DR SIGNOR; P16422; -.
DR BioGRID-ORCS; 4072; 34 hits in 1078 CRISPR screens.
DR ChiTaRS; EPCAM; human.
DR GeneWiki; Epithelial_cell_adhesion_molecule; -.
DR GenomeRNAi; 4072; -.
DR Pharos; P16422; Tbio.
DR PRO; PR:P16422; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P16422; protein.
DR Bgee; ENSG00000119888; Expressed in jejunal mucosa and 174 other tissues.
DR ExpressionAtlas; P16422; baseline and differential.
DR Genevisible; P16422; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.800.10; -; 1.
DR InterPro; IPR043406; EPCAM/Trop-2.
DR InterPro; IPR041630; EpCAM_N.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR PANTHER; PTHR14168; PTHR14168; 1.
DR Pfam; PF18635; EpCAM_N; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR SMART; SM00211; TY; 1.
DR SUPFAM; SSF57610; SSF57610; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Direct protein sequencing;
KW Disease variant; Disulfide bond; Glycoprotein;
KW Hereditary nonpolyposis colorectal cancer; Membrane; Reference proteome;
KW Repeat; Signal; Tight junction; Transmembrane; Transmembrane helix;
KW Tumor antigen.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..314
FT /note="Epithelial cell adhesion molecule"
FT /id="PRO_0000022467"
FT TOPO_DOM 24..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 63..135
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:11080501,
FT ECO:0000269|PubMed:18508581"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11080501,
FT ECO:0000269|PubMed:18508581"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18508581,
FT ECO:0000269|PubMed:19159218"
FT DISULFID 27..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:11080501"
FT DISULFID 29..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:11080501"
FT DISULFID 38..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:11080501"
FT DISULFID 66..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:11080501"
FT DISULFID 110..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:11080501"
FT DISULFID 118..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:11080501"
FT VARIANT 66
FT /note="C -> Y (in DIAR5; dbSNP:rs267606785)"
FT /evidence="ECO:0000269|PubMed:18572020"
FT /id="VAR_063829"
FT VARIANT 115
FT /note="M -> T (in dbSNP:rs1126497)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2108441, ECO:0000269|PubMed:2463074,
FT ECO:0000269|PubMed:2469722"
FT /id="VAR_018329"
FT MUTAGEN 74
FT /note="N->A: Changed glycosylation pattern. Complete loss
FT of glycosylation and substantial decrease in protein
FT expression; when associated with A-111 and A-198."
FT /evidence="ECO:0000269|PubMed:18508581"
FT MUTAGEN 111
FT /note="N->A: Changed glycosylation pattern. Complete loss
FT of glycosylation and substantial decrease in protein
FT expression; when associated with A-74 and A-198."
FT /evidence="ECO:0000269|PubMed:18508581"
FT MUTAGEN 198
FT /note="N->A: Decreased glycosyation, reduced protein
FT stability and significant decrease in protein expression.
FT Complete loss of glycosylation and substantial decrease in
FT protein expression; when associated with A-74 and A-111."
FT /evidence="ECO:0000269|PubMed:18508581"
FT CONFLICT 277
FT /note="I -> M (in Ref. 1; AAA36151/CAA32870 and 2;
FT AAA59543)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="K -> R (in Ref. 6; CAG47055)"
FT /evidence="ECO:0000305"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:4MZV"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:4MZV"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4MZV"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:4MZV"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:4MZV"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:4MZV"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:4MZV"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:4MZV"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4MZV"
FT STRAND 141..150
FT /evidence="ECO:0007829|PDB:4MZV"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:4MZV"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:4MZV"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:4MZV"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:4MZV"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:4MZV"
FT HELIX 209..220
FT /evidence="ECO:0007829|PDB:4MZV"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:4MZV"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:6I07"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:4MZV"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:4MZV"
SQ SEQUENCE 314 AA; 34932 MW; 023FCE418B2F1079 CRC64;
MAPPQVLAFG LLLAAATATF AAAQEECVCE NYKLAVNCFV NNNRQCQCTS VGAQNTVICS
KLAAKCLVMK AEMNGSKLGR RAKPEGALQN NDGLYDPDCD ESGLFKAKQC NGTSMCWCVN
TAGVRRTDKD TEITCSERVR TYWIIIELKH KAREKPYDSK SLRTALQKEI TTRYQLDPKF
ITSILYENNV ITIDLVQNSS QKTQNDVDIA DVAYYFEKDV KGESLFHSKK MDLTVNGEQL
DLDPGQTLIY YVDEKAPEFS MQGLKAGVIA VIVVVVIAVV AGIVVLVISR KKRMAKYEKA
EIKEMGEMHR ELNA
