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

 EPCAM_PIG               Reviewed;         314 AA.
Q75QW1;
28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
23-MAY-2018, entry version 75.
RecName: Full=Epithelial cell adhesion molecule;
Short=Ep-CAM;
AltName: Full=Tumor-associated calcium signal transducer 1;
AltName: CD_antigen=CD326;
Flags: Precursor;
Name=TACSTD1; Synonyms=EPCAM;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=15507398; DOI=10.1016/j.clim.2004.08.013;
Nochi T., Yuki Y., Terahara K., Hino A., Kunisawa J., Kweon M.N.,
Yamaguchi T., Kiyono H.;
"Biological role of Ep-CAM in the physical interaction between
epithelial cells and lymphocytes in intestinal epithelium.";
Clin. Immunol. 113:326-339(2004).
-!- 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,
ECO:0000269|PubMed:15507398}.
-!- 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; AB161197; BAD08374.1; -; mRNA.
RefSeq; NP_999584.1; NM_214419.1.
UniGene; Ssc.51858; -.
ProteinModelPortal; Q75QW1; -.
SMR; Q75QW1; -.
STRING; 9823.ENSSSCP00000008996; -.
PaxDb; Q75QW1; -.
PeptideAtlas; Q75QW1; -.
PRIDE; Q75QW1; -.
Ensembl; ENSSSCT00000009230; ENSSSCP00000008996; ENSSSCG00000008429.
Ensembl; ENSSSCT00000061463; ENSSSCP00000045246; ENSSSCG00000008429.
GeneID; 403163; -.
KEGG; ssc:403163; -.
CTD; 4072; -.
eggNOG; ENOG410IFI6; Eukaryota.
eggNOG; ENOG4111M3B; LUCA.
GeneTree; ENSGT00390000018245; -.
HOGENOM; HOG000074086; -.
InParanoid; Q75QW1; -.
KO; K06737; -.
OMA; REKPYDV; -.
OrthoDB; EOG091G0G1E; -.
TreeFam; TF332767; -.
Reactome; R-SSC-202733; Cell surface interactions at the vascular wall.
Proteomes; UP000008227; Chromosome 3.
Bgee; ENSSSCG00000008429; -.
Genevisible; Q75QW1; SS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
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_0000380184.
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 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}.
SEQUENCE 314 AA; 34833 MW; 88177EFD6D20D1F2 CRC64;
MAPPQVLAFG LLLAAATAAV AAAQQGCVCE NYKLTTNCSL NALGQCQCTS IGAQNSVICS
KLASKCLVMK AEMTGSKAGR RLKPENAIQN NDGLYDPDCD ENGLFKAKQC NGTSMCWCVN
TAGVRRTDKD SEISCLERVR TYWIIIELKH KTREKPYDVT SLQNALKEVI TDRYQLDPKY
ITNILYENDI ITIDLVQNSS QKTLNEVDIA DVAYYFEKDV KDESLFHSKR MDLRVNGELL
DLDPGQTSIY YVDEKPPEFS MQGLQAGIIA VIAVVAIAIV AGIIVLIVST KKRRAKYEKA
EIKEMGEMHR ELNA


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