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TFF3_RAT
ID   TFF3_RAT                Reviewed;          81 AA.
AC   Q03191; Q68FZ2;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 135.
DE   RecName: Full=Trefoil factor 3;
DE   AltName: Full=Intestinal trefoil factor;
DE            Short=rITF;
DE   AltName: Full=Polypeptide P1.B;
DE            Short=rP1.B;
DE   Flags: Precursor;
GN   Name=Tff3; Synonyms=Itf;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Intestine;
RX   PubMed=1763017; DOI=10.1073/pnas.88.24.11017;
RA   Suemori S., Lynch-Devaney K., Podolsky D.K.;
RT   "Identification and characterization of rat intestinal trefoil factor:
RT   tissue- and cell-specific member of the trefoil protein family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:11017-11021(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1439565; DOI=10.3109/00365529209095975;
RA   Poulsom R., Chinery R., Sarraf C., Lalani E.N., Stamp G., Elia G.,
RA   Wright N.;
RT   "Trefoil peptide expression in intestinal adaptation and renewal.";
RL   Scand. J. Gastroenterol. Suppl. 192:17-28(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Wistar; TISSUE=Brain;
RX   PubMed=8750886; DOI=10.1016/0169-328x(95)00137-h;
RA   Probst J.C., Skutella T., Mueller-Schmid A., Jirikowski G.F., Hoffmann W.;
RT   "Molecular and cellular analysis of rP1.B in the rat hypothalamus: in situ
RT   hybridization and immunohistochemistry of a new P-domain neuropeptide.";
RL   Brain Res. Mol. Brain Res. 33:269-276(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-80, AND TISSUE SPECIFICITY.
RC   STRAIN=Wistar; TISSUE=Ileum;
RX   PubMed=1637322; DOI=10.1042/bj2850005;
RA   Chinery R., Poulson R., Rogers L.A., Jeffery R.E., Longcroft J.M.,
RA   Hanby A.M., Wright N.A.;
RT   "Localization of intestinal trefoil-factor mRNA in rat stomach and
RT   intestine by hybridization in situ.";
RL   Biochem. J. 285:5-8(1992).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=7721858; DOI=10.1074/jbc.270.16.9353;
RA   Sands B.E., Ogata H., Lynch-Devaney K., Debeaumont M., Ezzell R.M.,
RA   Podolsky D.K.;
RT   "Molecular cloning of the rat intestinal trefoil factor gene.
RT   Characterization of an intestinal goblet cell-associated promoter.";
RL   J. Biol. Chem. 270:9353-9361(1995).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-81, AND SUBCELLULAR LOCATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Small intestine;
RX   PubMed=9299425; DOI=10.1006/bbrc.1997.7144;
RA   Tan X.D., Hsueh W., Chang H., Wei K.-R., Gonzalez-Crussi F.;
RT   "Characterization of a putative receptor for intestinal trefoil factor in
RT   rat small intestine: identification by in situ binding and ligand
RT   blotting.";
RL   Biochem. Biophys. Res. Commun. 237:673-677(1997).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=8454642; DOI=10.1016/s0021-9258(18)53305-6;
RA   Podolsky D.K., Lynch-Devaney K., Stow J.L., Oates P., Murgue B.,
RA   Debeaumont M., Sands B.E., Mahida Y.R.;
RT   "Identification of human intestinal trefoil factor. Goblet cell-specific
RT   expression of a peptide targeted for apical secretion.";
RL   J. Biol. Chem. 268:6694-6702(1993).
RN   [9]
RP   INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=19076725; DOI=10.1111/j.1476-5381.2008.00044.x;
RA   Hernandez C., Santamatilde E., McCreath K.J., Cervera A.M., Diez I.,
RA   Ortiz-Masia D., Martinez N., Calatayud S., Esplugues J.V., Barrachina M.D.;
RT   "Induction of trefoil factor (TFF)1, TFF2 and TFF3 by hypoxia is mediated
RT   by hypoxia inducible factor-1: implications for gastric mucosal healing.";
RL   Br. J. Pharmacol. 156:262-272(2009).
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:0000269|PubMed:1763017, ECO:0000269|PubMed:9299425}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q07654}.
CC   -!- TISSUE SPECIFICITY: Expressed in goblet cells of the intestines, and
CC       colon, in paraventricular hypothalamus and supraoptic nuclei. Weakly
CC       expressed in gastric epithelial cells (at protein level). Expressed by
CC       goblet cells of small and large intestinal epithelia, kidney and
CC       stomach. Expressed in the paraventricular hypothalamus, arcuate nucleus
CC       and amygdala of the brain. Weakly expressed in gastric epithelial
CC       cells. {ECO:0000269|PubMed:1637322, ECO:0000269|PubMed:1763017,
CC       ECO:0000269|PubMed:19076725, ECO:0000269|PubMed:8454642,
CC       ECO:0000269|PubMed:8750886}.
CC   -!- INDUCTION: Up-regulated by hypoxia in gastric epithelial cells. Up-
CC       regulated by hypoxia-inducible factor 1 alpha (HIF1A).
CC       {ECO:0000269|PubMed:19076725}.
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DR   EMBL; M80826; AAA42270.1; -; mRNA.
DR   EMBL; S49317; AAB24079.2; -; mRNA.
DR   EMBL; U48825; AAC52439.1; -; mRNA.
DR   EMBL; BC078873; AAH78873.1; -; mRNA.
DR   EMBL; X66956; CAA47378.1; -; mRNA.
DR   EMBL; U20984; AAB01063.1; -; Genomic_DNA.
DR   EMBL; AF012534; AAB71352.1; -; mRNA.
DR   PIR; A41441; A41441.
DR   PIR; A56366; A56366.
DR   PIR; JC5623; JC5623.
DR   PIR; S23963; S23963.
DR   RefSeq; NP_037174.2; NM_013042.2.
DR   AlphaFoldDB; Q03191; -.
DR   SMR; Q03191; -.
DR   STRING; 10116.ENSRNOP00000060620; -.
DR   PaxDb; Q03191; -.
DR   GeneID; 25563; -.
DR   KEGG; rno:25563; -.
DR   UCSC; RGD:3847; rat.
DR   CTD; 7033; -.
DR   RGD; 3847; Tff3.
DR   eggNOG; ENOG502SV7V; Eukaryota.
DR   InParanoid; Q03191; -.
DR   OrthoDB; 1563185at2759; -.
DR   PhylomeDB; Q03191; -.
DR   TreeFam; TF336092; -.
DR   PRO; PR:Q03191; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005576; C:extracellular region; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030141; C:secretory granule; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IBA:GO_Central.
DR   GO; GO:0010906; P:regulation of glucose metabolic process; ISO:RGD.
DR   GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR   GO; GO:0042060; P:wound healing; TAS:RGD.
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   1: Evidence at protein level;
KW   Cytoplasm; Disulfide bond; Extracellular matrix; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..81
FT                   /note="Trefoil factor 3"
FT                   /id="PRO_0000023467"
FT   DOMAIN          31..74
FT                   /note="P-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   DISULFID        33..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   DISULFID        43..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   DISULFID        53..70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   DISULFID        79
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   CONFLICT        8
FT                   /note="T -> I (in Ref. 3; AAC52439, 4; AAH78873 and 6;
FT                   AAB01063)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        35
FT                   /note="V -> A (in Ref. 1; AAA42270)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        37
FT                   /note="A -> T (in Ref. 1; AAA42270)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44
FT                   /note="G -> N (in Ref. 1; AAA42270)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        81
FT                   /note="F -> LDPA (in Ref. 2; AAB24079)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   81 AA;  8944 MW;  915052312C7B517E CRC64;
     METRAFWTTL LLVLVAGSSC KAQEFVGLSP SQCMVPANVR VDCGYPTVTS EQCNNRGCCF
     DSSIPNVPWC FKPLQETECT F
 
 
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