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Trefoil factor 1 (Breast cancer estrogen-inducible protein) (PNR-2) (Polypeptide P1.A) (hP1.A) (Protein pS2)

 TFF1_HUMAN              Reviewed;          84 AA.
P04155;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
01-NOV-1986, sequence version 1.
20-JUN-2018, entry version 178.
RecName: Full=Trefoil factor 1;
AltName: Full=Breast cancer estrogen-inducible protein;
AltName: Full=PNR-2;
AltName: Full=Polypeptide P1.A;
Short=hP1.A;
AltName: Full=Protein pS2;
Flags: Precursor;
Name=TFF1; Synonyms=BCEI, PS2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6324130; DOI=10.1093/nar/12.6.2861;
Jakowlew S.B., Breathnach R., Jeltsch J.-M., Masiakowski P.,
Chambon P.;
"Sequence of the pS2 mRNA induced by estrogen in the human breast
cancer cell line MCF-7.";
Nucleic Acids Res. 12:2861-2878(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Mammary cancer;
PubMed=3838275; DOI=10.1089/dna.1985.4.11;
Prud'Homme J.-F., Fridlansky F., le Cunff M., Atger M.,
Mercier-Bodart C., Pichon M.-F., Milgrom E.;
"Cloning of a gene expressed in human breast cancer and regulated by
estrogen in MCF-7 cells.";
DNA 4:11-21(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3822834; DOI=10.1093/nar/15.4.1401;
Jeltsch J.-M., Roberts M., Schatz C., Garnier J.-M., Brown A.M.C.,
Chambon P.;
"Structure of the human oestrogen-responsive gene pS2.";
Nucleic Acids Res. 15:1401-1414(1987).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Gastric carcinoma;
PubMed=2311759; DOI=10.1016/0014-5793(90)80572-Z;
Takahashi H., Kida N., Fujii R., Tanaka K., Ohta M., Mori K.,
Hayashi K.;
"Expression of the pS2 gene in human gastric cancer cells derived from
poorly differentiated adenocarcinoma.";
FEBS Lett. 261:283-286(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2185238;
Mori K., Fujii R., Kida N., Takahashi H., Ohkubo S., Fujino M.,
Ohta M., Hayashi K.;
"Complete primary structure of the human estrogen-responsive gene
(pS2) product.";
J. Biochem. 107:73-76(1990).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10950923; DOI=10.1006/geno.2000.6253;
Berry A., Scott H.S., Kudoh J., Talior I., Korostishevsky M.,
Wattenhofer M., Guipponi M., Barras C., Rossier C., Shibuya K.,
Wang J., Kawasaki K., Asakawa S., Minoshima S., Shimizu N.,
Antonarakis S.E., Bonne-Tamir B.;
"Refined localization of autosomal recessive nonsyndromic deafness
DFNB10 locus using 34 novel microsatellite markers, genomic structure,
and exclusion of six known genes in the region.";
Genomics 68:22-29(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, Kidney, and Stomach;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 25-84.
PubMed=3146413;
Rio M.-C., Lepage P., Diemunsch P., Roitsch C., Chambon P.;
"Primary structure of human protein pS2.";
C. R. Acad. Sci. III, Sci. Vie 307:825-831(1988).
[10]
PROTEIN SEQUENCE OF 25-84, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND INTERACTION WITH GKN2.
TISSUE=Stomach;
PubMed=15924415; DOI=10.1021/bi047287n;
Westley B.R., Griffin S.M., May F.E.B.;
"Interaction between TFF1, a gastric tumor suppressor trefoil protein,
and TFIZ1, a Brichos domain-containing protein with homology to SP-
C.";
Biochemistry 44:7967-7975(2005).
[11]
PROTEIN SEQUENCE OF 25-63, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16308573; DOI=10.1172/JCI25342;
Chutipongtanate S., Nakagawa Y., Sritippayawan S., Pittayamateekul J.,
Parichatikanond P., Westley B.R., May F.E., Malasit P.,
Thongboonkerd V.;
"Identification of human urinary trefoil factor 1 as a novel calcium
oxalate crystal growth inhibitor.";
J. Clin. Invest. 115:3613-3622(2005).
[12]
PROTEIN SEQUENCE OF 25-60.
PubMed=3261981; DOI=10.1016/S0006-291X(88)81094-5;
Mori K., Fujii R., Kida N., Ohta M., Hayashi K.;
"Identification of a polypeptide secreted by human breast cancer cells
(MCF-7) as the human estrogen-responsive gene (pS2) product.";
Biochem. Biophys. Res. Commun. 155:366-372(1988).
[13]
PROTEIN SEQUENCE OF 25-39.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[14]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=3041593; DOI=10.1126/science.3041593;
Rio M.C., Bellocq J.-P., Daniel J.Y., Tomasetto C., Lathe R.,
Chenard M.P., Batzenschlager A., Chambon P.;
"Breast cancer-associated pS2 protein: synthesis and secretion by
normal stomach mucosa.";
Science 241:705-708(1988).
[15]
TISSUE SPECIFICITY.
PubMed=16718800;
Shi S.-Q., Cai J.-T., Yang J.-M.;
"Expression of trefoil factors 1 and 2 in precancerous condition and
gastric cancer.";
World J. Gastroenterol. 12:3119-3122(2006).
[16]
TISSUE SPECIFICITY.
PubMed=17143957;
Ren J.L., Luo J.-Y., Lu Y.-P., Wang L., Shi H.-X.;
"Molecular forms of trefoil factor 1 in normal gastric mucosa and its
expression in normal and abnormal gastric tissues.";
World J. Gastroenterol. 12:7361-7364(2006).
[17]
TISSUE SPECIFICITY.
PubMed=17242463; DOI=10.1369/jhc.6A7100.2007;
Madsen J., Nielsen O., Tornoe I., Thim L., Holmskov U.;
"Tissue localization of human trefoil factors 1, 2, and 3.";
J. Histochem. Cytochem. 55:505-513(2007).
[18]
STRUCTURE BY NMR.
PubMed=8521850; DOI=10.1111/j.1432-1033.1995.847_3.x;
Polshakov V.I., Frenkiel T.A., Westley B.R., Chadwick M.P.,
May F.E.B., Carr M.D., Feeney J.;
"NMR-based structural studies of the pNR-2/pS2 single domain trefoil
peptide. Similarities to porcine spasmolytic peptide and evidence for
a monomeric structure.";
Eur. J. Biochem. 233:847-855(1995).
[19]
STRUCTURE BY NMR.
PubMed=9096235; DOI=10.1006/jmbi.1997.0896;
Polshakov V.I., Williams M.A., Gargaro A.R., Frenkiel T.A.,
Westley B.R., Chadwick M.P., May F.E.B., Feeney J.;
"High-resolution solution structure of human pNR-2/pS2: a single
trefoil motif protein.";
J. Mol. Biol. 267:418-432(1997).
[20]
VARIANTS ILE-32; LYS-32; ASP-34; LYS-37; ILE-46 AND VAL-55.
PubMed=10982763; DOI=10.1053/gast.2000.16483;
Park W.-S., Oh R.-R., Park J.-Y., Lee J.-H., Shin M.-S., Kim H.-S.,
Lee H.-K., Kim Y.-S., Kim S.-Y., Lee S.-H., Yoo N.-J., Lee J.-Y.;
"Somatic mutations of the trefoil factor family 1 gene in gastric
cancer.";
Gastroenterology 119:691-698(2000).
[21]
VARIANTS ASP-34 AND LYS-37, AND MUTAGENESIS OF CYS-82.
PubMed=16697734; DOI=10.1053/j.gastro.2006.01.040;
Yio X., Diamond M., Zhang J.-Y., Weinstein H., Wang L.-H., Werther L.,
Itzkowitz S.;
"Trefoil factor family-1 mutations enhance gastric cancer cell
invasion through distinct signaling pathways.";
Gastroenterology 130:1696-1706(2006).
-!- FUNCTION: Stabilizer of the mucous gel overlying the
gastrointestinal mucosa that provides a physical barrier against
various noxious agents. May inhibit the growth of calcium oxalate
crystals in urine. {ECO:0000269|PubMed:16308573}.
-!- SUBUNIT: Heterodimer with GKN2; disulfide linked.
-!- INTERACTION:
O00481:BTN3A1; NbExp=3; IntAct=EBI-743871, EBI-2809309;
Q6UX41:BTNL8; NbExp=3; IntAct=EBI-743871, EBI-4314379;
Q6UXZ3:CD300LD; NbExp=3; IntAct=EBI-743871, EBI-4314468;
Q96PJ5:FCRL4; NbExp=3; IntAct=EBI-743871, EBI-4314687;
Q9NYZ4:SIGLEC8; NbExp=3; IntAct=EBI-743871, EBI-4314991;
Q9UMX0:UBQLN1; NbExp=3; IntAct=EBI-743871, EBI-741480;
P15622-3:ZNF250; NbExp=3; IntAct=EBI-743871, EBI-10177272;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15924415,
ECO:0000269|PubMed:3041593}.
-!- TISSUE SPECIFICITY: Found in stomach, with highest levels in the
upper gastric mucosal cells (at protein level). Detected in goblet
cells of the small and large intestine and rectum, small
submucosal glands in the esophagus, mucous acini of the sublingual
gland, submucosal glands of the trachea, and epithelial cells
lining the exocrine pancreatic ducts but not in the remainder of
the pancreas (at protein level). Scattered expression is detected
in the epithelial cells of the gallbladder and submucosal glands
of the vagina, and weak expression is observed in the bronchial
goblet cells of the pseudostratified epithelia in the respiratory
system (at protein level). Detected in urine (at protein level).
Strongly expressed in breast cancer but at low levels in normal
mammary tissue. It is regulated by estrogen in MCF-7 cells. Strong
expression found in normal gastric mucosa and in the regenerative
tissues surrounding ulcerous lesions of gastrointestinal tract,
but lower expression found in gastric cancer (at protein level).
{ECO:0000269|PubMed:15924415, ECO:0000269|PubMed:16308573,
ECO:0000269|PubMed:16718800, ECO:0000269|PubMed:17143957,
ECO:0000269|PubMed:17242463, ECO:0000269|PubMed:3041593,
ECO:0000269|PubMed:3838275}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TFF1ID201.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X00474; CAA25155.1; -; mRNA.
EMBL; M12075; AAA52402.1; -; mRNA.
EMBL; X05030; CAA28695.1; -; Genomic_DNA.
EMBL; X05321; CAA28695.1; JOINED; Genomic_DNA.
EMBL; X05322; CAA28695.1; JOINED; Genomic_DNA.
EMBL; X52003; CAA36254.1; -; mRNA.
EMBL; AB038162; BAB13729.1; -; Genomic_DNA.
EMBL; AP001746; BAA95532.1; -; Genomic_DNA.
EMBL; BC032811; AAH32811.1; -; mRNA.
CCDS; CCDS13685.1; -.
PIR; A26667; A26667.
RefSeq; NP_003216.1; NM_003225.2.
UniGene; Hs.162807; -.
PDB; 1HI7; NMR; -; A/B=25-84.
PDB; 1PS2; NMR; -; A=25-84.
PDBsum; 1HI7; -.
PDBsum; 1PS2; -.
ProteinModelPortal; P04155; -.
SMR; P04155; -.
BioGrid; 112889; 21.
IntAct; P04155; 18.
MINT; P04155; -.
STRING; 9606.ENSP00000291527; -.
BioMuta; TFF1; -.
DMDM; 131127; -.
MaxQB; P04155; -.
PaxDb; P04155; -.
PeptideAtlas; P04155; -.
PRIDE; P04155; -.
ProteomicsDB; 51666; -.
DNASU; 7031; -.
Ensembl; ENST00000291527; ENSP00000291527; ENSG00000160182.
GeneID; 7031; -.
KEGG; hsa:7031; -.
UCSC; uc002zax.2; human.
CTD; 7031; -.
DisGeNET; 7031; -.
EuPathDB; HostDB:ENSG00000160182.2; -.
GeneCards; TFF1; -.
HGNC; HGNC:11755; TFF1.
HPA; CAB002170; -.
HPA; HPA003425; -.
MIM; 113710; gene.
neXtProt; NX_P04155; -.
OpenTargets; ENSG00000160182; -.
PharmGKB; PA36470; -.
eggNOG; ENOG410J868; Eukaryota.
eggNOG; ENOG410Z7FU; LUCA.
GeneTree; ENSGT00840000129881; -.
HOGENOM; HOG000121778; -.
HOVERGEN; HBG004364; -.
InParanoid; P04155; -.
KO; K22456; -.
OMA; PEEECEF; -.
OrthoDB; EOG091G0XBT; -.
PhylomeDB; P04155; -.
TreeFam; TF336092; -.
Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
SIGNOR; P04155; -.
ChiTaRS; TFF1; human.
EvolutionaryTrace; P04155; -.
GeneWiki; Trefoil_factor_1; -.
GenomeRNAi; 7031; -.
PRO; PR:P04155; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000160182; -.
CleanEx; HS_TFF1; -.
Genevisible; P04155; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
GO; GO:0030154; P:cell differentiation; IEA:Ensembl.
GO; GO:0007586; P:digestion; IBA:GO_Central.
GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
GO; GO:0010039; P:response to iron ion; IEA:Ensembl.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IBA:GO_Central.
CDD; cd00111; Trefoil; 1.
InterPro; IPR017994; P_trefoil_chordata.
InterPro; IPR017957; P_trefoil_CS.
InterPro; IPR000519; P_trefoil_dom.
InterPro; IPR028824; TFF1.
PANTHER; PTHR13826:SF18; PTHR13826:SF18; 1.
Pfam; PF00088; Trefoil; 1.
PRINTS; PR00680; PTREFOIL.
SMART; SM00018; PD; 1.
PROSITE; PS00025; P_TREFOIL_1; 1.
PROSITE; PS51448; P_TREFOIL_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Growth factor; Polymorphism; Reference proteome;
Secreted; Signal.
SIGNAL 1 24 {ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:15924415,
ECO:0000269|PubMed:16308573,
ECO:0000269|PubMed:3146413,
ECO:0000269|PubMed:3261981}.
CHAIN 25 84 Trefoil factor 1.
/FTId=PRO_0000023456.
DOMAIN 29 72 P-type. {ECO:0000255|PROSITE-
ProRule:PRU00779}.
COMPBIAS 79 83 Glu-rich (acidic).
DISULFID 31 57
DISULFID 41 56
DISULFID 51 68
VARIANT 22 22 T -> I (in dbSNP:rs34795821).
/FTId=VAR_053563.
VARIANT 32 32 T -> I (in a gastric carcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:10982763}.
/FTId=VAR_015281.
VARIANT 32 32 T -> K (in a gastric carcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:10982763}.
/FTId=VAR_015282.
VARIANT 34 34 A -> D (in a gastric carcinoma sample;
somatic mutation; abolishes inhibition of
gastric cancer cell growth; abolishes
inhibition of apoptosis in
gasterointestinal epithelial cells;
increases invasive activity in epithelial
cells). {ECO:0000269|PubMed:10982763,
ECO:0000269|PubMed:16697734}.
/FTId=VAR_015283.
VARIANT 37 37 E -> K (in a gastric carcinoma sample;
somatic mutation; abolishes inhibition of
gastric cancer cell growth; abolishes
inhibition of apoptosis in
gasterointestinal epithelial cells;
increases invasive activity in epithelial
cells). {ECO:0000269|PubMed:10982763,
ECO:0000269|PubMed:16697734}.
/FTId=VAR_015284.
VARIANT 46 46 V -> I (in a gastric adenoma sample;
somatic mutation).
{ECO:0000269|PubMed:10982763}.
/FTId=VAR_015285.
VARIANT 55 55 G -> V (in a gastric carcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:10982763}.
/FTId=VAR_015286.
MUTAGEN 82 82 C->S: Abolishes inhibition of gastric
cancer cell growth.
{ECO:0000269|PubMed:16697734}.
STRAND 28 30 {ECO:0000244|PDB:1HI7}.
TURN 35 37 {ECO:0000244|PDB:1HI7}.
STRAND 40 42 {ECO:0000244|PDB:1HI7}.
HELIX 48 52 {ECO:0000244|PDB:1HI7}.
TURN 53 55 {ECO:0000244|PDB:1HI7}.
STRAND 61 65 {ECO:0000244|PDB:1HI7}.
STRAND 67 69 {ECO:0000244|PDB:1HI7}.
STRAND 72 74 {ECO:0000244|PDB:1HI7}.
STRAND 79 82 {ECO:0000244|PDB:1HI7}.
SEQUENCE 84 AA; 9150 MW; 65198523BAD6EBC7 CRC64;
MATMENKVIC ALVLVSMLAL GTLAEAQTET CTVAPRERQN CGFPGVTPSQ CANKGCCFDD
TVRGVPWCFY PNTIDVPPEE ECEF


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