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EPCAM_PIG
ID   EPCAM_PIG               Reviewed;         314 AA.
AC   Q75QW1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=15507398; DOI=10.1016/j.clim.2004.08.013;
RA   Nochi T., Yuki Y., Terahara K., Hino A., Kunisawa J., Kweon M.N.,
RA   Yamaguchi T., Kiyono H.;
RT   "Biological role of Ep-CAM in the physical interaction between epithelial
RT   cells and lymphocytes in intestinal epithelium.";
RL   Clin. Immunol. 113:326-339(2004).
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, ECO:0000269|PubMed:15507398}.
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; AB161197; BAD08374.1; -; mRNA.
DR   RefSeq; NP_999584.1; NM_214419.1.
DR   AlphaFoldDB; Q75QW1; -.
DR   SMR; Q75QW1; -.
DR   STRING; 9823.ENSSSCP00000008996; -.
DR   PaxDb; Q75QW1; -.
DR   PeptideAtlas; Q75QW1; -.
DR   PRIDE; Q75QW1; -.
DR   Ensembl; ENSSSCT00000061463; ENSSSCP00000045246; ENSSSCG00000008429.
DR   Ensembl; ENSSSCT00030004106; ENSSSCP00030001625; ENSSSCG00030002993.
DR   Ensembl; ENSSSCT00035075603; ENSSSCP00035030790; ENSSSCG00035056583.
DR   Ensembl; ENSSSCT00040016447; ENSSSCP00040006601; ENSSSCG00040012351.
DR   Ensembl; ENSSSCT00045057516; ENSSSCP00045040226; ENSSSCG00045033606.
DR   Ensembl; ENSSSCT00050072337; ENSSSCP00050031111; ENSSSCG00050053079.
DR   Ensembl; ENSSSCT00055039113; ENSSSCP00055031106; ENSSSCG00055019863.
DR   Ensembl; ENSSSCT00060040228; ENSSSCP00060017035; ENSSSCG00060029769.
DR   Ensembl; ENSSSCT00070001323; ENSSSCP00070001159; ENSSSCG00070000698.
DR   GeneID; 403163; -.
DR   KEGG; ssc:403163; -.
DR   CTD; 4072; -.
DR   VGNC; VGNC:87726; EPCAM.
DR   eggNOG; ENOG502QVSU; Eukaryota.
DR   GeneTree; ENSGT00390000018245; -.
DR   HOGENOM; CLU_075326_0_0_1; -.
DR   InParanoid; Q75QW1; -.
DR   OMA; NGTTTCW; -.
DR   OrthoDB; 1017141at2759; -.
DR   TreeFam; TF332767; -.
DR   Reactome; R-SSC-202733; Cell surface interactions at the vascular wall.
DR   Proteomes; UP000008227; Chromosome 3.
DR   Proteomes; UP000314985; Chromosome 3.
DR   Bgee; ENSSSCG00000008429; Expressed in epididymis and 35 other tissues.
DR   ExpressionAtlas; Q75QW1; baseline and differential.
DR   Genevisible; Q75QW1; SS.
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:0098641; F:cadherin binding involved in cell-cell adhesion; IBA:GO_Central.
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_0000380184"
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        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;  34833 MW;  88177EFD6D20D1F2 CRC64;
     MAPPQVLAFG LLLAAATAAV AAAQQGCVCE NYKLTTNCSL NALGQCQCTS IGAQNSVICS
     KLASKCLVMK AEMTGSKAGR RLKPENAIQN NDGLYDPDCD ENGLFKAKQC NGTSMCWCVN
     TAGVRRTDKD SEISCLERVR TYWIIIELKH KTREKPYDVT SLQNALKEVI TDRYQLDPKY
     ITNILYENDI ITIDLVQNSS QKTLNEVDIA DVAYYFEKDV KDESLFHSKR MDLRVNGELL
     DLDPGQTSIY YVDEKPPEFS MQGLQAGIIA VIAVVAIAIV AGIIVLIVST KKRRAKYEKA
     EIKEMGEMHR ELNA
 
 
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