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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: -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

Miscellaneous

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

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

Keywordsi

Molecular functionIsomerase, Rotamase
Biological processProtein transport, Transport

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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiP14832
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

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi32207, 154 interactors
DIPiDIP-5203N
IntActiP14832, 94 interactors
MINTiP14832
STRINGi4932.YDR155C

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

Phylogenomic databases

GeneTreeiENSGT00760000119119
HOGENOMiHOG000065981
InParanoidiP14832
KOiK01802
OMAiEPFAVSK
OrthoDBiEOG092C5DG5

Family and domain databases

Gene3Di2.40.100.10, 1 hit
InterProiView protein in InterPro
IPR029000 Cyclophilin-like_dom_sf
IPR024936 Cyclophilin-type_PPIase
IPR020892 Cyclophilin-type_PPIase_CS
IPR002130 Cyclophilin-type_PPIase_dom
PANTHERiPTHR11071 PTHR11071, 1 hit
PfamiView protein in Pfam
PF00160 Pro_isomerase, 1 hit
PIRSFiPIRSF001467 Peptidylpro_ismrse, 1 hit
PRINTSiPR00153 CSAPPISMRASE
SUPFAMiSSF50891 SSF50891, 1 hit
PROSITEiView protein in PROSITE
PS00170 CSA_PPIASE_1, 1 hit
PS50072 CSA_PPIASE_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiCYPH_YEAST
AccessioniPrimary (citable) accession number: P14832
Secondary accession number(s): D6VSD6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 192 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health