ID   TFF3_PIG                Reviewed;          80 AA.
AC   Q29183;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 69.
DE   RecName: Full=Trefoil factor 3;
DE   AltName: Full=Intestinal trefoil factor;
DE   Flags: Precursor;
GN   Name=TFF3; Synonyms=ITF;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Small intestine;
RX   PubMed=8672129; DOI=10.1007/s003359900153;
RA   Winteroe A.K., Fredholm M., Davies W.;
RT   "Evaluation and characterization of a porcine small intestine cDNA library:
RT   analysis of 839 clones.";
RL   Mamm. Genome 7:509-517(1996).
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; F14493; CAA23086.1; -; mRNA.
DR   STRING; 9823.ENSSSCP00000024677; -.
DR   PaxDb; Q29183; -.
DR   PeptideAtlas; Q29183; -.
DR   eggNOG; ENOG502SV7V; Eukaryota.
DR   InParanoid; Q29183; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..80
FT                   /note="Trefoil factor 3"
FT                   /id="PRO_0000376811"
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;  8752 MW;  4DCB9F9123578678 CRC64;
     MEARMFWLLV VLLALASSSS AGEYVGLSAN QCAVPAKDRV DCGYPQVTPE QCNNRGCCFD
     SSIXGVPWCF KPLQETECTF