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TFF2_CANLF
ID   TFF2_CANLF              Reviewed;         129 AA.
AC   Q863J2;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Trefoil factor 2;
DE   Flags: Precursor;
GN   Name=TFF2;
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=Gastric mucosa;
RA   Campbell B.G., Jabbes M.;
RT   "Canine trefoil factor 2 (TFF2) mRNA from gastric mucosa.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibits gastrointestinal motility and gastric acid
CC       secretion. Could function as a structural component of gastric mucus,
CC       possibly by stabilizing glycoproteins in the mucus gel through
CC       interactions with carbohydrate side chains (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR   EMBL; AY264843; AAP21820.1; -; mRNA.
DR   RefSeq; NP_001002991.1; NM_001002991.1.
DR   AlphaFoldDB; Q863J2; -.
DR   SMR; Q863J2; -.
DR   STRING; 9615.ENSCAFP00000057618; -.
DR   PaxDb; Q863J2; -.
DR   PRIDE; Q863J2; -.
DR   GeneID; 403489; -.
DR   KEGG; cfa:403489; -.
DR   CTD; 7032; -.
DR   eggNOG; ENOG502S5ZY; Eukaryota.
DR   InParanoid; Q863J2; -.
DR   OrthoDB; 1563185at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0031723; F:CXCR4 chemokine receptor binding; IBA:GO_Central.
DR   GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IBA:GO_Central.
DR   GO; GO:0060455; P:negative regulation of gastric acid secretion; IBA:GO_Central.
DR   CDD; cd00111; Trefoil; 2.
DR   Gene3D; 4.10.110.10; -; 2.
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; 2.
DR   PRINTS; PR00680; PTREFOIL.
DR   SMART; SM00018; PD; 2.
DR   SUPFAM; SSF57492; SSF57492; 2.
DR   PROSITE; PS00025; P_TREFOIL_1; 2.
DR   PROSITE; PS51448; P_TREFOIL_2; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Pyrrolidone carboxylic acid; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..129
FT                   /note="Trefoil factor 2"
FT                   /id="PRO_0000023459"
FT   DOMAIN          29..73
FT                   /note="P-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   DOMAIN          79..122
FT                   /note="P-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   MOD_RES         24
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P01359"
FT   DISULFID        29..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   DISULFID        31..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        81..107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   DISULFID        91..106
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   DISULFID        101..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
SQ   SEQUENCE   129 AA;  14102 MW;  D0AE5DAB4CE6ABE0 CRC64;
     MGPRGLQLLA VLLALGLCAP AGAQKPSACQ CSRIEASHRK NCGFPGISAS ECFNTGCCFD
     SRVPNVPWCF HPLPKQESEQ CVMEVAARKN CGYPGISPQE CASRNCCFSD TIRNVPWCFF
     PILNQDCHY
 
 
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