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Protein

Peptidyl-prolyl cis-trans isomerase

Gene

CPR1

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. Involved in histone deacetylase complexes, suggesting a function in chromatin. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles. Regulates the meiotic gene program via the Set3C histone deacetylase complex to promote efficient sporulation, and the prolyl-isomerase activity is required for this function.3 Publications

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).1 Publication

Enzyme regulationi

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.

GO - Molecular functioni

  • cyclosporin A binding Source: SGD
  • peptidyl-prolyl cis-trans isomerase activity Source: SGD

GO - Biological processi

  • ascospore formation Source: SGD
  • cellular protein metabolic process Source: SGD
  • histone deacetylation Source: SGD
  • positive regulation of meiotic nuclear division Source: SGD
  • protein folding Source: InterPro
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Cyclosporin

Enzyme and pathway databases

BioCyciYEAST:YDR155C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase (EC:5.2.1.8)
Short name:
PPIase
Alternative name(s):
Cyclophilin
Short name:
CPH
Cyclosporin A-binding protein
PPI-II
Rotamase
Gene namesi
Name:CPR1
Synonyms:CPH1, CYP1, SCC1
Ordered Locus Names:YDR155C
ORF Names:YD8358.10C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR155C.
SGDiS000002562. CPR1.

Subcellular locationi

GO - Cellular componenti

  • histone deacetylase complex Source: SGD
  • mitochondrial intermembrane space Source: SGD
  • nucleus Source: SGD
  • Set3 complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 162161Peptidyl-prolyl cis-trans isomerasePRO_0000064132Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei71 – 711Phosphothreonine1 Publication
Modified residuei142 – 1421Phosphoserine1 Publication
Modified residuei145 – 1451Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP14832.
PaxDbiP14832.
PeptideAtlasiP14832.
PRIDEiP14832.

Interactioni

Subunit structurei

Interacts with a complex composed of SIN3 and RPD3. Identified in the Set3C complex with HOS2, HST1, SNT1, SIF2, HOS4/YIL112W and SET3.3 Publications

Protein-protein interaction databases

BioGridi32207. 84 interactions.
DIPiDIP-5203N.
IntActiP14832. 63 interactions.
MINTiMINT-494205.

Structurei

Secondary structure

1
162
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Beta strandi13 – 2210Combined sources
Turni24 – 263Combined sources
Helixi28 – 3912Combined sources
Turni40 – 423Combined sources
Beta strandi53 – 553Combined sources
Turni56 – 583Combined sources
Beta strandi59 – 624Combined sources
Turni65 – 673Combined sources
Beta strandi68 – 714Combined sources
Beta strandi92 – 987Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi110 – 1156Combined sources
Helixi118 – 1203Combined sources
Turni121 – 1233Combined sources
Beta strandi126 – 1327Combined sources
Helixi134 – 1418Combined sources
Beta strandi154 – 1618Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ISTX-ray1.90A/B1-162[»]
1VDNX-ray1.60A1-162[»]
ProteinModelPortaliP14832.
SMRiP14832. Positions 2-162.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14832.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 161157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
InParanoidiP14832.
KOiK01802.
OMAiTIVIEEM.
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.

P14832-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQVYFDVEA DGQPIGRVVF KLYNDIVPKT AENFRALCTG EKGFGYAGSP
60 70 80 90 100
FHRVIPDFML QGGDFTAGNG TGGKSIYGGK FPDENFKKHH DRPGLLSMAN
110 120 130 140 150
AGPNTNGSQF FITTVPCPWL DGKHVVFGEV VDGYDIVKKV ESLGSPSGAT
160
KARIVVAKSG EL
Length:162
Mass (Da):17,391
Last modified:January 23, 2007 - v3
Checksum:i012D8E8E4D85B4B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17505 mRNA. Translation: CAA35545.1.
M30513 Genomic DNA. Translation: AAA34528.1.
Z50046 Genomic DNA. Translation: CAA90376.1.
AY557665 Genomic DNA. Translation: AAS55991.1.
BK006938 Genomic DNA. Translation: DAA11996.1.
PIRiS25443. CSBY.
RefSeqiNP_010439.1. NM_001180462.1.

Genome annotation databases

EnsemblFungiiYDR155C; YDR155C; YDR155C.
GeneIDi851733.
KEGGisce:YDR155C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17505 mRNA. Translation: CAA35545.1.
M30513 Genomic DNA. Translation: AAA34528.1.
Z50046 Genomic DNA. Translation: CAA90376.1.
AY557665 Genomic DNA. Translation: AAS55991.1.
BK006938 Genomic DNA. Translation: DAA11996.1.
PIRiS25443. CSBY.
RefSeqiNP_010439.1. NM_001180462.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ISTX-ray1.90A/B1-162[»]
1VDNX-ray1.60A1-162[»]
ProteinModelPortaliP14832.
SMRiP14832. Positions 2-162.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32207. 84 interactions.
DIPiDIP-5203N.
IntActiP14832. 63 interactions.
MINTiMINT-494205.

Proteomic databases

MaxQBiP14832.
PaxDbiP14832.
PeptideAtlasiP14832.
PRIDEiP14832.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR155C; YDR155C; YDR155C.
GeneIDi851733.
KEGGisce:YDR155C.

Organism-specific databases

EuPathDBiFungiDB:YDR155C.
SGDiS000002562. CPR1.

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
InParanoidiP14832.
KOiK01802.
OMAiTIVIEEM.
OrthoDBiEOG757D7G.

Enzyme and pathway databases

BioCyciYEAST:YDR155C-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP14832.
NextBioi969457.
PROiP14832.

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. "Nucleotide sequence of a full-length cDNA coding for cyclophilin (peptidyl-prolyl cis-trans isomerase) of Saccharomyces cerevisiae."
    Dietmeier K., Tropschug M.
    Nucleic Acids Res. 18:373-373(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Yeast cyclophilin: isolation and characterization of the protein, cDNA and gene."
    Haendler B., Keller R., Hiestand P.C., Kocher H.P., Wegmann G., Movva N.R.
    Gene 83:39-46(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-112 AND 120-151, ACETYLATION AT SER-2, CLEAVAGE OF INITIATOR METHIONINE.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    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 2-10; 30-37; 75-78; 81-85 AND 159-162, FUNCTION, CATALYTIC ACTIVITY.
  7. "The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program."
    Pijnappel W.W.M.P., Schaft D., Roguev A., Shevchenko A., Tekotte H., Wilm M., Rigaut G., Seraphin B., Aasland R., Stewart A.F.
    Genes Dev. 15:2991-3004(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH HOS2; HST1; SNT1; SIF2; YIL112W AND SET3.
  8. "Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase."
    Arevalo-Rodriguez M., Cardenas M.E., Wu X., Hanes S.D., Heitman J.
    EMBO J. 19:3739-3749(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPD3.
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "Cyclophilin A mediates Vid22p function in the import of fructose-1,6-bisphosphatase into Vid vesicles."
    Brown C.R., Cui D.-Y., Hung G.G.-C., Chiang H.-L.
    J. Biol. Chem. 276:48017-48026(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Cyclophilin A is localized to the nucleus and controls meiosis in Saccharomyces cerevisiae."
    Arevalo-Rodriguez M., Heitman J.
    Eukaryot. Cell 4:17-29(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SET3C COMPLEX, INTERACTION WITH SNT1 AND SIF2.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  13. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71; SER-142 AND SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  18. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Turns are essential in the folding of the globular beta-barrel structure of yeast cyclophilin A, CPR1."
    Kashima A., Yoshikawa-Fujioka S., Hayano T., Takahashi N., Konno M.
    Submitted (DEC-2001) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
  20. "Crystal structure of yeast cyclophilin A complexed with ACE-Ala-Ala-Pro-Ala-7-amino-4-methylcoumarin."
    Konno M., Shibano T., Okudaira K., Takahashi N.
    Submitted (MAR-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).

Entry informationi

Entry nameiCYPH_YEAST
AccessioniPrimary (citable) accession number: P14832
Secondary accession number(s): D6VSD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 86000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.