EPCAM_RAT
ID EPCAM_RAT Reviewed; 315 AA.
AC O55159;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Epithelial cell adhesion molecule;
DE Short=Ep-CAM;
DE AltName: Full=Epithelial glycoprotein 314;
DE Short=EGP314;
DE AltName: Full=Protein D5.7A;
DE AltName: Full=Tumor-associated calcium signal transducer 1;
DE AltName: CD_antigen=CD326;
DE Flags: Precursor;
GN Name=Epcam; Synonyms=Tacstd1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BDIX; TISSUE=Colon carcinoma;
RX PubMed=10327052; DOI=10.1038/sj.onc.1202542;
RA Wuerfel J., Roesel M., Seiter S., Claas C., Herlevsen M., Weth R.,
RA Zoeller M.;
RT "Metastasis-association of the rat ortholog of the human epithelial
RT glycoprotein antigen EGP314.";
RL Oncogene 18:2323-2334(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CLDN7.
RX PubMed=16054130; DOI=10.1016/j.yexcr.2005.06.013;
RA Ladwein M., Pape U.F., Schmidt D.S., Schnoelzer M., Fiedler S.,
RA Langbein L., Franke W.W., Moldenhauer G., Zoeller M.;
RT "The cell-cell adhesion molecule EpCAM interacts directly with the tight
RT junction protein claudin-7.";
RL Exp. Cell Res. 309:345-357(2005).
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 (By similarity). Interacts with phosphorylated CLDN7.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lateral cell membrane
CC {ECO:0000269|PubMed:16054130}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16054130}. Cell junction, tight junction
CC {ECO:0000269|PubMed:16054130}. Note=Colocalizes with CLDN7 at the
CC lateral cell membrane and tight junction.
CC {ECO:0000269|PubMed:16054130}.
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; AJ001044; CAA04498.1; -; mRNA.
DR EMBL; CH473947; EDM02636.1; -; Genomic_DNA.
DR EMBL; BC072691; AAH72691.1; -; mRNA.
DR RefSeq; NP_612550.1; NM_138541.1.
DR RefSeq; XP_017449516.1; XM_017594027.1.
DR AlphaFoldDB; O55159; -.
DR SMR; O55159; -.
DR STRING; 10116.ENSRNOP00000021135; -.
DR GlyGen; O55159; 2 sites.
DR iPTMnet; O55159; -.
DR PhosphoSitePlus; O55159; -.
DR jPOST; O55159; -.
DR PaxDb; O55159; -.
DR PRIDE; O55159; -.
DR Ensembl; ENSRNOT00000021135; ENSRNOP00000021135; ENSRNOG00000015667.
DR GeneID; 171577; -.
DR KEGG; rno:171577; -.
DR UCSC; RGD:621365; rat.
DR CTD; 4072; -.
DR RGD; 621365; Epcam.
DR eggNOG; ENOG502QVSU; Eukaryota.
DR GeneTree; ENSGT00390000018245; -.
DR HOGENOM; CLU_075326_0_0_1; -.
DR InParanoid; O55159; -.
DR OMA; NGTTTCW; -.
DR OrthoDB; 1017141at2759; -.
DR PhylomeDB; O55159; -.
DR TreeFam; TF332767; -.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR PRO; PR:O55159; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Proteomes; UP000234681; Chromosome 6.
DR Bgee; ENSRNOG00000015667; Expressed in jejunum and 19 other tissues.
DR Genevisible; O55159; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IDA:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; ISO:RGD.
DR GO; GO:2000147; P:positive regulation of cell motility; IDA:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; ISO:RGD.
DR GO; GO:0048863; P:stem cell differentiation; ISO:RGD.
DR GO; GO:0001657; P:ureteric bud development; ISO:RGD.
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 1: Evidence at protein 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..315
FT /note="Epithelial cell adhesion molecule"
FT /id="PRO_0000380185"
FT TOPO_DOM 24..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..315
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 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 315 AA; 35207 MW; 024F796B18F85BC4 CRC64;
MAPPKALAFG LLLAVVTATL AAAQKDCVCN NYKLTSRCYE NENGECQCTS YGTQNTVICS
KLASKCLVMK AEMTHSKSGR RMKPEGAIQN NDGLYDPECD EQGLFKAKQC NGTATCWCVN
TAGVRRTDKD TEITCSERVR TYWIIIELKH KERAQPYNFE SLHTALQDTF ASRYMLNPKF
IKSIMYENNV ITIDLMQNSS QKTQDDVDIA DVAYYFEKDV KGESLFHSSK SMDLRVNGEL
LDLDPGQTLI YYVDEKAPEF SMQGLTAGII AVIVVVVLAV IAGIVVLVIS TRKRSAKYEK
AEIKEMGEIH RELNA
