P25719 (CYPC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	182 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from mutant phenotype PubMed 17881727. Source: SGD protein folding Inferred from direct assay Ref.7. Source: SGD protein peptidyl-prolyl isomerization Inferred from direct assay Ref.7. Source: GOC
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay Ref.7. Source: SGD
Molecular_function	peptide binding Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay Ref.7. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 20	20	Mitochondrion Ref.1 Ref.6
	Chain	21 – 182	162	Peptidyl-prolyl cis-trans isomerase C, mitochondrial		PRO_0000025487
Regions
	Domain	25 – 181	157	PPIase cyclophilin-type
Experimental info
	Mutagenesis	73	1	R → A: Strongly reduces in vitro PPIase activity and in vivo protein folding activity. Reduces binding to cyclosporin A 2-fold. Ref.8
	Mutagenesis	144	1	H → Q: Strongly reduces in vitro PPIase activity and in vivo protein folding activity. Reduces binding to cyclosporin A 2-fold. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P25719 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 96C9A5B75250EF55	FASTA	182	19,919
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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. , 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.
PIR	S30507.
RefSeq	NP_013633.1. NM_001182437.1.
3D structure databases
ProteinModelPortal	P25719.
SMR	P25719. Positions 23-182.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	35063. 17 interactions.
DIP	DIP-6534N.
IntAct	P25719. 1 interaction.
MINT	MINT-2784972.
STRING	4932.YML078W.
Proteomic databases
PaxDb	P25719.
PeptideAtlas	P25719.
PRIDE	P25719.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YML078W; YML078W; YML078W.
GeneID	854897.
KEGG	sce:YML078W.
Organism-specific databases
CYGD	YML078w.
SGD	S000004543. CPR3.
Phylogenomic databases
eggNOG	COG0652.
GeneTree	ENSGT00750000117619.
HOGENOM	HOG000065981.
KO	K01802.
OMA	IEFELYD.
OrthoDB	EOG757D7G.
Enzyme and pathway databases
BioCyc	YEAST:YML078W-MONOMER.
Gene expression databases
Genevestigator	P25719.
Family and domain databases
InterPro	IPR024936. Cyclophilin-type_PPIase. IPR020892. Cyclophilin-type_PPIase_CS. IPR002130. Cyclophilin-type_PPIase_dom. [Graphical view]
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PIRSF	PIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTS	PR00153. CSAPPISMRASE.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977867.

Entry information

Entry name

CYPC_YEAST

Accession

Primary (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:	April 16, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program