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P04155

- TFF1_HUMAN

UniProt

P04155 - TFF1_HUMAN

Protein

Trefoil factor 1

Gene

TFF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. carbohydrate metabolic process Source: ProtInc
    2. cell differentiation Source: Ensembl
    3. digestion Source: ProtInc
    4. maintenance of gastrointestinal epithelium Source: Ensembl
    5. negative regulation of cell proliferation Source: Ensembl
    6. response to estradiol Source: BHF-UCL
    7. response to iron ion Source: Ensembl
    8. response to peptide hormone Source: Ensembl

    Keywords - Molecular functioni

    Growth factor

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trefoil factor 1
    Alternative name(s):
    Breast cancer estrogen-inducible protein
    PNR-2
    Polypeptide P1.A
    Short name:
    hP1.A
    Protein pS2
    Gene namesi
    Name:TFF1
    Synonyms:BCEI, PS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:11755. TFF1.

    Subcellular locationi

    Secreted 2 Publications

    GO - Cellular componenti

    1. extracellular space Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi82 – 821C → S: Abolishes inhibition of gastric cancer cell growth. 1 Publication

    Organism-specific databases

    PharmGKBiPA36470.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24245 PublicationsAdd
    BLAST
    Chaini25 – 8460Trefoil factor 1PRO_0000023456Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi31 ↔ 57
    Disulfide bondi41 ↔ 56
    Disulfide bondi51 ↔ 68

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiP04155.
    PaxDbiP04155.
    PeptideAtlasiP04155.
    PRIDEiP04155.

    Expressioni

    Tissue specificityi

    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).7 Publications

    Gene expression databases

    BgeeiP04155.
    CleanExiHS_TFF1.
    GenevestigatoriP04155.

    Organism-specific databases

    HPAiCAB002170.
    HPA003425.

    Interactioni

    Subunit structurei

    Heterodimer with GKN2; disulfide linked.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BTN3A1O004813EBI-743871,EBI-2809309
    BTNL8Q6UX413EBI-743871,EBI-4314379
    CD300LDQ6UXZ33EBI-743871,EBI-4314468
    FCRL4Q96PJ53EBI-743871,EBI-4314687
    SIGLEC8Q9NYZ43EBI-743871,EBI-4314991

    Protein-protein interaction databases

    BioGridi112889. 16 interactions.
    IntActiP04155. 7 interactions.
    MINTiMINT-1461530.
    STRINGi9606.ENSP00000291527.

    Structurei

    Secondary structure

    1
    84
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 303
    Turni35 – 373
    Beta strandi40 – 423
    Helixi48 – 525
    Turni53 – 553
    Beta strandi61 – 655
    Beta strandi67 – 693
    Beta strandi72 – 743
    Beta strandi79 – 824

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HI7NMR-A/B25-84[»]
    1PS2NMR-A25-84[»]
    ProteinModelPortaliP04155.
    SMRiP04155. Positions 25-84.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04155.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 7244P-typePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi79 – 835Glu-rich (acidic)

    Sequence similaritiesi

    Contains 1 P-type (trefoil) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG46001.
    HOGENOMiHOG000121778.
    HOVERGENiHBG004364.
    InParanoidiP04155.
    OMAiPEEECEF.
    OrthoDBiEOG70W3GT.
    PhylomeDBiP04155.
    TreeFamiTF336092.

    Family and domain databases

    Gene3Di4.10.110.10. 1 hit.
    InterProiIPR000519. P_trefoil.
    IPR017994. P_trefoil_chordata.
    IPR017957. P_trefoil_CS.
    IPR028824. TFF1.
    [Graphical view]
    PANTHERiPTHR13826:SF15. PTHR13826:SF15. 1 hit.
    PfamiPF00088. Trefoil. 1 hit.
    [Graphical view]
    PRINTSiPR00680. PTREFOIL.
    SMARTiSM00018. PD. 1 hit.
    [Graphical view]
    SUPFAMiSSF57492. SSF57492. 1 hit.
    PROSITEiPS00025. P_TREFOIL_1. 1 hit.
    PS51448. P_TREFOIL_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P04155-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATMENKVIC ALVLVSMLAL GTLAEAQTET CTVAPRERQN CGFPGVTPSQ   50
    CANKGCCFDD TVRGVPWCFY PNTIDVPPEE ECEF 84
    Length:84
    Mass (Da):9,150
    Last modified:November 1, 1986 - v1
    Checksum:i65198523BAD6EBC7
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221T → I.
    Corresponds to variant rs34795821 [ dbSNP | Ensembl ].
    VAR_053563
    Natural varianti32 – 321T → I in a gastric carcinoma sample; somatic mutation. 1 Publication
    VAR_015281
    Natural varianti32 – 321T → K in a gastric carcinoma sample; somatic mutation. 1 Publication
    VAR_015282
    Natural varianti34 – 341A → 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. 2 Publications
    VAR_015283
    Natural varianti37 – 371E → 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. 2 Publications
    VAR_015284
    Natural varianti46 – 461V → I in a gastric adenoma sample; somatic mutation. 1 Publication
    VAR_015285
    Natural varianti55 – 551G → V in a gastric carcinoma sample; somatic mutation. 1 Publication
    VAR_015286

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00474 mRNA. Translation: CAA25155.1.
    M12075 mRNA. Translation: AAA52402.1.
    X05030, X05321, X05322 Genomic DNA. Translation: CAA28695.1.
    X52003 mRNA. Translation: CAA36254.1.
    AB038162 Genomic DNA. Translation: BAB13729.1.
    AP001746 Genomic DNA. Translation: BAA95532.1.
    BC032811 mRNA. Translation: AAH32811.1.
    CCDSiCCDS13685.1.
    PIRiA26667.
    RefSeqiNP_003216.1. NM_003225.2.
    UniGeneiHs.162807.

    Genome annotation databases

    EnsembliENST00000291527; ENSP00000291527; ENSG00000160182.
    GeneIDi7031.
    KEGGihsa:7031.
    UCSCiuc002zax.1. human.

    Polymorphism databases

    DMDMi131127.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00474 mRNA. Translation: CAA25155.1 .
    M12075 mRNA. Translation: AAA52402.1 .
    X05030 , X05321 , X05322 Genomic DNA. Translation: CAA28695.1 .
    X52003 mRNA. Translation: CAA36254.1 .
    AB038162 Genomic DNA. Translation: BAB13729.1 .
    AP001746 Genomic DNA. Translation: BAA95532.1 .
    BC032811 mRNA. Translation: AAH32811.1 .
    CCDSi CCDS13685.1.
    PIRi A26667.
    RefSeqi NP_003216.1. NM_003225.2.
    UniGenei Hs.162807.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HI7 NMR - A/B 25-84 [» ]
    1PS2 NMR - A 25-84 [» ]
    ProteinModelPortali P04155.
    SMRi P04155. Positions 25-84.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112889. 16 interactions.
    IntActi P04155. 7 interactions.
    MINTi MINT-1461530.
    STRINGi 9606.ENSP00000291527.

    Polymorphism databases

    DMDMi 131127.

    Proteomic databases

    MaxQBi P04155.
    PaxDbi P04155.
    PeptideAtlasi P04155.
    PRIDEi P04155.

    Protocols and materials databases

    DNASUi 7031.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000291527 ; ENSP00000291527 ; ENSG00000160182 .
    GeneIDi 7031.
    KEGGi hsa:7031.
    UCSCi uc002zax.1. human.

    Organism-specific databases

    CTDi 7031.
    GeneCardsi GC21M043782.
    HGNCi HGNC:11755. TFF1.
    HPAi CAB002170.
    HPA003425.
    MIMi 113710. gene.
    neXtProti NX_P04155.
    PharmGKBi PA36470.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46001.
    HOGENOMi HOG000121778.
    HOVERGENi HBG004364.
    InParanoidi P04155.
    OMAi PEEECEF.
    OrthoDBi EOG70W3GT.
    PhylomeDBi P04155.
    TreeFami TF336092.

    Miscellaneous databases

    ChiTaRSi TFF1. human.
    EvolutionaryTracei P04155.
    GeneWikii Trefoil_factor_1.
    GenomeRNAii 7031.
    NextBioi 27469.
    PROi P04155.
    SOURCEi Search...

    Gene expression databases

    Bgeei P04155.
    CleanExi HS_TFF1.
    Genevestigatori P04155.

    Family and domain databases

    Gene3Di 4.10.110.10. 1 hit.
    InterProi IPR000519. P_trefoil.
    IPR017994. P_trefoil_chordata.
    IPR017957. P_trefoil_CS.
    IPR028824. TFF1.
    [Graphical view ]
    PANTHERi PTHR13826:SF15. PTHR13826:SF15. 1 hit.
    Pfami PF00088. Trefoil. 1 hit.
    [Graphical view ]
    PRINTSi PR00680. PTREFOIL.
    SMARTi SM00018. PD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57492. SSF57492. 1 hit.
    PROSITEi PS00025. P_TREFOIL_1. 1 hit.
    PS51448. P_TREFOIL_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the pS2 mRNA induced by estrogen in the human breast cancer cell line MCF-7."
      Jakowlew S.B., Breathnach R., Jeltsch J.-M., Masiakowski P., Chambon P.
      Nucleic Acids Res. 12:2861-2878(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of a gene expressed in human breast cancer and regulated by estrogen in MCF-7 cells."
      Prud'Homme J.-F., Fridlansky F., le Cunff M., Atger M., Mercier-Bodart C., Pichon M.-F., Milgrom E.
      DNA 4:11-21(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Mammary cancer.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Expression of the pS2 gene in human gastric cancer cells derived from poorly differentiated adenocarcinoma."
      Takahashi H., Kida N., Fujii R., Tanaka K., Ohta M., Mori K., Hayashi K.
      FEBS Lett. 261:283-286(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Gastric carcinoma.
    5. "Complete primary structure of the human estrogen-responsive gene (pS2) product."
      Mori K., Fujii R., Kida N., Takahashi H., Ohkubo S., Fujino M., Ohta M., Hayashi K.
      J. Biochem. 107:73-76(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "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."
      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.
      Genomics 68:22-29(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "The DNA sequence of human chromosome 21."
      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.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon, Kidney and Stomach.
    9. "Primary structure of human protein pS2."
      Rio M.-C., Lepage P., Diemunsch P., Roitsch C., Chambon P.
      C. R. Acad. Sci. III, Sci. Vie 307:825-831(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-84.
    10. "Interaction between TFF1, a gastric tumor suppressor trefoil protein, and TFIZ1, a Brichos domain-containing protein with homology to SP-C."
      Westley B.R., Griffin S.M., May F.E.B.
      Biochemistry 44:7967-7975(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-84, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH GKN2.
      Tissue: Stomach.
    11. "Identification of human urinary trefoil factor 1 as a novel calcium oxalate crystal growth inhibitor."
      Chutipongtanate S., Nakagawa Y., Sritippayawan S., Pittayamateekul J., Parichatikanond P., Westley B.R., May F.E., Malasit P., Thongboonkerd V.
      J. Clin. Invest. 115:3613-3622(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-63, FUNCTION, TISSUE SPECIFICITY.
    12. "Identification of a polypeptide secreted by human breast cancer cells (MCF-7) as the human estrogen-responsive gene (pS2) product."
      Mori K., Fujii R., Kida N., Ohta M., Hayashi K.
      Biochem. Biophys. Res. Commun. 155:366-372(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-60.
    13. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-39.
    14. "Breast cancer-associated pS2 protein: synthesis and secretion by normal stomach mucosa."
      Rio M.C., Bellocq J.-P., Daniel J.Y., Tomasetto C., Lathe R., Chenard M.P., Batzenschlager A., Chambon P.
      Science 241:705-708(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    15. "Expression of trefoil factors 1 and 2 in precancerous condition and gastric cancer."
      Shi S.-Q., Cai J.-T., Yang J.-M.
      World J. Gastroenterol. 12:3119-3122(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    16. "Molecular forms of trefoil factor 1 in normal gastric mucosa and its expression in normal and abnormal gastric tissues."
      Ren J.L., Luo J.-Y., Lu Y.-P., Wang L., Shi H.-X.
      World J. Gastroenterol. 12:7361-7364(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    17. "Tissue localization of human trefoil factors 1, 2, and 3."
      Madsen J., Nielsen O., Tornoe I., Thim L., Holmskov U.
      J. Histochem. Cytochem. 55:505-513(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    18. "NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure."
      Polshakov V.I., Frenkiel T.A., Westley B.R., Chadwick M.P., May F.E.B., Carr M.D., Feeney J.
      Eur. J. Biochem. 233:847-855(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    19. "High-resolution solution structure of human pNR-2/pS2: a single trefoil motif protein."
      Polshakov V.I., Williams M.A., Gargaro A.R., Frenkiel T.A., Westley B.R., Chadwick M.P., May F.E.B., Feeney J.
      J. Mol. Biol. 267:418-432(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    20. Cited for: VARIANTS ILE-32; LYS-32; ASP-34; LYS-37; ILE-46 AND VAL-55.
    21. "Trefoil factor family-1 mutations enhance gastric cancer cell invasion through distinct signaling pathways."
      Yio X., Diamond M., Zhang J.-Y., Weinstein H., Wang L.-H., Werther L., Itzkowitz S.
      Gastroenterology 130:1696-1706(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ASP-34 AND LYS-37, MUTAGENESIS OF CYS-82.

    Entry informationi

    Entry nameiTFF1_HUMAN
    AccessioniPrimary (citable) accession number: P04155
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1986
    Last sequence update: November 1, 1986
    Last modified: October 1, 2014
    This is version 153 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3