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TFF3_CANLF
ID   TFF3_CANLF              Reviewed;          80 AA.
AC   Q863B4;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Trefoil factor 3;
DE   AltName: Full=Intestinal trefoil factor;
DE   Flags: Precursor;
GN   Name=TFF3; Synonyms=ITF;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Colon mucosa;
RA   Campbell B.G., Jabbes M.;
RT   "Canine trefoil factor 3 (TFF3) mRNA from colonic mucosa.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the maintenance and repair of the intestinal
CC       mucosa. Promotes the mobility of epithelial cells in healing processes
CC       (motogen) (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Homodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:Q07654}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q07654}.
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DR   EMBL; AY264844; AAP21821.1; -; mRNA.
DR   RefSeq; NP_001002990.1; NM_001002990.1.
DR   AlphaFoldDB; Q863B4; -.
DR   SMR; Q863B4; -.
DR   STRING; 9612.ENSCAFP00000032737; -.
DR   PaxDb; Q863B4; -.
DR   Ensembl; ENSCAFT00000109373; ENSCAFP00000074539; ENSCAFG00000053768.
DR   Ensembl; ENSCAFT00030041012; ENSCAFP00030035787; ENSCAFG00030022325.
DR   Ensembl; ENSCAFT00040045961; ENSCAFP00040040100; ENSCAFG00040024680.
DR   Ensembl; ENSCAFT00845054078; ENSCAFP00845042482; ENSCAFG00845030487.
DR   GeneID; 403488; -.
DR   KEGG; cfa:403488; -.
DR   CTD; 7033; -.
DR   VEuPathDB; HostDB:ENSCAFG00845030487; -.
DR   eggNOG; ENOG502SV7V; Eukaryota.
DR   GeneTree; ENSGT00940000162416; -.
DR   InParanoid; Q863B4; -.
DR   OrthoDB; 1563185at2759; -.
DR   Proteomes; UP000002254; Chromosome 31.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IBA:GO_Central.
DR   GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
DR   CDD; cd00111; Trefoil; 1.
DR   Gene3D; 4.10.110.10; -; 1.
DR   InterPro; IPR017994; P_trefoil_chordata.
DR   InterPro; IPR017957; P_trefoil_CS.
DR   InterPro; IPR000519; P_trefoil_dom.
DR   InterPro; IPR044913; P_trefoil_dom_sf.
DR   PANTHER; PTHR13826; PTHR13826; 1.
DR   Pfam; PF00088; Trefoil; 1.
DR   PRINTS; PR00680; PTREFOIL.
DR   SMART; SM00018; PD; 1.
DR   SUPFAM; SSF57492; SSF57492; 1.
DR   PROSITE; PS00025; P_TREFOIL_1; 1.
DR   PROSITE; PS51448; P_TREFOIL_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Disulfide bond; Extracellular matrix; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..80
FT                   /note="Trefoil factor 3"
FT                   /id="PRO_0000023464"
FT   DOMAIN          30..73
FT                   /note="P-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   DISULFID        32..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   DISULFID        42..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   DISULFID        52..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   DISULFID        78
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
SQ   SEQUENCE   80 AA;  8865 MW;  9BEFD90482647183 CRC64;
     MEARVLWLLV VVLVLGSSSL AVAYQGLATN LCEVPPKDRV DCGYPEITSE QCVNRGCCFD
     SSIHGVPWCF KPLQDTECRF
 
 
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