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Epithelial cell adhesion molecule (Ep-CAM) (Adenocarcinoma-associated antigen) (Cell surface glycoprotein Trop-1) (Epithelial cell surface antigen) (Epithelial glycoprotein) (EGP) (Epithelial glycoprotein 314) (EGP314) (hEGP314) (KS 1/4 antigen) (KSA) (Major gastrointestinal tumor-associated protein GA733-2) (Tumor-associated calcium signal transducer 1) (CD antigen CD326)

 EPCAM_HUMAN             Reviewed;         314 AA.
P16422; P18180; Q6FG26; Q6FG49; Q96C47; Q9UCD0;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 2.
25-OCT-2017, entry version 173.
RecName: Full=Epithelial cell adhesion molecule;
Short=Ep-CAM;
AltName: Full=Adenocarcinoma-associated antigen;
AltName: Full=Cell surface glycoprotein Trop-1;
AltName: Full=Epithelial cell surface antigen;
AltName: Full=Epithelial glycoprotein;
Short=EGP;
AltName: Full=Epithelial glycoprotein 314;
Short=EGP314;
Short=hEGP314;
AltName: Full=KS 1/4 antigen;
AltName: Full=KSA;
AltName: Full=Major gastrointestinal tumor-associated protein GA733-2;
AltName: Full=Tumor-associated calcium signal transducer 1;
AltName: CD_antigen=CD326;
Flags: Precursor;
Name=EPCAM; Synonyms=GA733-2, M1S2, M4S1, MIC18, TACSTD1, TROP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-115.
TISSUE=Lung adenocarcinoma;
PubMed=2463074;
Strnad J., Hamilton A.E., Beavers L.S., Gamboa G.C., Apelgren L.D.,
Taber L.D., Sportsman J.R., Bumol T.F., Sharp J.D., Gadski R.A.;
"Molecular cloning and characterization of a human
adenocarcinoma/epithelial cell surface antigen complementary DNA.";
Cancer Res. 49:314-317(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-115.
PubMed=2469722;
Perez M.S., Walker L.E.;
"Isolation and characterization of a cDNA encoding the KS1/4
epithelial carcinoma marker.";
J. Immunol. 142:3662-3667(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-115.
PubMed=2108441; DOI=10.1073/pnas.87.7.2755;
Simon B., Podolsky D.K., Moldenhauer G., Isselbacher K.J.,
Gattoni-Celli S., Brand S.J.;
"Epithelial glycoprotein is a member of a family of epithelial cell
surface antigens homologous to nidogen, a matrix adhesion protein.";
Proc. Natl. Acad. Sci. U.S.A. 87:2755-2759(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Colon carcinoma;
PubMed=2333300; DOI=10.1073/pnas.87.9.3542;
Szala S., Froehlich M., Scollon M., Kasai Y., Steplewski Z.,
Koprowski H., Linnenbach A.J.;
"Molecular cloning of cDNA for the carcinoma-associated antigen GA733-
2.";
Proc. Natl. Acad. Sci. U.S.A. 87:3542-3546(1990).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lymphoma;
PubMed=8382772; DOI=10.1128/MCB.13.3.1507;
Linnenbach A.J., Seng B.A., Wu S., Robbins S., Scollon M., Pyrc J.J.,
Druck T., Huebner K.;
"Retroposition in a family of carcinoma-associated antigen genes.";
Mol. Cell. Biol. 13:1507-1515(1993).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-115.
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-126.
TISSUE=Placenta;
PubMed=2911574; DOI=10.1073/pnas.86.1.27;
Linnenbach A.J., Wojcierowski J., Wu S., Pyrc J.J., Ross A.H.,
Dietzschold B., Speicher D., Koprowski H.;
"Sequence investigation of the major gastrointestinal tumor-associated
antigen gene family, GA733.";
Proc. Natl. Acad. Sci. U.S.A. 86:27-31(1989).
[11]
PROTEIN SEQUENCE OF 82-100, AND SUBUNIT.
PubMed=7693697;
Bjoerk P., Joensson U., Svedberg H., Larsson K., Lind P., Dillner J.,
Hedlund G., Dohlsten M., Kalland T.;
"Isolation, partial characterization, and molecular cloning of a human
colon adenocarcinoma cell-surface glycoprotein recognized by the C215
mouse monoclonal antibody.";
J. Biol. Chem. 268:24232-24241(1993).
[12]
DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-74 AND ASN-111.
PubMed=11080501; DOI=10.1074/jbc.M008839200;
Chong J.M., Speicher D.W.;
"Determination of disulfide bond assignments and N-glycosylation sites
of the human gastrointestinal carcinoma antigen GA733-2 (CO17-1A, EGP,
KS1-4, KSA, and Ep-CAM).";
J. Biol. Chem. 276:5804-5813(2001).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15195135; DOI=10.1038/sj.onc.1207610;
Muenz M., Kieu C., Mack B., Schmitt B., Zeidler R., Gires O.;
"The carcinoma-associated antigen EpCAM upregulates c-myc and induces
cell proliferation.";
Oncogene 23:5748-5758(2004).
[14]
FUNCTION.
PubMed=15922867; DOI=10.1016/j.canlet.2004.11.048;
Muenz M., Zeidler R., Gires O.;
"The tumour-associated antigen EpCAM upregulates the fatty acid
binding protein E-FABP.";
Cancer Lett. 225:151-157(2005).
[15]
SUBCELLULAR LOCATION, AND INTERACTION WITH CLDN7.
PubMed=16054130; DOI=10.1016/j.yexcr.2005.06.013;
Ladwein M., Pape U.F., Schmidt D.S., Schnoelzer M., Fiedler S.,
Langbein L., Franke W.W., Moldenhauer G., Zoeller M.;
"The cell-cell adhesion molecule EpCAM interacts directly with the
tight junction protein claudin-7.";
Exp. Cell Res. 309:345-357(2005).
[16]
GLYCOSYLATION AT ASN-74; ASN-111 AND ASN-198, AND MUTAGENESIS OF
ASN-74; ASN-111 AND ASN-198.
PubMed=18508581; DOI=10.2741/3075;
Munz M., Fellinger K., Hofmann T., Schmitt B., Gires O.;
"Glycosylation is crucial for stability of tumour and cancer stem cell
antigen EpCAM.";
Front. Biosci. 13:5195-5201(2008).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[18]
INVOLVEMENT IN HNPCC8.
PubMed=19098912; DOI=10.1038/ng.283;
Ligtenberg M.J., Kuiper R.P., Chan T.L., Goossens M., Hebeda K.M.,
Voorendt M., Lee T.Y., Bodmer D., Hoenselaar E.,
Hendriks-Cornelissen S.J., Tsui W.Y., Kong C.K., Brunner H.G.,
van Kessel A.G., Yuen S.T., van Krieken J.H., Leung S.Y.,
Hoogerbrugge N.;
"Heritable somatic methylation and inactivation of MSH2 in families
with Lynch syndrome due to deletion of the 3' exons of TACSTD1.";
Nat. Genet. 41:112-117(2009).
[19]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=20064925; DOI=10.1074/jbc.M109.077081;
Lu T.Y., Lu R.M., Liao M.Y., Yu J., Chung C.H., Kao C.F., Wu H.C.;
"Epithelial cell adhesion molecule regulation is associated with the
maintenance of the undifferentiated phenotype of human embryonic stem
cells.";
J. Biol. Chem. 285:8719-8732(2010).
[20]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19785009; DOI=10.1002/stem.221;
Ng V.Y., Ang S.N., Chan J.X., Choo A.B.;
"Characterization of epithelial cell adhesion molecule as a surface
marker on undifferentiated human embryonic stem cells.";
Stem Cells 28:29-35(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
VARIANT DIAR5 TYR-66.
PubMed=18572020; DOI=10.1053/j.gastro.2008.05.036;
Sivagnanam M., Mueller J.L., Lee H., Chen Z., Nelson S.F., Turner D.,
Zlotkin S.H., Pencharz P.B., Ngan B.Y., Libiger O., Schork N.J.,
Lavine J.E., Taylor S., Newbury R.O., Kolodner R.D., Hoffman H.M.;
"Identification of EpCAM as the gene for congenital tufting
enteropathy.";
Gastroenterology 135:429-437(2008).
-!- FUNCTION: May act as a physical homophilic interaction molecule
between intestinal epithelial cells (IECs) and intraepithelial
lymphocytes (IELs) at the mucosal epithelium for providing
immunological barrier as a first line of defense against mucosal
infection. Plays a role in embryonic stem cells proliferation and
differentiation. Up-regulates the expression of FABP5, MYC and
cyclins A and E. {ECO:0000269|PubMed:15195135,
ECO:0000269|PubMed:15922867, ECO:0000269|PubMed:19785009,
ECO:0000269|PubMed:20064925}.
-!- SUBUNIT: Monomer. Interacts with phosphorylated CLDN7.
{ECO:0000269|PubMed:16054130, ECO:0000269|PubMed:7693697}.
-!- SUBCELLULAR LOCATION: Lateral cell membrane
{ECO:0000269|PubMed:15195135, ECO:0000269|PubMed:16054130,
ECO:0000269|PubMed:19785009}; Single-pass type I membrane protein
{ECO:0000269|PubMed:16054130}. Cell junction, tight junction
{ECO:0000269|PubMed:16054130}. Note=Colocalizes with CLDN7 at the
lateral cell membrane and tight junction.
{ECO:0000269|PubMed:16054130}.
-!- TISSUE SPECIFICITY: Highly and selectively expressed by
undifferentiated rather than differentiated embryonic stem cells
(ESC). Levels rapidly diminish as soon as ESC's differentiate (at
protein levels). Expressed in almost all epithelial cell membranes
but not on mesodermal or neural cell membranes. Found on the
surface of adenocarcinoma. {ECO:0000269|PubMed:20064925}.
-!- PTM: Hyperglycosylated in carcinoma tissue as compared with
autologous normal epithelia. Glycosylation at Asn-198 is crucial
for protein stability. {ECO:0000269|PubMed:11080501,
ECO:0000269|PubMed:18508581, ECO:0000269|PubMed:19159218}.
-!- DISEASE: Diarrhea 5, with tufting enteropathy, congenital (DIAR5)
[MIM:613217]: An intractable diarrhea of infancy characterized by
villous atrophy and absence of inflammation, with intestinal
epithelial cell dysplasia manifesting as focal epithelial tufts in
the duodenum and jejunum. {ECO:0000269|PubMed:18572020}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Hereditary non-polyposis colorectal cancer 8 (HNPCC8)
[MIM:613244]: An autosomal dominant disease associated with marked
increase in cancer susceptibility. It is characterized by a
familial predisposition to early-onset colorectal carcinoma (CRC)
and extra-colonic tumors of the gastrointestinal, urological and
female reproductive tracts. HNPCC is reported to be the most
common form of inherited colorectal cancer in the Western world.
Clinically, HNPCC is often divided into two subgroups. Type I is
characterized by hereditary predisposition to colorectal cancer, a
young age of onset, and carcinoma observed in the proximal colon.
Type II is characterized by increased risk for cancers in certain
tissues such as the uterus, ovary, breast, stomach, small
intestine, skin, and larynx in addition to the colon. Diagnosis of
classical HNPCC is based on the Amsterdam criteria: 3 or more
relatives affected by colorectal cancer, one a first degree
relative of the other two; 2 or more generation affected; 1 or
more colorectal cancers presenting before 50 years of age;
exclusion of hereditary polyposis syndromes. The term 'suspected
HNPCC' or 'incomplete HNPCC' can be used to describe families who
do not or only partially fulfill the Amsterdam criteria, but in
whom a genetic basis for colon cancer is strongly suspected.
{ECO:0000269|PubMed:19098912}. Note=The disease is caused by
mutations affecting the gene represented in this entry. HNPCC8
results from heterozygous deletion of 3-prime exons of EPCAM and
intergenic regions directly upstream of MSH2, resulting in
transcriptional read-through and epigenetic silencing of MSH2 in
tissues expressing EPCAM.
-!- SIMILARITY: Belongs to the EPCAM family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TACSTD1ID42459ch2p21.html";
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EMBL; M32325; AAA36151.1; -; mRNA.
EMBL; X14758; CAA32870.1; -; mRNA.
EMBL; M26481; AAA59543.1; -; mRNA.
EMBL; M32306; AAA35723.1; -; mRNA.
EMBL; M33011; AAA35861.1; -; mRNA.
EMBL; M93036; AAB00775.1; -; Genomic_DNA.
EMBL; M93029; AAB00775.1; JOINED; Genomic_DNA.
EMBL; M93030; AAB00775.1; JOINED; Genomic_DNA.
EMBL; M93031; AAB00775.1; JOINED; Genomic_DNA.
EMBL; M93032; AAB00775.1; JOINED; Genomic_DNA.
EMBL; M93033; AAB00775.1; JOINED; Genomic_DNA.
EMBL; M93034; AAB00775.1; JOINED; Genomic_DNA.
EMBL; M93035; AAB00775.1; JOINED; Genomic_DNA.
EMBL; CR542259; CAG47055.1; -; mRNA.
EMBL; CR542283; CAG47078.1; -; mRNA.
EMBL; AC079775; AAY15095.1; -; Genomic_DNA.
EMBL; CH471053; EAX00218.1; -; Genomic_DNA.
EMBL; BC014785; AAH14785.1; -; mRNA.
CCDS; CCDS1833.1; -.
PIR; B48149; B48149.
RefSeq; NP_002345.2; NM_002354.2.
UniGene; Hs.542050; -.
PDB; 4MZV; X-ray; 1.86 A; A=24-265.
PDBsum; 4MZV; -.
ProteinModelPortal; P16422; -.
SMR; P16422; -.
BioGrid; 110250; 5.
IntAct; P16422; 2.
MINT; MINT-4999389; -.
STRING; 9606.ENSP00000263735; -.
ChEMBL; CHEMBL3580493; -.
DrugBank; DB05831; ING-1.
DrugBank; DB05319; oportuzumab monatox.
iPTMnet; P16422; -.
PhosphoSitePlus; P16422; -.
BioMuta; EPCAM; -.
DMDM; 160266056; -.
EPD; P16422; -.
MaxQB; P16422; -.
PaxDb; P16422; -.
PeptideAtlas; P16422; -.
PRIDE; P16422; -.
DNASU; 4072; -.
Ensembl; ENST00000263735; ENSP00000263735; ENSG00000119888.
GeneID; 4072; -.
KEGG; hsa:4072; -.
UCSC; uc002rvx.4; human.
CTD; 4072; -.
DisGeNET; 4072; -.
EuPathDB; HostDB:ENSG00000119888.10; -.
GeneCards; EPCAM; -.
GeneReviews; EPCAM; -.
H-InvDB; HIX0002040; -.
HGNC; HGNC:11529; EPCAM.
HPA; CAB003809; -.
HPA; CAB030012; -.
HPA; CAB055098; -.
HPA; HPA026761; -.
HPA; HPA067463; -.
MalaCards; EPCAM; -.
MIM; 185535; gene.
MIM; 613217; phenotype.
MIM; 613244; phenotype.
neXtProt; NX_P16422; -.
OpenTargets; ENSG00000119888; -.
Orphanet; 144; Hereditary nonpolyposis colon cancer.
Orphanet; 92050; Intestinal epithelial dysplasia.
PharmGKB; PA35493; -.
eggNOG; ENOG410IFI6; Eukaryota.
eggNOG; ENOG4111M3B; LUCA.
GeneTree; ENSGT00390000018245; -.
HOGENOM; HOG000074086; -.
InParanoid; P16422; -.
KO; K06737; -.
PhylomeDB; P16422; -.
TreeFam; TF332767; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
ChiTaRS; EPCAM; human.
GeneWiki; Epithelial_cell_adhesion_molecule; -.
GenomeRNAi; 4072; -.
PRO; PR:P16422; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000119888; -.
CleanEx; HS_EPCAM; -.
ExpressionAtlas; P16422; baseline and differential.
Genevisible; P16422; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IBA:GO_Central.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IEA:Ensembl.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; IDA:UniProtKB.
GO; GO:2000147; P:positive regulation of cell motility; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IMP:UniProtKB.
GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
Gene3D; 4.10.800.10; -; 1.
InterPro; IPR000716; Thyroglobulin_1.
InterPro; IPR036857; Thyroglobulin_1_sf.
Pfam; PF00086; Thyroglobulin_1; 1.
SMART; SM00211; TY; 1.
SUPFAM; SSF57610; SSF57610; 1.
PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Hereditary nonpolyposis colorectal cancer; Membrane;
Polymorphism; Reference proteome; Repeat; Signal; Tight junction;
Transmembrane; Transmembrane helix; Tumor antigen.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 314 Epithelial cell adhesion molecule.
/FTId=PRO_0000022467.
TOPO_DOM 24 265 Extracellular. {ECO:0000255}.
TRANSMEM 266 288 Helical. {ECO:0000255}.
TOPO_DOM 289 314 Cytoplasmic. {ECO:0000255}.
DOMAIN 63 135 Thyroglobulin type-1.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine; partial.
{ECO:0000269|PubMed:11080501,
ECO:0000269|PubMed:18508581}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11080501,
ECO:0000269|PubMed:18508581}.
CARBOHYD 198 198 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18508581,
ECO:0000269|PubMed:19159218}.
DISULFID 27 46 {ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:11080501}.
DISULFID 29 59 {ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:11080501}.
DISULFID 38 48 {ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:11080501}.
DISULFID 66 99 {ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:11080501}.
DISULFID 110 116 {ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:11080501}.
DISULFID 118 135 {ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:11080501}.
VARIANT 66 66 C -> Y (in DIAR5; dbSNP:rs267606785).
{ECO:0000269|PubMed:18572020}.
/FTId=VAR_063829.
VARIANT 115 115 M -> T (in dbSNP:rs1126497).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2108441,
ECO:0000269|PubMed:2463074,
ECO:0000269|PubMed:2469722}.
/FTId=VAR_018329.
MUTAGEN 74 74 N->A: Changed glycosylation pattern.
Complete loss of glycosylation and
substantial decrease in protein
expression; when associated with A-111
and A-198. {ECO:0000269|PubMed:18508581}.
MUTAGEN 111 111 N->A: Changed glycosylation pattern.
Complete loss of glycosylation and
substantial decrease in protein
expression; when associated with A-74 and
A-198. {ECO:0000269|PubMed:18508581}.
MUTAGEN 198 198 N->A: Decreased glycosyation, reduced
protein stability and significant
decrease in protein expression. Complete
loss of glycosylation and substantial
decrease in protein expression; when
associated with A-74 and A-111.
{ECO:0000269|PubMed:18508581}.
CONFLICT 277 277 I -> M (in Ref. 1; AAA36151/CAA32870 and
2; AAA59543). {ECO:0000305}.
CONFLICT 303 303 K -> R (in Ref. 6; CAG47055).
{ECO:0000305}.
STRAND 35 40 {ECO:0000244|PDB:4MZV}.
STRAND 46 50 {ECO:0000244|PDB:4MZV}.
STRAND 56 58 {ECO:0000244|PDB:4MZV}.
HELIX 65 72 {ECO:0000244|PDB:4MZV}.
TURN 73 75 {ECO:0000244|PDB:4MZV}.
STRAND 107 111 {ECO:0000244|PDB:4MZV}.
TURN 112 114 {ECO:0000244|PDB:4MZV}.
STRAND 115 120 {ECO:0000244|PDB:4MZV}.
STRAND 130 132 {ECO:0000244|PDB:4MZV}.
STRAND 141 150 {ECO:0000244|PDB:4MZV}.
HELIX 159 173 {ECO:0000244|PDB:4MZV}.
HELIX 178 180 {ECO:0000244|PDB:4MZV}.
STRAND 181 187 {ECO:0000244|PDB:4MZV}.
STRAND 190 196 {ECO:0000244|PDB:4MZV}.
TURN 199 201 {ECO:0000244|PDB:4MZV}.
HELIX 209 220 {ECO:0000244|PDB:4MZV}.
STRAND 226 228 {ECO:0000244|PDB:4MZV}.
HELIX 244 246 {ECO:0000244|PDB:4MZV}.
STRAND 248 255 {ECO:0000244|PDB:4MZV}.
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


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