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P25719

- CYPC_YEAST

UniProt

P25719 - CYPC_YEAST

Protein

Peptidyl-prolyl cis-trans isomerase C, mitochondrial

Gene

CPR3

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 135 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      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. This isozyme is required for growth on lactate at high temperature.3 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by the immunosuppressant drug cyclosporin A and by SDZ NIM811, a PPIase inhibitor.

    GO - Molecular functioni

    1. peptide binding Source: UniProtKB-KW
    2. peptidyl-prolyl cis-trans isomerase activity Source: SGD

    GO - Biological processi

    1. apoptotic process Source: SGD
    2. protein folding Source: SGD
    3. protein peptidyl-prolyl isomerization Source: GOC

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Ligandi

    Cyclosporin

    Enzyme and pathway databases

    BioCyciYEAST:YML078W-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase C, mitochondrial (EC:5.2.1.8)
    Short name:
    PPIase C
    Alternative name(s):
    Cyclophilin C
    PPI-III
    Rotamase C
    Gene namesi
    Name:CPR3
    Synonyms:CYP3
    Ordered Locus Names:YML078W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYML078w.
    SGDiS000004543. CPR3.

    Subcellular locationi

    Mitochondrion matrix 3 Publications

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: SGD

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi73 – 731R → A: Strongly reduces in vitro PPIase activity and in vivo protein folding activity. Reduces binding to cyclosporin A 2-fold. 1 Publication
    Mutagenesisi144 – 1441H → Q: Strongly reduces in vitro PPIase activity and in vivo protein folding activity. Reduces binding to cyclosporin A 2-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2020Mitochondrion1 PublicationAdd
    BLAST
    Chaini21 – 182162Peptidyl-prolyl cis-trans isomerase C, mitochondrialPRO_0000025487Add
    BLAST

    Proteomic databases

    MaxQBiP25719.
    PaxDbiP25719.
    PeptideAtlasiP25719.
    PRIDEiP25719.

    Expressioni

    Gene expression databases

    GenevestigatoriP25719.

    Interactioni

    Protein-protein interaction databases

    BioGridi35063. 17 interactions.
    DIPiDIP-6534N.
    IntActiP25719. 1 interaction.
    MINTiMINT-2784972.
    STRINGi4932.YML078W.

    Structurei

    3D structure databases

    ProteinModelPortaliP25719.
    SMRiP25719. Positions 23-182.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 181157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the cyclophilin-type PPIase family.Curated
    Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0652.
    GeneTreeiENSGT00750000117619.
    HOGENOMiHOG000065981.
    KOiK01802.
    OMAiMANAGEN.
    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.

    P25719-1 [UniParc]FASTAAdd to Basket

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    MFKRSIIQQS RLFSNSASRL GKKVFFDPAV NGTKIGRIEF ELYDNVVPKT    50
    AENFRALCTG EKGWGYKGVP FHRIIPDFMI QGGDTDLTNG FGGKSIYGSK 100
    FADENFVKKH DKAGLLSMAN AGPNTNGSQF FITTVPCPWL DGKHVVFGEV 150
    TKGMDIVKAI ESYGTASGKP RAEIVIEEAG EL 182
    Length:182
    Mass (Da):19,919
    Last modified:May 1, 1992 - v1
    Checksum:i96C9A5B75250EF55
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84758 Genomic DNA. Translation: AAA34548.1.
    X56962 Genomic DNA. Translation: CAA40282.1.
    Z46373 Genomic DNA. Translation: CAA86500.1.
    AY557761 Genomic DNA. Translation: AAS56087.1.
    BK006946 Genomic DNA. Translation: DAA09819.1.
    PIRiS30507.
    RefSeqiNP_013633.1. NM_001182437.1.

    Genome annotation databases

    EnsemblFungiiYML078W; YML078W; YML078W.
    GeneIDi854897.
    KEGGisce:YML078W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84758 Genomic DNA. Translation: AAA34548.1 .
    X56962 Genomic DNA. Translation: CAA40282.1 .
    Z46373 Genomic DNA. Translation: CAA86500.1 .
    AY557761 Genomic DNA. Translation: AAS56087.1 .
    BK006946 Genomic DNA. Translation: DAA09819.1 .
    PIRi S30507.
    RefSeqi NP_013633.1. NM_001182437.1.

    3D structure databases

    ProteinModelPortali P25719.
    SMRi P25719. Positions 23-182.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35063. 17 interactions.
    DIPi DIP-6534N.
    IntActi P25719. 1 interaction.
    MINTi MINT-2784972.
    STRINGi 4932.YML078W.

    Proteomic databases

    MaxQBi P25719.
    PaxDbi P25719.
    PeptideAtlasi P25719.
    PRIDEi P25719.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YML078W ; YML078W ; YML078W .
    GeneIDi 854897.
    KEGGi sce:YML078W.

    Organism-specific databases

    CYGDi YML078w.
    SGDi S000004543. CPR3.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci YEAST:YML078W-MONOMER.

    Miscellaneous databases

    NextBioi 977867.

    Gene expression databases

    Genevestigatori P25719.

    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. "The yeast cyclophilin multigene family: purification, cloning and characterization of a new isoform."
      McLaughlin M.M., Bossard M.J., Koser P.L., Cafferkey R., Morris R.A., Miles L.M., Strickler J., Bergsma D.J., Levy M.A., Livi G.P.
      Gene 111:85-92(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-35.
    2. "A yeast cyclophilin gene essential for lactate metabolism at high temperature."
      Davis E.S., Becker A., Heitman J., Hall M.N., Brennan M.B.
      Proc. Natl. Acad. Sci. U.S.A. 89:11169-11173(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. 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 21-63, FUNCTION, CATALYTIC ACTIVITY.
    7. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "R73A and H144Q mutants of the yeast mitochondrial cyclophilin Cpr3 exhibit a low prolyl isomerase activity in both peptide and protein-folding assays."
      Scholz C., Maier P., Dolinski K., Heitman J., Schmid F.X.
      FEBS Lett. 443:367-369(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ARG-73 AND HIS-144.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    13. "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 nameiCYPC_YEAST
    AccessioniPrimary (citable) accession number: P25719
    Secondary accession number(s): D6W0K5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 135 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1960 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3