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   27-MAR-2024, entry version 150.
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   GlyCosmos; Q99JW5; 2 sites, No reported glycans.
DR   GlyGen; Q99JW5; 2 sites.
DR   iPTMnet; Q99JW5; -.
DR   PhosphoSitePlus; Q99JW5; -.
DR   EPD; Q99JW5; -.
DR   jPOST; Q99JW5; -.
DR   MaxQB; Q99JW5; -.
DR   PaxDb; 10090-ENSMUSP00000061935; -.
DR   PeptideAtlas; Q99JW5; -.
DR   ProteomicsDB; 275528; -.
DR   Antibodypedia; 3539; 5262 antibodies from 61 providers.
DR   DNASU; 17075; -.
DR   Ensembl; ENSMUST00000053577.9; ENSMUSP00000061935.9; ENSMUSG00000045394.10.
DR   Ensembl; ENSMUST00000234623.2; ENSMUSP00000157040.2; ENSMUSG00000045394.10.
DR   GeneID; 17075; -.
DR   KEGG; mmu:17075; -.
DR   UCSC; uc008duy.1; mouse.
DR   AGR; MGI:106653; -.
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; TQNSVIC; -.
DR   OrthoDB; 5305981at2759; -.
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 78 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 220 other cell types or tissues.
DR   ExpressionAtlas; Q99JW5; baseline and differential.
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: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; Thyroglobulin type-1; 1.
DR   InterPro; IPR049420; EPCAM-Trop-2_C.
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:SF2; EPITHELIAL CELL ADHESION MOLECULE; 1.
DR   PANTHER; PTHR14168; TUMOR-ASSOCIATED CALCIUM SIGNAL TRANSDUCER; 1.
DR   Pfam; PF21283; EPCAM-Trop-2_C; 1.
DR   Pfam; PF18635; EpCAM_N; 1.
DR   Pfam; PF00086; Thyroglobulin_1; 1.
DR   SMART; SM00211; TY; 1.
DR   SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1.
DR   PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
DR   Genevisible; Q99JW5; MM.
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
//