EPCAM_CHICK
ID EPCAM_CHICK Reviewed; 306 AA.
AC Q5F381;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Epithelial cell adhesion molecule;
DE Short=Ep-CAM;
DE AltName: Full=Tumor-associated calcium signal transducer 1;
DE Flags: Precursor;
GN Name=EPCAM; Synonyms=TACSTD1; ORFNames=RCJMB04_29h4;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- SUBCELLULAR LOCATION: Lateral cell membrane
CC {ECO:0000250|UniProtKB:P16422}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P16422}.
CC -!- SIMILARITY: Belongs to the EPCAM family. {ECO:0000305}.
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DR EMBL; AJ851769; CAH65403.1; -; mRNA.
DR RefSeq; NP_001012582.1; NM_001012564.1.
DR AlphaFoldDB; Q5F381; -.
DR SMR; Q5F381; -.
DR STRING; 9031.ENSGALP00000014571; -.
DR PaxDb; Q5F381; -.
DR GeneID; 421292; -.
DR KEGG; gga:421292; -.
DR CTD; 4072; -.
DR VEuPathDB; HostDB:geneid_421292; -.
DR eggNOG; ENOG502QVSU; Eukaryota.
DR InParanoid; Q5F381; -.
DR OrthoDB; 1017141at2759; -.
DR PhylomeDB; Q5F381; -.
DR PRO; PR:Q5F381; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IBA:GO_Central.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.800.10; -; 1.
DR InterPro; IPR043406; EPCAM/Trop-2.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR PANTHER; PTHR14168; PTHR14168; 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 membrane; Disulfide bond; Glycoprotein; Membrane; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..306
FT /note="Epithelial cell adhesion molecule"
FT /id="PRO_0000380186"
FT TOPO_DOM 20..260
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..130
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 61..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 105..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 112..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 306 AA; 34360 MW; BDC7C9769267D900 CRC64;
MELLRGAALL LLLCAAACAQ DSCTCTKNKR VTNCRLIDNV CHCNSIGSSV PVNCEILTSK
CLLMKAEMAN TKSGRREKPK DALQDTDGLY DPECENNGLF KAKQCNGTTC WCVNTAGVRR
TDKHDTDLKC NQLVRTTWII IEMRHAERKT PLNAESLTRY LKDTITSRYM LDGRYISGVV
YENPTITIDL KQNSSDKTPG DVDITDVAYY FEKDVKDDSI FLNNKLNMNI DNEELKFDNM
MVYYVDEVPP EFSMKSLTAG VIAVIVIVVL AIVAGIIGLV LSRRRKGKYV KAEMKEMNEM
HRGLNA