EPCAM_MOUSE
ID EPCAM_MOUSE Reviewed; 315 AA.
AC Q99JW5; Q61512;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Epithelial cell adhesion molecule;
DE Short=Ep-CAM;
DE AltName: Full=Epithelial glycoprotein 314;
DE Short=EGP314;
DE Short=mEGP314;
DE AltName: Full=Protein 289A;
DE AltName: Full=Tumor-associated calcium signal transducer 1;
DE AltName: CD_antigen=CD326;
DE Flags: Precursor;
GN Name=Epcam; Synonyms=Tacstd1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1729376;
RA Bergsagel P.L., Victor-Kobrin C., Timblin C.R., Trepel J., Kuehl W.M.;
RT "A murine cDNA encodes a pan-epithelial glycoprotein that is also expressed
RT on plasma cells.";
RL J. Immunol. 148:590-596(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; M76124; AAA37543.1; -; mRNA.
DR EMBL; AK145752; BAE26627.1; -; mRNA.
DR EMBL; AK167182; BAE39317.1; -; mRNA.
DR EMBL; BC005618; AAH05618.1; -; mRNA.
DR EMBL; BC094465; AAH94465.1; -; mRNA.
DR CCDS; CCDS29018.1; -.
DR RefSeq; NP_032558.2; NM_008532.2.
DR AlphaFoldDB; Q99JW5; -.
DR SMR; Q99JW5; -.
DR IntAct; Q99JW5; 3.
DR STRING; 10090.ENSMUSP00000061935; -.
DR GlyGen; Q99JW5; 2 sites.
DR iPTMnet; Q99JW5; -.
DR PhosphoSitePlus; Q99JW5; -.
DR EPD; Q99JW5; -.
DR jPOST; Q99JW5; -.
DR MaxQB; Q99JW5; -.
DR PaxDb; Q99JW5; -.
DR PeptideAtlas; Q99JW5; -.
DR PRIDE; Q99JW5; -.
DR ProteomicsDB; 275528; -.
DR Antibodypedia; 3539; 4504 antibodies from 59 providers.
DR DNASU; 17075; -.
DR Ensembl; ENSMUST00000053577; ENSMUSP00000061935; ENSMUSG00000045394.
DR Ensembl; ENSMUST00000234623; ENSMUSP00000157040; ENSMUSG00000045394.
DR GeneID; 17075; -.
DR KEGG; mmu:17075; -.
DR UCSC; uc008duy.1; mouse.
DR CTD; 4072; -.
DR MGI; MGI:106653; Epcam.
DR VEuPathDB; HostDB:ENSMUSG00000045394; -.
DR eggNOG; ENOG502QVSU; Eukaryota.
DR GeneTree; ENSGT00390000018245; -.
DR HOGENOM; CLU_075326_0_0_1; -.
DR InParanoid; Q99JW5; -.
DR OMA; NGTTTCW; -.
DR OrthoDB; 1017141at2759; -.
DR PhylomeDB; Q99JW5; -.
DR TreeFam; TF332767; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR BioGRID-ORCS; 17075; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Epcam; mouse.
DR PRO; PR:Q99JW5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q99JW5; protein.
DR Bgee; ENSMUSG00000045394; Expressed in left colon and 217 other tissues.
DR ExpressionAtlas; Q99JW5; baseline and differential.
DR Genevisible; Q99JW5; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:MGI.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; ISO:MGI.
DR GO; GO:2000147; P:positive regulation of cell motility; ISO:MGI.
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:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; ISO:MGI.
DR GO; GO:0048863; P:stem cell differentiation; ISO:MGI.
DR GO; GO:0001657; P:ureteric bud development; IEP: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 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_0000380183"
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"
FT CONFLICT 87
FT /note="Missing (in Ref. 1; AAA37543)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 35019 MW; FDA853E165BA8906 CRC64;
MAGPQALAFG LLLAVVTATL AAAQRDCVCD NYKLATSCSL NEYGECQCTS YGTQNTVICS
KLASKCLAMK AEMTHSKSGR RIKPEGAIQN NDGLYDPDCD EQGLFKAKQC NGTATCWCVN
TAGVRRTDKD TEITCSERVR TYWIIIELKH KERESPYDHQ SLQTALQEAF TSRYKLNQKF
IKNIMYENNV ITIDLMQNSS QKTQDDVDIA DVAYYFEKDV KGESLFHSSK SMDLRVNGEP
LDLDPGQTLI YYVDEKAPEF SMQGLTAGII AVIVVVSLAV IAGIVVLVIS TRKKSAKYEK
AEIKEMGEIH RELNA
