Reviewed, UniProtKB/Swiss-Prot P25719 (CYPC_YEAST)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase C, mitochondrial
      Short name(s)=PPIase, Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin C
    PPI-III

Gene names

Name:	CPR3
Synonyms:	CYP3
Ordered Locus Names:	YML078W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Inhibited by the immunosuppressant drug cyclosporin A and by SDZ NIM811, a PPIase inhibitor.
Subcellular location	Mitochondrion matrix.
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
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	apoptosis Inferred from mutant phenotype. Source: SGD protein folding Ref.6 Inferred from direct assay. Source: SGD
Cellular component	mitochondrion Ref.6 Ref.10 Inferred from direct assay. Source: SGD
Molecular function	peptidyl-prolyl cis-trans isomerase activity Ref.6 Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Transit peptide	1 – 20	20	Mitochondrion
	Chain	21 – 182	162	Peptidyl-prolyl cis-trans isomerase C, mitochondrial
Regions
	Domain	25 – 181	157	PPIase cyclophilin-type
Amino acid modifications
	Modified residue	99	1	Phosphoserine
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
	Mutagenesis	144	1	H → Q: Strongly reduces in vitro PPIase activity and in vivo protein folding activity. Reduces binding to cyclosporin A 2-fold

Sequences

	Sequence		Length	Mass (Da)
	P25719-1 [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: 1547957] [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: 1454795] [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: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"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: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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: 8431466] [Abstract] Cited for: CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE.
[6]	"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: 7603990] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"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: 10025965] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ARG-73 AND HIS-144.
[8]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"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: 14576278] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"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 0:0-0(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M84758 Genomic DNA. Translation: AAA34548.1. X56962 Genomic DNA. Translation: CAA40282.1. Z46373 Genomic DNA. Translation: CAA86500.1. AY557761 Genomic DNA. Translation: AAS56087.1.
PIR	S30507.
RefSeq	NP_013633.1.
3D structure databases
HSSP	HSSP built from PDB template 1E3B based on UniProtKB P52011.
SMR	P25719. Positions 23-182.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6534N.
IntAct	P25719.
Proteomic databases
PeptideAtlas	P25719.
Genome annotation databases
Ensembl	YML078W. Saccharomyces cerevisiae. [Contig view]
GeneID	854897.
GenomeReviews	Gene locus YML078W in contig Z71257_GR.
KEGG	sce:YML078W.
NMPDR	fig|4932.3.peg.4670.
Organism-specific databases
CYGD	YML078w.
SGD	S000004543. CPR3.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P25719.
Gene expression databases
GermOnline	YML078W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002130. PPIase_cyclophilin. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
PANTHER	PTHR11071. PPIase_cyclophilin. 1 hit.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProDom	P25719. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
LinkHub	P25719.
ProtoNet	Search...

Entry information

Entry name

CYPC_YEAST

Accession

Primary (citable) accession number: P25719

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	July 22, 2008
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)