ID A0A2R9A8B2_PANPA Unreviewed; 314 AA.
AC A0A2R9A8B2;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Epithelial cell adhesion molecule {ECO:0000256|ARBA:ARBA00015562};
DE AltName: Full=Tumor-associated calcium signal transducer 1 {ECO:0000256|ARBA:ARBA00031829};
GN Name=EPCAM {ECO:0000313|Ensembl:ENSPPAP00000011646.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000011646.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000011646.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00024978}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Lateral cell membrane {ECO:0000256|ARBA:ARBA00004591}; Single-pass type
CC I membrane protein {ECO:0000256|ARBA:ARBA00004591}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the EPCAM family.
CC {ECO:0000256|ARBA:ARBA00007669}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
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DR EMBL; AJFE02079016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02079017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02079018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02079019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02079020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02079021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003822725.1; XM_003822677.2.
DR AlphaFoldDB; A0A2R9A8B2; -.
DR Ensembl; ENSPPAT00000034306.1; ENSPPAP00000011646.1; ENSPPAG00000029030.1.
DR GeneID; 100984252; -.
DR KEGG; pps:100984252; -.
DR CTD; 4072; -.
DR GeneTree; ENSGT00390000018245; -.
DR OMA; TQNSVIC; -.
DR OrthoDB; 5305981at2759; -.
DR Proteomes; UP000240080; Unplaced.
DR Bgee; ENSPPAG00000029030; Expressed in adult mammalian kidney and 5 other cell types or tissues.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..314
FT /note="Epithelial cell adhesion molecule"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015312294"
FT TRANSMEM 266..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..135
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
SQ SEQUENCE 314 AA; 34928 MW; 7EF6664D41A3794F CRC64;
MAPPQVLAFG LLLAAATATF AAAQEECVCE NYKLAVNCFV NNNHQCQCTS IGAQNTVICS
KLAAKCLVMK AEMNGSKLGR RAKPEGALQN NDGLYDPDCD ESGLFKAKQC NGTSTCWCVN
TAGVRRTDKD TEITCSERVR TYWIIIELKH KAREKPYDGK SLRTALQKEI TTRYQLDPKF
ITNILYENNV ITIDLVQNSS QKTQNDVDIA DVAYYFEKDV KGESLFHSKK MDLTVNGEQL
DLDPGQTLIY YVDEKAPEFS MQGLKAGVIA VIVVVVIAVV AGIVVLVFSR KKRMAKYEKA
EIKEMGEMHR ELNA
//
