EPCAM_MACMU
ID EPCAM_MACMU Reviewed; 314 AA.
AC Q1WER1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16619291; DOI=10.1002/eji.200535514;
RA Elia L., Mennuni C., Storto M., Podda S., Calvaruso F., Salucci V.,
RA Aurisicchio L., Scarito A., Ciliberto G., La Monica N., Palombo F.;
RT "Genetic vaccines against Ep-CAM break tolerance to self in a limited
RT subset of subjects: initial identification of predictive biomarkers.";
RL Eur. J. Immunol. 36:1337-1349(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ341470; ABC70159.1; -; mRNA.
DR RefSeq; NP_001035118.1; NM_001040029.1.
DR AlphaFoldDB; Q1WER1; -.
DR SMR; Q1WER1; -.
DR STRING; 9544.ENSMMUP00000016268; -.
DR Ensembl; ENSMMUT00000056802; ENSMMUP00000048687; ENSMMUG00000012390.
DR GeneID; 677680; -.
DR KEGG; mcc:677680; -.
DR CTD; 4072; -.
DR VEuPathDB; HostDB:ENSMMUG00000012390; -.
DR VGNC; VGNC:106156; EPCAM.
DR eggNOG; ENOG502QVSU; Eukaryota.
DR GeneTree; ENSGT00390000018245; -.
DR HOGENOM; CLU_075326_0_0_1; -.
DR InParanoid; Q1WER1; -.
DR OrthoDB; 1017141at2759; -.
DR Proteomes; UP000006718; Chromosome 13.
DR Bgee; ENSMMUG00000012390; Expressed in colon and 14 other tissues.
DR ExpressionAtlas; Q1WER1; baseline.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
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:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
DR GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
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_0000380182"
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 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"
SQ SEQUENCE 314 AA; 34879 MW; 2D5A7806F848A562 CRC64;
MAPPQVLAFG LLLAAATASF AAAQKECVCE NYKLAVNCFL NDNGQCQCTS IGAQNTVLCS
KLAAKCLVMK AEMNGSKLGR RAKPEGALQN NDGLYDPDCD ESGLFKAKQC NGTSTCWCVN
TAGVRRTDKD TEITCSERVR TYWIIIELKH KAREKPYDVQ SLRTALEEAI KTRYQLDPKF
ITNILYEDNV ITIDLVQNSS QKTQNDVDIA DVAYYFEKDV KGESLFHSKK MDLRVNGEQL
DLDPGQTLIY YVDEKAPEFS MQGLKAGVIA VIVVVVIAIV AGIVVLVISR KKRMAKYEKA
EIKEMGEIHR ELNA
