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Protein

Peptidyl-prolyl cis-trans isomerase CYP7

Gene

CPR7

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. Plays a major role in negative regulation of the heat shock transcription factor (HSF).

Catalytic activityi

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

GO - Molecular functioni

  • peptidyl-prolyl cis-trans isomerase activity Source: SGD
  • unfolded protein binding Source: SGD

GO - Biological processi

  • cellular response to heat Source: SGD
  • protein refolding Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BioCyciYEAST:YJR032W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase CYP7 (EC:5.2.1.8)
Short name:
PPIase CYP7
Alternative name(s):
Rotamase CYP7
Gene namesi
Name:CPR7
Ordered Locus Names:YJR032W
ORF Names:J1585
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR032W.
SGDiS000003793. CPR7.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393Peptidyl-prolyl cis-trans isomerase CYP7PRO_0000064174Add
BLAST

Proteomic databases

MaxQBiP47103.
PeptideAtlasiP47103.

Interactioni

Subunit structurei

Interacts with RPD3 and CNS1.

Binary interactionsi

WithEntry#Exp.IntActNotes
CNS1P333132EBI-5436,EBI-4806
HSC82P151082EBI-5436,EBI-8666
HSP82P028293EBI-5436,EBI-8659
RPD3P325612EBI-5436,EBI-15864

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi33785. 153 interactions.
DIPiDIP-2312N.
IntActiP47103. 8 interactions.
MINTiMINT-1540906.

Structurei

3D structure databases

ProteinModelPortaliP47103.
SMRiP47103. Positions 4-385.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 196189PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST
Repeati240 – 27334TPR 1Add
BLAST
Repeati292 – 32534TPR 2Add
BLAST
Repeati330 – 36334TPR 3Add
BLAST

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
Contains 3 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

HOGENOMiHOG000065980.
InParanoidiP47103.
KOiK01802.
OMAiDIYEEYP.
OrthoDBiEOG7HMS9R.

Family and domain databases

Gene3Di1.10.150.160. 1 hit.
1.25.40.10. 1 hit.
2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR023114. Elongated_TPR_rpt_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
PF00515. TPR_1. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47103-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIQDPLVYLD ISIDKKPIGR IVCKLFREKA PKTTENFYKL CAGDVKSPLK
60 70 80 90 100
DQQYLSYKGN GFHRVVKNFM IQAGDIVFGT QKDSSSSSVG KGGCSIYADK
110 120 130 140 150
EEVKTDDESF CYGNFEDENL GEFVEPFTLG MANLGSPNTN NSQFFITTYA
160 170 180 190 200
APHLNGKHSI FGQVVHGKSV VRTIENCRVD SDGVPESDVR ISDCGVWEKT
210 220 230 240 250
MGVPLYNASN DQIGGDVYEE YPDDDTHFGD DDFGKALEAA NIIKESGTLL
260 270 280 290 300
FKKKDYSNAF FKYRKSLNYI NEYMPEPDVD KERNIQFINL KMKIYLNLSL
310 320 330 340 350
VLFNLERYDD AIMYATYLLE MDNVPNRDQA KAYYRRGNSY LKKKRLDEAL
360 370 380 390
QDYIFCKEKN PDDEVIEQRI EYVNRLIEEN KEKTRKNISK FFS
Length:393
Mass (Da):45,134
Last modified:November 1, 1995 - v1
Checksum:i1532F255E8016F4F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti237 – 2371L → F in AAC49415 (PubMed:8873448).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48868 Genomic DNA. Translation: AAC49415.1.
Z49532 Genomic DNA. Translation: CAA89559.1.
X87297 Genomic DNA. Translation: CAA60725.1.
AY693103 Genomic DNA. Translation: AAT93122.1.
BK006943 Genomic DNA. Translation: DAA08821.1.
PIRiS57050.
RefSeqiNP_012566.1. NM_001181690.1.

Genome annotation databases

EnsemblFungiiYJR032W; YJR032W; YJR032W.
GeneIDi853489.
KEGGisce:YJR032W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48868 Genomic DNA. Translation: AAC49415.1.
Z49532 Genomic DNA. Translation: CAA89559.1.
X87297 Genomic DNA. Translation: CAA60725.1.
AY693103 Genomic DNA. Translation: AAT93122.1.
BK006943 Genomic DNA. Translation: DAA08821.1.
PIRiS57050.
RefSeqiNP_012566.1. NM_001181690.1.

3D structure databases

ProteinModelPortaliP47103.
SMRiP47103. Positions 4-385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33785. 153 interactions.
DIPiDIP-2312N.
IntActiP47103. 8 interactions.
MINTiMINT-1540906.

Proteomic databases

MaxQBiP47103.
PeptideAtlasiP47103.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR032W; YJR032W; YJR032W.
GeneIDi853489.
KEGGisce:YJR032W.

Organism-specific databases

EuPathDBiFungiDB:YJR032W.
SGDiS000003793. CPR7.

Phylogenomic databases

HOGENOMiHOG000065980.
InParanoidiP47103.
KOiK01802.
OMAiDIYEEYP.
OrthoDBiEOG7HMS9R.

Enzyme and pathway databases

BioCyciYEAST:YJR032W-MONOMER.

Miscellaneous databases

NextBioi974116.
PROiP47103.

Family and domain databases

Gene3Di1.10.150.160. 1 hit.
1.25.40.10. 1 hit.
2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR023114. Elongated_TPR_rpt_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
PF00515. TPR_1. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of two CyP-40-like cyclophilins in Saccharomyces cerevisiae, one of which is required for normal growth."
    Duina A.A., Marsh J.A., Gaber R.F.
    Yeast 12:943-952(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The sequence of 24.3 kb from chromosome X reveals five complete open reading frames, all of which correspond to new genes, and a tandem insertion of a Ty1 transposon."
    Zagulski M., Babinska B., Gromadka R., Migdalski A., Rytka J., Sulicka J., Herbert C.J.
    Yeast 11:1179-1186(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCYP7_YEAST
AccessioniPrimary (citable) accession number: P47103
Secondary accession number(s): D6VWK5, Q92323
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3230 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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