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P14832

- CYPH_YEAST

UniProt

P14832 - CYPH_YEAST

Protein

Peptidyl-prolyl cis-trans isomerase

Gene

CPR1

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 156 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in histone deacetylase complexes, suggesting a function in chromatin. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles. Regulates the meiotic gene program via the Set3C histone deacetylase complex to promote efficient sporulation, and the prolyl-isomerase activity is required for this function.3 Publications

    Catalytic activityi

    Peptidylproline (omega=180) = peptidylproline (omega=0).1 Publication

    Enzyme regulationi

    Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.

    GO - Molecular functioni

    1. cyclosporin A binding Source: SGD
    2. peptidyl-prolyl cis-trans isomerase activity Source: SGD

    GO - Biological processi

    1. ascospore formation Source: SGD
    2. cellular protein metabolic process Source: SGD
    3. histone deacetylation Source: SGD
    4. positive regulation of meiosis Source: SGD
    5. protein folding Source: UniProtKB-KW
    6. protein peptidyl-prolyl isomerization Source: GOC
    7. protein transport Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    Cyclosporin

    Enzyme and pathway databases

    BioCyciYEAST:YDR155C-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase (EC:5.2.1.8)
    Short name:
    PPIase
    Alternative name(s):
    Cyclophilin
    Short name:
    CPH
    Cyclosporin A-binding protein
    PPI-II
    Rotamase
    Gene namesi
    Name:CPR1
    Synonyms:CPH1, CYP1, SCC1
    Ordered Locus Names:YDR155C
    ORF Names:YD8358.10C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    SGDiS000002562. CPR1.

    Subcellular locationi

    GO - Cellular componenti

    1. histone deacetylase complex Source: SGD
    2. mitochondrial intermembrane space Source: SGD
    3. nucleus Source: SGD
    4. Set3 complex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 162161Peptidyl-prolyl cis-trans isomerasePRO_0000064132Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications
    Modified residuei71 – 711Phosphothreonine1 Publication
    Modified residuei142 – 1421Phosphoserine1 Publication
    Modified residuei145 – 1451Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP14832.
    PaxDbiP14832.
    PeptideAtlasiP14832.
    PRIDEiP14832.

    Expressioni

    Gene expression databases

    GenevestigatoriP14832.

    Interactioni

    Subunit structurei

    Interacts with a complex composed of SIN3 and RPD3. Identified in the Set3C complex with HOS2, HST1, SNT1, SIF2, HOS4/YIL112W and SET3.3 Publications

    Protein-protein interaction databases

    BioGridi32207. 83 interactions.
    DIPiDIP-5203N.
    IntActiP14832. 63 interactions.
    MINTiMINT-494205.
    STRINGi4932.YDR155C.

    Structurei

    Secondary structure

    1
    162
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 108
    Beta strandi13 – 2210
    Turni24 – 263
    Helixi28 – 3912
    Turni40 – 423
    Beta strandi53 – 553
    Turni56 – 583
    Beta strandi59 – 624
    Turni65 – 673
    Beta strandi68 – 714
    Beta strandi92 – 987
    Beta strandi100 – 1023
    Beta strandi110 – 1156
    Helixi118 – 1203
    Turni121 – 1233
    Beta strandi126 – 1327
    Helixi134 – 1418
    Beta strandi154 – 1618

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ISTX-ray1.90A/B1-162[»]
    1VDNX-ray1.60A1-162[»]
    ProteinModelPortaliP14832.
    SMRiP14832. Positions 2-162.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14832.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 161157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0652.
    GeneTreeiENSGT00750000117619.
    HOGENOMiHOG000065981.
    KOiK01802.
    OMAiFRELCTH.
    OrthoDBiEOG757D7G.

    Family and domain databases

    Gene3Di2.40.100.10. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view]
    PfamiPF00160. Pro_isomerase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSiPR00153. CSAPPISMRASE.
    SUPFAMiSSF50891. SSF50891. 1 hit.
    PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P14832-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQVYFDVEA DGQPIGRVVF KLYNDIVPKT AENFRALCTG EKGFGYAGSP    50
    FHRVIPDFML QGGDFTAGNG TGGKSIYGGK FPDENFKKHH DRPGLLSMAN 100
    AGPNTNGSQF FITTVPCPWL DGKHVVFGEV VDGYDIVKKV ESLGSPSGAT 150
    KARIVVAKSG EL 162
    Length:162
    Mass (Da):17,391
    Last modified:January 23, 2007 - v3
    Checksum:i012D8E8E4D85B4B7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17505 mRNA. Translation: CAA35545.1.
    M30513 Genomic DNA. Translation: AAA34528.1.
    Z50046 Genomic DNA. Translation: CAA90376.1.
    AY557665 Genomic DNA. Translation: AAS55991.1.
    BK006938 Genomic DNA. Translation: DAA11996.1.
    PIRiS25443. CSBY.
    RefSeqiNP_010439.1. NM_001180462.1.

    Genome annotation databases

    EnsemblFungiiYDR155C; YDR155C; YDR155C.
    GeneIDi851733.
    KEGGisce:YDR155C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17505 mRNA. Translation: CAA35545.1 .
    M30513 Genomic DNA. Translation: AAA34528.1 .
    Z50046 Genomic DNA. Translation: CAA90376.1 .
    AY557665 Genomic DNA. Translation: AAS55991.1 .
    BK006938 Genomic DNA. Translation: DAA11996.1 .
    PIRi S25443. CSBY.
    RefSeqi NP_010439.1. NM_001180462.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IST X-ray 1.90 A/B 1-162 [» ]
    1VDN X-ray 1.60 A 1-162 [» ]
    ProteinModelPortali P14832.
    SMRi P14832. Positions 2-162.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32207. 83 interactions.
    DIPi DIP-5203N.
    IntActi P14832. 63 interactions.
    MINTi MINT-494205.
    STRINGi 4932.YDR155C.

    Proteomic databases

    MaxQBi P14832.
    PaxDbi P14832.
    PeptideAtlasi P14832.
    PRIDEi P14832.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR155C ; YDR155C ; YDR155C .
    GeneIDi 851733.
    KEGGi sce:YDR155C.

    Organism-specific databases

    SGDi S000002562. CPR1.

    Phylogenomic databases

    eggNOGi COG0652.
    GeneTreei ENSGT00750000117619.
    HOGENOMi HOG000065981.
    KOi K01802.
    OMAi FRELCTH.
    OrthoDBi EOG757D7G.

    Enzyme and pathway databases

    BioCyci YEAST:YDR155C-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P14832.
    NextBioi 969457.

    Gene expression databases

    Genevestigatori P14832.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSi PR00153. CSAPPISMRASE.
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of a full-length cDNA coding for cyclophilin (peptidyl-prolyl cis-trans isomerase) of Saccharomyces cerevisiae."
      Dietmeier K., Tropschug M.
      Nucleic Acids Res. 18:373-373(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Yeast cyclophilin: isolation and characterization of the protein, cDNA and gene."
      Haendler B., Keller R., Hiestand P.C., Kocher H.P., Wegmann G., Movva N.R.
      Gene 83:39-46(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-112 AND 120-151, ACETYLATION AT SER-2, CLEAVAGE OF INITIATOR METHIONINE.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "Purification and properties of multiple molecular forms of yeast peptidyl prolyl cis-trans isomerase."
      Hasumi H., Nishikawa T.
      Biochim. Biophys. Acta 1161:161-167(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE OF 2-10; 30-37; 75-78; 81-85 AND 159-162, FUNCTION, CATALYTIC ACTIVITY.
    7. "The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program."
      Pijnappel W.W.M.P., Schaft D., Roguev A., Shevchenko A., Tekotte H., Wilm M., Rigaut G., Seraphin B., Aasland R., Stewart A.F.
      Genes Dev. 15:2991-3004(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH HOS2; HST1; SNT1; SIF2; YIL112W AND SET3.
    8. "Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase."
      Arevalo-Rodriguez M., Cardenas M.E., Wu X., Hanes S.D., Heitman J.
      EMBO J. 19:3739-3749(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RPD3.
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "Cyclophilin A mediates Vid22p function in the import of fructose-1,6-bisphosphatase into Vid vesicles."
      Brown C.R., Cui D.-Y., Hung G.G.-C., Chiang H.-L.
      J. Biol. Chem. 276:48017-48026(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Cyclophilin A is localized to the nucleus and controls meiosis in Saccharomyces cerevisiae."
      Arevalo-Rodriguez M., Heitman J.
      Eukaryot. Cell 4:17-29(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SET3C COMPLEX, INTERACTION WITH SNT1 AND SIF2.
    12. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    13. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71; SER-142 AND SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Turns are essential in the folding of the globular beta-barrel structure of yeast cyclophilin A, CPR1."
      Kashima A., Yoshikawa-Fujioka S., Hayano T., Takahashi N., Konno M.
      Submitted (DEC-2001) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
    20. "Crystal structure of yeast cyclophilin A complexed with ACE-Ala-Ala-Pro-Ala-7-amino-4-methylcoumarin."
      Konno M., Shibano T., Okudaira K., Takahashi N.
      Submitted (MAR-2004) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).

    Entry informationi

    Entry nameiCYPH_YEAST
    AccessioniPrimary (citable) accession number: P14832
    Secondary accession number(s): D6VSD6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 156 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 86000 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3