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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.
ReactomeiR-SCE-6781823. Formation of TC-NER Pre-Incision Complex.
R-SCE-6782135. Dual incision in TC-NER.
R-SCE-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SCE-6798695. Neutrophil degranulation.

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
Proteomesi
  • UP000002311 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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000641322 – 162Peptidyl-prolyl cis-trans isomeraseAdd BLAST161

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources2 Publications1
Cross-linki29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei71PhosphothreonineCombined sources1
Cross-linki123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei142PhosphoserineCombined sources1
Modified residuei145PhosphoserineCombined sources1
Cross-linki151Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki158Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP14832.
PRIDEiP14832.
TopDownProteomicsiP14832.

PTM databases

iPTMnetiP14832.

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. 87 interactors.
DIPiDIP-5203N.
IntActiP14832. 63 interactors.
MINTiMINT-494205.

Structurei

Secondary structure

1162
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 10Combined sources8
Beta strandi13 – 22Combined sources10
Turni24 – 26Combined sources3
Helixi28 – 39Combined sources12
Turni40 – 42Combined sources3
Beta strandi53 – 55Combined sources3
Turni56 – 58Combined sources3
Beta strandi59 – 62Combined sources4
Turni65 – 67Combined sources3
Beta strandi68 – 71Combined sources4
Beta strandi92 – 98Combined sources7
Beta strandi100 – 102Combined sources3
Beta strandi110 – 115Combined sources6
Helixi118 – 120Combined sources3
Turni121 – 123Combined sources3
Beta strandi126 – 132Combined sources7
Helixi134 – 141Combined sources8
Beta strandi154 – 161Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP14832.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 161PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST157

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
InParanoidiP14832.
KOiK01802.
OMAiIIMNTSE.
OrthoDBiEOG092C5DG5.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ISTX-ray1.90A/B1-162[»]
1VDNX-ray1.60A1-162[»]
ProteinModelPortaliP14832.
SMRiP14832.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32207. 87 interactors.
DIPiDIP-5203N.
IntActiP14832. 63 interactors.
MINTiMINT-494205.

PTM databases

iPTMnetiP14832.

Proteomic databases

MaxQBiP14832.
PRIDEiP14832.
TopDownProteomicsiP14832.

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

GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
InParanoidiP14832.
KOiK01802.
OMAiIIMNTSE.
OrthoDBiEOG092C5DG5.

Enzyme and pathway databases

BioCyciYEAST:YDR155C-MONOMER.
ReactomeiR-SCE-6781823. Formation of TC-NER Pre-Incision Complex.
R-SCE-6782135. Dual incision in TC-NER.
R-SCE-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SCE-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiP14832.
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...

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: November 30, 2016
This is version 179 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

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 one 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.