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Protein

Peptidyl-prolyl cis-trans isomerase C, mitochondrial

Gene

CPR3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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

  • peptide binding Source: UniProtKB-KW
  • peptidyl-prolyl cis-trans isomerase activity Source: SGD

GO - Biological processi

  • apoptotic process Source: SGD
  • protein folding Source: SGD
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 Componenti: Chromosome XIII

Organism-specific databases

CYGDiYML078w.
EuPathDBiFungiDB:YML078W.
SGDiS000004543. CPR3.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • 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 – 2020Mitochondrion1 PublicationAdd
BLAST
Chaini21 – 182162Peptidyl-prolyl cis-trans isomerase C, mitochondrialPRO_0000025487Add
BLAST

Proteomic databases

MaxQBiP25719.
PaxDbiP25719.
PeptideAtlasiP25719.
PRIDEiP25719.

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.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
InParanoidiP25719.
KOiK01802.
OMAiDNHFLNR.
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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
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

        10         20         30         40         50
MFKRSIIQQS RLFSNSASRL GKKVFFDPAV NGTKIGRIEF ELYDNVVPKT
60 70 80 90 100
AENFRALCTG EKGWGYKGVP FHRIIPDFMI QGGDTDLTNG FGGKSIYGSK
110 120 130 140 150
FADENFVKKH DKAGLLSMAN AGPNTNGSQF FITTVPCPWL DGKHVVFGEV
160 170 180
TKGMDIVKAI ESYGTASGKP RAEIVIEEAG EL
Length:182
Mass (Da):19,919
Last modified:May 1, 1992 - v1
Checksum:i96C9A5B75250EF55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Proteomic databases

MaxQBiP25719.
PaxDbiP25719.
PeptideAtlasiP25719.
PRIDEiP25719.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYML078w.
EuPathDBiFungiDB:YML078W.
SGDiS000004543. CPR3.

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
InParanoidiP25719.
KOiK01802.
OMAiDNHFLNR.
OrthoDBiEOG757D7G.

Enzyme and pathway databases

BioCyciYEAST:YML078W-MONOMER.

Miscellaneous databases

NextBioi977867.
PROiP25719.

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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
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]
ProtoNetiSearch...

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 24, 2015
This is version 140 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.