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P25719

- CYPC_YEAST

UniProt

P25719 - CYPC_YEAST

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Protein
Peptidyl-prolyl cis-trans isomerase C, mitochondrial
Gene
CPR3, CYP3, YML078W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

GO - Biological processi

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

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
Complete GO annotation...

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 – 2020Mitochondrion2 Publications
Add
BLAST
Chaini21 – 182162Peptidyl-prolyl cis-trans isomerase C, mitochondrial
PRO_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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 181157PPIase cyclophilin-type
Add
BLAST

Sequence similaritiesi

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

« Hide

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...

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 134 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.

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

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