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Protein

Peptidyl-prolyl cis-trans isomerase CPR4

Gene

CPR4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activityi

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

GO - Molecular functioni

  • peptidyl-prolyl cis-trans isomerase activity Source: SGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BioCyciYEAST:YCR069W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase CPR4 (EC:5.2.1.8)
Short name:
PPIase CPR4
Alternative name(s):
Rotamase
Gene namesi
Name:CPR4
Synonyms:CYP4, SCC3
Ordered Locus Names:YCR069W
ORF Names:YCR69W/YCR70W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome III

Organism-specific databases

CYGDiYCR069w.
EuPathDBiFungiDB:YCR069W.
SGDiS000000665. CPR4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei286 – 30318HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 318298Peptidyl-prolyl cis-trans isomerase CPR4PRO_0000025494Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP25334.
PaxDbiP25334.

Interactioni

Protein-protein interaction databases

BioGridi31045. 5 interactions.
IntActiP25334. 5 interactions.
MINTiMINT-4478613.

Structurei

3D structure databases

ProteinModelPortaliP25334.
SMRiP25334. Positions 40-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 225171PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00530000066609.
HOGENOMiHOG000065981.
InParanoidiP25334.
KOiK01802.
OMAiANALYNG.
OrthoDBiEOG7T1RPW.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P25334-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWLKSLLLCL YSLVLCQVHA APSSGKQITS KDVDLQKKYE PSPPATHRGI
60 70 80 90 100
ITIEYFDPVS KSMKEADLTF ELYGTVVPKT VNNFAMLAHG VKAVIEGKDP
110 120 130 140 150
NDIHTYSYRK TKINKVYPNK YIQGGVVAPD VGPFTVYGPK FDDENFYLKH
160 170 180 190 200
DRPERLAMAY FGPDSNTSEF IITTKADGNE ELDGKSVVFG QITSGLDQLM
210 220 230 240 250
DAIQYTETDE YGKPQHELRF LYFVLEILKI SNILDLHAAY TEKVEKFRNG
260 270 280 290 300
DVSVGSTLEN IFRNDKAYTP LTTSTGTTAY DLNHPISRAL MCLTVLGLCF
310
IAYKGMHEKP HTVSLRHK
Length:318
Mass (Da):35,780
Last modified:May 1, 1992 - v1
Checksum:iE23AE2763BF5DEE4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42275.1.
AY558152 Genomic DNA. Translation: AAS56478.1.
BK006937 Genomic DNA. Translation: DAA07541.1.
PIRiS26658. CSBYC3.
RefSeqiNP_009995.1. NM_001178780.1.

Genome annotation databases

EnsemblFungiiYCR069W; YCR069W; YCR069W.
GeneIDi850433.
KEGGisce:YCR069W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42275.1.
AY558152 Genomic DNA. Translation: AAS56478.1.
BK006937 Genomic DNA. Translation: DAA07541.1.
PIRiS26658. CSBYC3.
RefSeqiNP_009995.1. NM_001178780.1.

3D structure databases

ProteinModelPortaliP25334.
SMRiP25334. Positions 40-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31045. 5 interactions.
IntActiP25334. 5 interactions.
MINTiMINT-4478613.

Proteomic databases

MaxQBiP25334.
PaxDbiP25334.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYCR069W; YCR069W; YCR069W.
GeneIDi850433.
KEGGisce:YCR069W.

Organism-specific databases

CYGDiYCR069w.
EuPathDBiFungiDB:YCR069W.
SGDiS000000665. CPR4.

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00530000066609.
HOGENOMiHOG000065981.
InParanoidiP25334.
KOiK01802.
OMAiANALYNG.
OrthoDBiEOG7T1RPW.

Enzyme and pathway databases

BioCyciYEAST:YCR069W-MONOMER.

Miscellaneous databases

NextBioi966021.
PROiP25334.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of a third cyclophilin-homologous gene from Saccharomyces cerevisiae."
    Franco L., Jimenez A., Demolder J., Molemans F., Contreras R.
    Yeast 7:971-979(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.

Entry informationi

Entry nameiCYPR_YEAST
AccessioniPrimary (citable) accession number: P25334
Secondary accession number(s): D6VR72, P25658
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 22, 2015
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

External Data

Dasty 3

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 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.