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P14306

- CPYI_YEAST

UniProt

P14306 - CPYI_YEAST

Protein

Carboxypeptidase Y inhibitor

Gene

TFS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Specific and potent inhibitor of carboxypeptidase Y.1 Publication

    GO - Molecular functioni

    1. lipid binding Source: SGD
    2. peptidase inhibitor activity Source: SGD
    3. phospholipid binding Source: SGD
    4. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    GO - Biological processi

    1. regulation of proteolysis Source: SGD
    2. regulation of Ras protein signal transduction Source: SGD

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32303-MONOMER.

    Protein family/group databases

    MEROPSiI51.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxypeptidase Y inhibitor
    Short name:
    CPY inhibitor
    Alternative name(s):
    CDC25 suppressor 1
    I(C)
    Ic
    Protein DKA1
    Protein NSP1
    Gene namesi
    Name:TFS1
    Synonyms:DKA1, NSP1
    Ordered Locus Names:YLR178C
    ORF Names:L9470.19
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR178c.
    SGDiS000004168. TFS1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. fungal-type vacuole lumen Source: SGD
    3. fungal-type vacuole membrane Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 219219Carboxypeptidase Y inhibitorPRO_0000204753Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP14306.
    PaxDbiP14306.
    PeptideAtlasiP14306.

    Expressioni

    Gene expression databases

    GenevestigatoriP14306.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi31449. 28 interactions.
    DIPiDIP-669N.
    IntActiP14306. 3 interactions.
    MINTiMINT-2786931.
    STRINGi4932.YLR178C.

    Structurei

    Secondary structure

    1
    219
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 43
    Helixi7 – 1711
    Helixi20 – 234
    Beta strandi33 – 419
    Beta strandi44 – 463
    Helixi54 – 574
    Beta strandi62 – 687
    Beta strandi89 – 9911
    Beta strandi108 – 11912
    Beta strandi133 – 1397
    Beta strandi144 – 1474
    Beta strandi161 – 1699
    Helixi176 – 1783
    Helixi187 – 1893
    Beta strandi192 – 1943
    Helixi197 – 2026
    Turni203 – 2053
    Beta strandi207 – 21610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WPXX-ray2.70B1-219[»]
    ProteinModelPortaliP14306.
    SMRiP14306. Positions 1-219.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14306.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1881.
    GeneTreeiENSGT00740000116453.
    HOGENOMiHOG000237655.
    KOiK06910.
    OMAiAPSNTDH.
    OrthoDBiEOG70612X.

    Family and domain databases

    Gene3Di3.90.280.10. 1 hit.
    InterProiIPR001858. Phosphotidylethanolamine-bd_CS.
    IPR008914. PtdEtn-bd_prot_PEBP.
    [Graphical view]
    PfamiPF01161. PBP. 1 hit.
    [Graphical view]
    SUPFAMiSSF49777. SSF49777. 1 hit.
    PROSITEiPS01220. PBP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14306-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNQAIDFAQA SIDSYKKHGI LEDVIHDTSF QPSGILAVEY SSSAPVAMGN    50
    TLPTEKARSK PQFQFTFNKQ MQKSVPQANA YVPQDDDLFT LVMTDPDAPS 100
    KTDHKWSEFC HLVECDLKLL NEATHETSGA TEFFASEFNT KGSNTLIEYM 150
    GPAPPKGSGP HRYVFLLYKQ PKGVDSSKFS KIKDRPNWGY GTPATGVGKW 200
    AKENNLQLVA SNFFYAETK 219
    Length:219
    Mass (Da):24,357
    Last modified:July 1, 1993 - v2
    Checksum:i37D4FEC17677A573
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 561K → N in CAA44015. (PubMed:1745232)Curated
    Sequence conflicti165 – 1651F → L in CAA33456. (PubMed:2693892)Curated
    Sequence conflicti211 – 2199SNFFYAETK → VQFLLCGNEIGIYIYICICI YFLDFSAFHLTFYYFCFIYV FVTNGQMFVGTNVYVKQNT(PubMed:2693892)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15409 Genomic DNA. Translation: CAA33456.1.
    X62105 Genomic DNA. Translation: CAA44015.1.
    U17246 Genomic DNA. Translation: AAB67471.1.
    BK006945 Genomic DNA. Translation: DAA09498.1.
    PIRiS18843.
    RefSeqiNP_013279.1. NM_001182065.1.

    Genome annotation databases

    EnsemblFungiiYLR178C; YLR178C; YLR178C.
    GeneIDi850875.
    KEGGisce:YLR178C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15409 Genomic DNA. Translation: CAA33456.1 .
    X62105 Genomic DNA. Translation: CAA44015.1 .
    U17246 Genomic DNA. Translation: AAB67471.1 .
    BK006945 Genomic DNA. Translation: DAA09498.1 .
    PIRi S18843.
    RefSeqi NP_013279.1. NM_001182065.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WPX X-ray 2.70 B 1-219 [» ]
    ProteinModelPortali P14306.
    SMRi P14306. Positions 1-219.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31449. 28 interactions.
    DIPi DIP-669N.
    IntActi P14306. 3 interactions.
    MINTi MINT-2786931.
    STRINGi 4932.YLR178C.

    Protein family/group databases

    MEROPSi I51.001.

    Proteomic databases

    MaxQBi P14306.
    PaxDbi P14306.
    PeptideAtlasi P14306.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR178C ; YLR178C ; YLR178C .
    GeneIDi 850875.
    KEGGi sce:YLR178C.

    Organism-specific databases

    CYGDi YLR178c.
    SGDi S000004168. TFS1.

    Phylogenomic databases

    eggNOGi COG1881.
    GeneTreei ENSGT00740000116453.
    HOGENOMi HOG000237655.
    KOi K06910.
    OMAi APSNTDH.
    OrthoDBi EOG70612X.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32303-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P14306.
    NextBioi 967218.

    Gene expression databases

    Genevestigatori P14306.

    Family and domain databases

    Gene3Di 3.90.280.10. 1 hit.
    InterProi IPR001858. Phosphotidylethanolamine-bd_CS.
    IPR008914. PtdEtn-bd_prot_PEBP.
    [Graphical view ]
    Pfami PF01161. PBP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49777. SSF49777. 1 hit.
    PROSITEi PS01220. PBP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of NSP1, a locus encoding a component of a CDC25-dependent, nutrient-responsive pathway in Saccharomyces cerevisiae."
      Tripp M.L., Bouchard R.A., Pinon R.
      Mol. Microbiol. 3:1319-1327(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: X241.
    2. "TFS1: a suppressor of cdc25 mutations in Saccharomyces cerevisiae."
      Robinson L.C., Tatchell K.
      Mol. Gen. Genet. 230:241-250(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "A high-affinity inhibitor of yeast carboxypeptidase Y is encoded by TFS1 and shows homology to a family of lipid binding proteins."
      Bruun A.W., Svendsen I., Sorensen S.O., Kielland-Brandt M.C., Winther J.R.
      Biochemistry 37:3351-3357(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Overexpression and functional characterization of a serine carboxypeptidase inhibitor (I(C)) from Saccharomyces cerevisiae."
      Mima J., Suzuki H., Takahashi M., Hayashi R.
      J. Biochem. 132:967-973(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, ACETYLATION AT MET-1.
    7. "N-terminal acetyl group is essential for the inhibitory function of carboxypeptidase Y inhibitor (I(C))."
      Mima J., Kondo T., Hayashi R.
      FEBS Lett. 532:207-210(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCPYI_YEAST
    AccessioniPrimary (citable) accession number: P14306
    Secondary accession number(s): D6VYI2, P30312
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1030 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3