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Epithelial cell adhesion molecule (Ep-CAM) (Tumor-associated calcium signal transducer 1) (CD antigen CD326)

 EPCAM_BOVIN             Reviewed;         314 AA.
Q3T0L5; Q1JP89;
28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 1.
07-NOV-2018, entry version 65.
RecName: Full=Epithelial cell adhesion molecule;
Short=Ep-CAM;
AltName: Full=Tumor-associated calcium signal transducer 1;
AltName: CD_antigen=CD326;
Flags: Precursor;
Name=EPCAM; Synonyms=TACSTD1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
-!- 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 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Monomer. Interacts with phosphorylated CLDN7 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Lateral cell membrane
{ECO:0000250|UniProtKB:P16422}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P16422}. Cell junction, tight
junction {ECO:0000250|UniProtKB:P16422}. Note=Colocalizes with
CLDN7 at the lateral cell membrane and tight junction.
{ECO:0000250|UniProtKB:P16422}.
-!- PTM: Glycosylation at Asn-198 is crucial for protein stability.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the EPCAM family. {ECO:0000305}.
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EMBL; BC102346; AAI02347.1; -; mRNA.
EMBL; BT025464; ABF57420.1; -; mRNA.
RefSeq; NP_001030367.1; NM_001035290.1.
UniGene; Bt.9569; -.
ProteinModelPortal; Q3T0L5; -.
SMR; Q3T0L5; -.
STRING; 9913.ENSBTAP00000008487; -.
PaxDb; Q3T0L5; -.
PeptideAtlas; Q3T0L5; -.
PRIDE; Q3T0L5; -.
GeneID; 514039; -.
KEGG; bta:514039; -.
CTD; 4072; -.
eggNOG; ENOG410IFI6; Eukaryota.
eggNOG; ENOG4111M3B; LUCA.
HOGENOM; HOG000074086; -.
InParanoid; Q3T0L5; -.
KO; K06737; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IBA:GO_Central.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
CDD; cd00191; TY; 1.
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.
2: Evidence at transcript level;
Cell junction; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Membrane; Reference proteome; Repeat; Signal;
Tight junction; Transmembrane; Transmembrane helix.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 314 Epithelial cell adhesion molecule.
/FTId=PRO_0000380181.
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 37 37 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 198 198 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 27 46 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 29 59 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 38 48 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 66 99 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 110 116 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 118 135 {ECO:0000255|PROSITE-ProRule:PRU00500}.
CONFLICT 201 201 Q -> H (in Ref. 1; ABF57420).
{ECO:0000305}.
SEQUENCE 314 AA; 34859 MW; B836973C47B72DD1 CRC64;
MAPPQVLAFG LLVAAATAAV AADQEGCVCE NYKLTTNCSV NALGQCQCTS VGTQHSVICT
KLATKCLVMK AEMNHSKSGR RGKPEGAIQN NDGLYDPECD DKGLFKAKQC NGTSTCWCVN
TAGVRRTDKD SEISCSEPVR TYWIIIELKH KTREKPYDLQ SLQSALKDVI TNRYQLDPKY
ITNILYENDV ITIDLVQNSS QKTQNDVDIA DVAYYFEKDV KDESLFHSKR MDLRVNGELL
DLDPGRTSIY YVDEKPPEFS MQGLQAGIIA VIVVVVVAII AGIIVLVVSR KKSMTKYEKA
EIKEMGEMHR ELNA


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