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Database: UniProt
Entry: A0A2U3XZJ6_LEPWE
LinkDB: A0A2U3XZJ6_LEPWE
Original site: A0A2U3XZJ6_LEPWE 
ID   A0A2U3XZJ6_LEPWE        Unreviewed;       316 AA.
AC   A0A2U3XZJ6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
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|RefSeq:XP_006736887.1};
OS   Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC   Leptonychotes.
OX   NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006736887.1};
RN   [1] {ECO:0000313|RefSeq:XP_006736887.1}
RP   IDENTIFICATION.
RC   TISSUE=Liver {ECO:0000313|RefSeq:XP_006736887.1};
RG   RefSeq;
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   RefSeq; XP_006736887.1; XM_006736824.2.
DR   AlphaFoldDB; A0A2U3XZJ6; -.
DR   STRING; 9713.A0A2U3XZJ6; -.
DR   GeneID; 102739387; -.
DR   KEGG; lww:102739387; -.
DR   CTD; 4072; -.
DR   OrthoDB; 5305981at2759; -.
DR   Proteomes; UP000245341; Unplaced.
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:UP000245341};
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..316
FT                   /note="Epithelial cell adhesion molecule"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015408710"
FT   TRANSMEM        268..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          63..137
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
SQ   SEQUENCE   316 AA;  35568 MW;  13FBB1D4C082A96F CRC64;
     MARSQVLAFG LLFAAATLAV AVAQKACVCE NYKLTTNCSW NTNGQCECTS LGAQNSVICS
     KLATKCLVMK AEMTRSKSGR RVRPEGAFQN NDGLYDPDCD EKGLFKAKQC NGTTTCWCVN
     TAGVRRTDKD NDDEISCSER VRTYWIIIEL KHKTRETPYD TKSLRTALMK TITTRYQLDP
     KYITNILYEN DLITIDLMQN SSQKTQNDVD IADVAYYFEK DVKDESLFHS NRMDLRVNGE
     QLDLDPGRTA IYYVDEKPPE FSMQGLQAGI IAVIVVVTLA VIAGIVVLVI SRKNRMAKYE
     KAEIKEMGEM HRELNA
//
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