UniProtKB - P25719 (CYPC_YEAST)
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Protein
Peptidyl-prolyl cis-trans isomerase C, mitochondrial
Gene
CPR3
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
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.3 Publications
Miscellaneous
Present with 1960 molecules/cell in log phase SD medium.1 Publication
Catalytic activityi
Peptidylproline (omega=180) = peptidylproline (omega=0).1 Publication
Enzyme regulationi
Inhibited by the immunosuppressant drug cyclosporin A and by SDZ NIM811, a PPIase inhibitor.
GO - Molecular functioni
- peptidyl-prolyl cis-trans isomerase activity Source: SGD
GO - Biological processi
- apoptotic process Source: SGD
- protein folding Source: SGD
Keywordsi
Molecular function | Isomerase, Rotamase |
Enzyme and pathway databases
BioCyci | YEAST:YML078W-MONOMER |
Reactomei | R-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 C, mitochondrial (EC:5.2.1.8)Short name: PPIase C Alternative name(s): Cyclophilin C PPI-III Rotamase C |
Gene namesi | Name:CPR3 Synonyms:CYP3 Ordered Locus Names:YML078W |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
EuPathDBi | FungiDB:YML078W |
SGDi | S000004543 CPR3 |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 73 | R → A: Strongly reduces in vitro PPIase activity and in vivo protein folding activity. Reduces binding to cyclosporin A 2-fold. 1 Publication | 1 | |
Mutagenesisi | 144 | H → Q: Strongly reduces in vitro PPIase activity and in vivo protein folding activity. Reduces binding to cyclosporin A 2-fold. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 20 | Mitochondrion1 PublicationAdd BLAST | 20 | |
ChainiPRO_0000025487 | 21 – 182 | Peptidyl-prolyl cis-trans isomerase C, mitochondrialAdd BLAST | 162 |
Proteomic databases
MaxQBi | P25719 |
PaxDbi | P25719 |
PRIDEi | P25719 |
PTM databases
iPTMneti | P25719 |
Interactioni
Protein-protein interaction databases
BioGridi | 3506369 interactors. |
DIPi | DIP-6534N |
IntActi | P25719 8 interactors. |
MINTi | P25719 |
STRINGi | 4932.YML078W |
Structurei
3D structure databases
ProteinModelPortali | P25719 |
SMRi | P25719 |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 25 – 181 | PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST | 157 |
Sequence similaritiesi
Belongs to the cyclophilin-type PPIase family.Curated
Keywords - Domaini
Transit peptidePhylogenomic databases
GeneTreei | ENSGT00760000119119 |
HOGENOMi | HOG000065981 |
InParanoidi | P25719 |
KOi | K01802 |
OMAi | ELKHTGS |
OrthoDBi | EOG092C5DG5 |
Family and domain databases
Gene3Di | 2.40.100.101 hit |
InterProi | View protein in InterPro IPR029000 Cyclophilin-like_dom_sf IPR024936 Cyclophilin-type_PPIase IPR020892 Cyclophilin-type_PPIase_CS IPR002130 Cyclophilin-type_PPIase_dom |
PANTHERi | PTHR11071 PTHR11071, 1 hit |
Pfami | View protein in Pfam PF00160 Pro_isomerase, 1 hit |
PIRSFi | PIRSF001467 Peptidylpro_ismrse, 1 hit |
PRINTSi | PR00153 CSAPPISMRASE |
SUPFAMi | SSF50891 SSF50891, 1 hit |
PROSITEi | View protein in PROSITE PS00170 CSA_PPIASE_1, 1 hit PS50072 CSA_PPIASE_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P25719-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MFKRSIIQQS RLFSNSASRL GKKVFFDPAV NGTKIGRIEF ELYDNVVPKT
60 70 80 90 100
AENFRALCTG EKGWGYKGVP FHRIIPDFMI QGGDTDLTNG FGGKSIYGSK
110 120 130 140 150
FADENFVKKH DKAGLLSMAN AGPNTNGSQF FITTVPCPWL DGKHVVFGEV
160 170 180
TKGMDIVKAI ESYGTASGKP RAEIVIEEAG EL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | 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 |
PIRi | S30507 |
RefSeqi | NP_013633.1, NM_001182437.1 |
Genome annotation databases
EnsemblFungii | YML078W; YML078W; YML078W |
GeneIDi | 854897 |
KEGGi | sce:YML078W |
Similar proteinsi
Entry informationi
Entry namei | CYPC_YEAST | |
Accessioni | P25719Primary (citable) accession number: P25719 Secondary accession number(s): D6W0K5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 1, 1992 |
Last sequence update: | May 1, 1992 | |
Last modified: | March 28, 2018 | |
This is version 165 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |