ID A0A3Q1JE33_ANATE Unreviewed; 306 AA.
AC A0A3Q1JE33;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Epithelial cell adhesion molecule {ECO:0000256|ARBA:ARBA00015562};
DE AltName: Full=Tumor-associated calcium signal transducer 1 {ECO:0000256|ARBA:ARBA00031829};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000013311.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000013311.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
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DR AlphaFoldDB; A0A3Q1JE33; -.
DR STRING; 64144.ENSATEP00000013311; -.
DR Ensembl; ENSATET00000013528.2; ENSATEP00000013311.1; ENSATEG00000009305.2.
DR GeneTree; ENSGT00390000018245; -.
DR InParanoid; A0A3Q1JE33; -.
DR OMA; TQNSVIC; -.
DR OrthoDB; 5305981at2759; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0016020; C: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; 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; 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 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..306
FT /note="Epithelial cell adhesion molecule"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018626280"
FT TRANSMEM 262..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..135
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
SQ SEQUENCE 306 AA; 34512 MW; 79070C1E1A1B96B6 CRC64;
MKMWIAVFVA AFVAGAAAQC PCNTMKWAVC DGPPCQCTLQ LSESLPQSLG ECKNLVSKCY
LMKAEMYRAR TGQSTRSIEG KPVETAFVDN DGIYDPECEN DGKFKAKQCN NTAECWCVNS
AGVRRTDKGD KNIKCEELVE TYWIRLQLKH KPVANSVNAN NLNVSLVNAM NQRYLNDYSS
FVKKVQYDPS ARMIVVDVEK PPRNPIDLPT MAYYMEKDVK VLPLFLNKGN FTVNVDSQSL
QMEEILVYYV DEKPPTFTMK HLSGGIIAVI VVVVLAVVIG LLVLFFTRKR LSKKYNKAQQ
REMDPM
//