EPCAM_PIG
ID EPCAM_PIG Reviewed; 314 AA.
AC Q75QW1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Epithelial cell adhesion molecule;
DE Short=Ep-CAM;
DE AltName: Full=Tumor-associated calcium signal transducer 1;
DE AltName: CD_antigen=CD326;
DE Flags: Precursor;
GN Name=TACSTD1; Synonyms=EPCAM;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=15507398; DOI=10.1016/j.clim.2004.08.013;
RA Nochi T., Yuki Y., Terahara K., Hino A., Kunisawa J., Kweon M.N.,
RA Yamaguchi T., Kiyono H.;
RT "Biological role of Ep-CAM in the physical interaction between epithelial
RT cells and lymphocytes in intestinal epithelium.";
RL Clin. Immunol. 113:326-339(2004).
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 (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:15507398}.
CC -!- SUBUNIT: Monomer. Interacts with phosphorylated CLDN7 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lateral cell membrane
CC {ECO:0000250|UniProtKB:P16422}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P16422}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:P16422}. Note=Colocalizes with CLDN7 at the
CC lateral cell membrane and tight junction.
CC {ECO:0000250|UniProtKB:P16422}.
CC -!- PTM: Glycosylation at Asn-198 is crucial for protein stability.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EPCAM family. {ECO:0000305}.
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DR EMBL; AB161197; BAD08374.1; -; mRNA.
DR RefSeq; NP_999584.1; NM_214419.1.
DR AlphaFoldDB; Q75QW1; -.
DR SMR; Q75QW1; -.
DR STRING; 9823.ENSSSCP00000008996; -.
DR PaxDb; Q75QW1; -.
DR PeptideAtlas; Q75QW1; -.
DR PRIDE; Q75QW1; -.
DR Ensembl; ENSSSCT00000061463; ENSSSCP00000045246; ENSSSCG00000008429.
DR Ensembl; ENSSSCT00030004106; ENSSSCP00030001625; ENSSSCG00030002993.
DR Ensembl; ENSSSCT00035075603; ENSSSCP00035030790; ENSSSCG00035056583.
DR Ensembl; ENSSSCT00040016447; ENSSSCP00040006601; ENSSSCG00040012351.
DR Ensembl; ENSSSCT00045057516; ENSSSCP00045040226; ENSSSCG00045033606.
DR Ensembl; ENSSSCT00050072337; ENSSSCP00050031111; ENSSSCG00050053079.
DR Ensembl; ENSSSCT00055039113; ENSSSCP00055031106; ENSSSCG00055019863.
DR Ensembl; ENSSSCT00060040228; ENSSSCP00060017035; ENSSSCG00060029769.
DR Ensembl; ENSSSCT00070001323; ENSSSCP00070001159; ENSSSCG00070000698.
DR GeneID; 403163; -.
DR KEGG; ssc:403163; -.
DR CTD; 4072; -.
DR VGNC; VGNC:87726; EPCAM.
DR eggNOG; ENOG502QVSU; Eukaryota.
DR GeneTree; ENSGT00390000018245; -.
DR HOGENOM; CLU_075326_0_0_1; -.
DR InParanoid; Q75QW1; -.
DR OMA; NGTTTCW; -.
DR OrthoDB; 1017141at2759; -.
DR TreeFam; TF332767; -.
DR Reactome; R-SSC-202733; Cell surface interactions at the vascular wall.
DR Proteomes; UP000008227; Chromosome 3.
DR Proteomes; UP000314985; Chromosome 3.
DR Bgee; ENSSSCG00000008429; Expressed in epididymis and 35 other tissues.
DR ExpressionAtlas; Q75QW1; baseline and differential.
DR Genevisible; Q75QW1; SS.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Tight junction; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..314
FT /note="Epithelial cell adhesion molecule"
FT /id="PRO_0000380184"
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 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 29..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 38..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 66..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 110..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 118..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
SQ 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