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P25719 (CYPC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase C, mitochondrial

Short name=PPIase C
EC=5.2.1.8
Alternative name(s):
Cyclophilin C
PPI-III
Rotamase C
Gene names
Name:CPR3
Synonyms:CYP3
Ordered Locus Names:YML078W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length182 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0). Ref.6

Enzyme regulation

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

Subcellular location

Mitochondrion matrix Ref.7 Ref.9 Ref.11.

Miscellaneous

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

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2020Mitochondrion Ref.1 Ref.6
Chain21 – 182162Peptidyl-prolyl cis-trans isomerase C, mitochondrial
PRO_0000025487

Regions

Domain25 – 181157PPIase cyclophilin-type

Experimental info

Mutagenesis731R → A: Strongly reduces in vitro PPIase activity and in vivo protein folding activity. Reduces binding to cyclosporin A 2-fold. Ref.8
Mutagenesis1441H → Q: Strongly reduces in vitro PPIase activity and in vivo protein folding activity. Reduces binding to cyclosporin A 2-fold. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P25719 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 96C9A5B75250EF55

FASTA18219,919
        10         20         30         40         50         60 
MFKRSIIQQS RLFSNSASRL GKKVFFDPAV NGTKIGRIEF ELYDNVVPKT AENFRALCTG 

        70         80         90        100        110        120 
EKGWGYKGVP FHRIIPDFMI QGGDTDLTNG FGGKSIYGSK FADENFVKKH DKAGLLSMAN 

       130        140        150        160        170        180 
AGPNTNGSQF FITTVPCPWL DGKHVVFGEV TKGMDIVKAI ESYGTASGKP RAEIVIEEAG 


EL 

« Hide

References

« Hide 'large scale' references
[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]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Cyclophilin catalyzes protein folding in yeast mitochondria."
Matouschek A., Rospert S., Schmid K., Glick B.S., Schatz G.
Proc. Natl. Acad. Sci. U.S.A. 92:6319-6323(1995) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[10]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS30507.
RefSeqNP_013633.1. NM_001182437.1.

3D structure databases

ProteinModelPortalP25719.
SMRP25719. Positions 23-182.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35063. 17 interactions.
DIPDIP-6534N.
IntActP25719. 1 interaction.
MINTMINT-2784972.
STRING4932.YML078W.

Proteomic databases

MaxQBP25719.
PaxDbP25719.
PeptideAtlasP25719.
PRIDEP25719.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYML078W; YML078W; YML078W.
GeneID854897.
KEGGsce:YML078W.

Organism-specific databases

CYGDYML078w.
SGDS000004543. CPR3.

Phylogenomic databases

eggNOGCOG0652.
GeneTreeENSGT00750000117619.
HOGENOMHOG000065981.
KOK01802.
OMAMANAGEN.
OrthoDBEOG757D7G.

Enzyme and pathway databases

BioCycYEAST:YML078W-MONOMER.

Gene expression databases

GenevestigatorP25719.

Family and domain databases

Gene3D2.40.100.10. 1 hit.
InterProIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. SSF50891. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977867.

Entry information

Entry nameCYPC_YEAST
AccessionPrimary (citable) accession number: P25719
Secondary accession number(s): D6W0K5
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families