TFF2_PIG
ID TFF2_PIG Reviewed; 127 AA.
AC P01359;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 4.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Trefoil factor 2;
DE AltName: Full=Pancreatic spasmolytic polypeptide;
DE Short=PSP;
DE AltName: Full=Spasmolytic polypeptide;
DE Short=SP;
DE Flags: Precursor; Fragment;
GN Name=TFF2; Synonyms=SML1;
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 [MRNA].
RX PubMed=2303034; DOI=10.1002/j.1460-2075.1990.tb08125.x;
RA Tomasetto C., Rio M.C., Gautier C., Wolf C., Hareuveni M., Chambon P.,
RA Lathe R.;
RT "hSP, the domain-duplicated homolog of pS2 protein, is co-expressed with
RT pS2 in stomach but not in breast carcinoma.";
RL EMBO J. 9:407-414(1990).
RN [2]
RP PROTEIN SEQUENCE OF 22-127, AND PYROGLUTAMATE FORMATION AT GLN-22.
RX PubMed=2857575; DOI=10.1016/0167-4838(85)90226-2;
RA Thim L., Thomsen J., Christensen M., Joergensen K.H.;
RT "The amino acid sequence of pancreatic spasmolytic polypeptide.";
RL Biochim. Biophys. Acta 827:410-418(1985).
RN [3]
RP SEQUENCE REVISION TO 69; 84; 89 AND 95.
RX PubMed=2804132; DOI=10.1016/0167-4838(89)90288-4;
RA Rose K., Savoy L.-A., Thim L., Christensen M., Joergensen K.H.;
RT "Revised amino acid sequence of pancreatic spasmolytic polypeptide exhibits
RT greater similarity with an inducible pS2 peptide found in a human breast
RT cancer cell line.";
RL Biochim. Biophys. Acta 998:297-300(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=8302836; DOI=10.1073/pnas.91.3.1084;
RA De A., Brown D., Gorman M., Carr M., Sanderson M.R., Freemont P.S.;
RT "Crystal structure of a disulfide-linked 'trefoil' motif found in a large
RT family of putative growth factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1084-1088(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=1518804; DOI=10.1002/prot.340130408;
RA Gajhede M., Thim L., Joergensen K.H., Melberg S.G.;
RT "Pancreatic spasmolytic polypeptide: crystallization, circular dichroism
RT analysis, and preliminary X-ray diffraction studies.";
RL Proteins 13:364-368(1992).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC TISSUE=Pancreas;
RX PubMed=8081739; DOI=10.1016/0969-2126(93)90014-8;
RA Gajhede M., Petersen T.N., Henriksen A., Petersen J.F.W., Dauter Z.,
RA Wilson K.S., Thim L.;
RT "Pancreatic spasmolytic polypeptide: first three-dimensional structure of a
RT member of the mammalian trefoil family of peptides.";
RL Structure 1:253-262(1993).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RC TISSUE=Pancreas;
RX PubMed=15299636; DOI=10.1107/s0907444996001345;
RA Petersen T.N., Henriksen A., Gajhede M.;
RT "Structure of porcine pancreatic spasmolytic polypeptide at 1.95-A
RT resolution.";
RL Acta Crystallogr. D 52:730-737(1996).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=1536842; DOI=10.1021/bi00122a015;
RA Carr M.D.;
RT "1H NMR-based determination of the secondary structure of porcine
RT pancreatic spasmolytic polypeptide: one of a new family of 'trefoil' motif
RT containing cell growth factors.";
RL Biochemistry 31:1998-2004(1992).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=8134374; DOI=10.1073/pnas.91.6.2206;
RA Carr M.D., Bauer C.J., Gradwell M.J., Feeney J.;
RT "Solution structure of a trefoil-motif-containing cell growth factor,
RT porcine spasmolytic protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2206-2210(1994).
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.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Found in pancreas.
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DR EMBL; X51696; CAA35993.1; -; mRNA.
DR PIR; S12373; JOPGP.
DR PDB; 1PCP; NMR; -; A=23-127.
DR PDB; 1POS; X-ray; 2.60 A; A/B=23-127.
DR PDB; 1PSP; X-ray; 2.50 A; A/B=23-127.
DR PDB; 2PSP; X-ray; 1.95 A; A/B=23-127.
DR PDBsum; 1PCP; -.
DR PDBsum; 1POS; -.
DR PDBsum; 1PSP; -.
DR PDBsum; 2PSP; -.
DR AlphaFoldDB; P01359; -.
DR BMRB; P01359; -.
DR SMR; P01359; -.
DR STRING; 9823.ENSSSCP00000025323; -.
DR PaxDb; P01359; -.
DR eggNOG; ENOG502S5ZY; Eukaryota.
DR InParanoid; P01359; -.
DR EvolutionaryTrace; P01359; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:0008083; F:growth factor activity; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Growth factor;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL <1..21
FT /evidence="ECO:0000269|PubMed:2857575"
FT CHAIN 22..127
FT /note="Trefoil factor 2"
FT /id="PRO_0000023462"
FT DOMAIN 27..71
FT /note="P-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 77..120
FT /note="P-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT MOD_RES 22
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2857575"
FT DISULFID 27..125
FT DISULFID 29..56
FT DISULFID 40..55
FT DISULFID 50..67
FT DISULFID 79..105
FT DISULFID 89..104
FT DISULFID 99..116
FT CONFLICT 82
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="R -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:2PSP"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:2PSP"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:2PSP"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1PCP"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2PSP"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1PCP"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:2PSP"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2PSP"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:2PSP"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1PCP"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:2PSP"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2PSP"
SQ SEQUENCE 127 AA; 13834 MW; F9012134CE13CF5C CRC64;
EPQRPAPGHP PPAGAVCLTG AQKPAACRCS RQDPKNRVNC GFPGITSDQC FTSGCCFDSQ
VPGVPWCFKP LPAQESEECV MEVSARKNCG YPGISPEDCA RRNCCFSDTI PEVPWCFFPM
SVEDCHY
