CPR3

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
Inferred from direct assayⁱ
- 7603990

Complete GO annotation...

GO - Biological processⁱ

apoptotic process
Source: SGD
Inferred from mutant phenotypeⁱ
- 17881727
protein folding
Source: SGD
Inferred from direct assayⁱ
- 7603990

Complete GO annotation...

Keywordsⁱ

Molecular function	Isomerase, Rotamase

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	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae
Proteomesⁱ	UP000002311 Componentⁱ: Chromosome XIII

Organism-specific databases

EuPathDBⁱ	FungiDB:YML078W.
Saccharomyces Genome Database More...SGDⁱ	S000004543. CPR3.

Subcellular locationⁱ

Mitochondrion matrix
3 Publications
Manual assertion based on experiment inⁱ
- Ref.7
  "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] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION.
- Ref.9
  "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] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
- Ref.11
  "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] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

GO - Cellular componentⁱ

mitochondrial matrix Source: UniProtKB-SubCell
mitochondrion
Source: SGD
Inferred from direct assayⁱ
- 7603990

Complete GO annotation...

Keywords - Cellular componentⁱ

Mitochondrion

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

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P25719.
PRIDEⁱ	P25719.

PTM databases

iPTMnetⁱ	P25719.

iPTMnetⁱ

P25719.

Interactionⁱ

Protein-protein interaction databases

BioGridⁱ	35063. 22 interactors.
Database of interacting proteins More...DIPⁱ	DIP-6534N.
IntActⁱ	P25719. 1 interactor.
Molecular INTeraction database More...MINTⁱ	MINT-2784972.

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 peptide

Phylogenomic databases

Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000119119.
HOGENOMⁱ	HOG000065981.
InParanoidⁱ	P25719.
KEGG Orthology (KO) More...KOⁱ	K01802.
OMAⁱ	FFINFKD.
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C5DG5.

Family and domain databases

Gene3Dⁱ	2.40.100.10. 1 hit.
InterProⁱ	View protein in InterPro IPR029000. Cyclophilin-like_dom. IPR024936. Cyclophilin-type_PPIase. IPR020892. Cyclophilin-type_PPIase_CS. IPR002130. Cyclophilin-type_PPIase_dom.
PANTHERⁱ	PTHR11071. PTHR11071. 1 hit.
Pfam protein domain database More...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.

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P25719-1 [UniParc]FASTA Add to basket

« Hide

        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

Length:182

Mass (Da):19,919

Last modified:May 1, 1992 - v1

Checksum:ⁱ96C9A5B75250EF55

GO

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.
NCBI Reference Sequences More...RefSeqⁱ	NP_013633.1. NM_001182437.1.

Genome annotation databases

EnsemblFungiⁱ	YML078W; YML078W; YML078W.
GeneIDⁱ	854897.
KEGGⁱ	sce:YML078W.

Cross-referencesⁱ

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.
NCBI Reference Sequences More...RefSeqⁱ	NP_013633.1. NM_001182437.1.

3D structure databases

ProteinModelPortalⁱ	P25719.
SMRⁱ	P25719.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	35063. 22 interactors.
Database of interacting proteins More...DIPⁱ	DIP-6534N.
IntActⁱ	P25719. 1 interactor.
Molecular INTeraction database More...MINTⁱ	MINT-2784972.

PTM databases

iPTMnetⁱ	P25719.

iPTMnetⁱ

P25719.

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P25719.
PRIDEⁱ	P25719.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblFungiⁱ	YML078W; YML078W; YML078W.
GeneIDⁱ	854897.
KEGGⁱ	sce:YML078W.

Organism-specific databases

EuPathDBⁱ	FungiDB:YML078W.
Saccharomyces Genome Database More...SGDⁱ	S000004543. CPR3.

Phylogenomic databases

Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000119119.
HOGENOMⁱ	HOG000065981.
InParanoidⁱ	P25719.
KEGG Orthology (KO) More...KOⁱ	K01802.
OMAⁱ	FFINFKD.
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C5DG5.

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.

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P25719.

PROⁱ

PR:P25719.

Family and domain databases

Gene3Dⁱ	2.40.100.10. 1 hit.
InterProⁱ	View protein in InterPro IPR029000. Cyclophilin-like_dom. IPR024936. Cyclophilin-type_PPIase. IPR020892. Cyclophilin-type_PPIase_CS. IPR002130. Cyclophilin-type_PPIase_dom.
PANTHERⁱ	PTHR11071. PTHR11071. 1 hit.
Pfam protein domain database More...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.
ProtoNetⁱ	Search...

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:	June 7, 2017
	This is version 158 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
Yeast chromosome XIII
Yeast (Saccharomyces cerevisiae) chromosome XIII: 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.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P25719 (CYPC_YEAST)

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Peptidyl-prolyl cis-trans isomerase C, mitochondrial

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

Enzyme regulationⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ