EPCAM_BOVIN
ID EPCAM_BOVIN Reviewed; 314 AA.
AC Q3T0L5; Q1JP89;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=EPCAM; Synonyms=TACSTD1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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; BC102346; AAI02347.1; -; mRNA.
DR EMBL; BT025464; ABF57420.1; -; mRNA.
DR RefSeq; NP_001030367.1; NM_001035290.1.
DR AlphaFoldDB; Q3T0L5; -.
DR SMR; Q3T0L5; -.
DR STRING; 9913.ENSBTAP00000008487; -.
DR PaxDb; Q3T0L5; -.
DR PeptideAtlas; Q3T0L5; -.
DR GeneID; 514039; -.
DR KEGG; bta:514039; -.
DR CTD; 4072; -.
DR eggNOG; ENOG502QVSU; Eukaryota.
DR InParanoid; Q3T0L5; -.
DR OrthoDB; 1017141at2759; -.
DR Proteomes; UP000009136; Unplaced.
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: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_0000380181"
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 74
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"
FT CONFLICT 201
FT /note="Q -> H (in Ref. 1; ABF57420)"
FT /evidence="ECO:0000305"
SQ 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
