Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P23285 (CYPB_YEAST)

Last modified June 16, 2009. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl cis-trans isomerase B
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin B
    Cyclophilin-related protein
Gene names
Name: CPR2
Synonyms: CRG, CYP2, SCC2
Ordered Locus Names: YHR057C
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

Cyclosporin A (CsA) inhibits CYPB.

Subcellular location

Secreted.

Miscellaneous

Present with 339 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase B subfamily.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCyclosporin
   Molecular functionIsomerase
Rotamase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpeptide binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-prolyl cis-trans isomerase activity Ref.4

Inferred from direct assay. Source: SGD

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 205185Peptidyl-prolyl cis-trans isomerase B
PRO_0000025486

Regions

Domain39 – 198160PPIase cyclophilin-type

Sequences

Sequence LengthMass (Da)Tools
P23285-1 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 616EAEB434837A6D

FASTA20522,769
        10         20         30         40         50         60 
MKFSGLWCWL LLFLSVNVIA SDVGELIDQD DEVITQKVFF DIEHGEEKVG RIVIGLYGKV 

        70         80         90        100        110        120 
CPKTAKNFYK LSTTTNSKKG FIGSTFHRVI PNFMVQGGDF TDGTGVGGKS IYGDTFPDEN 

       130        140        150        160        170        180 
FTLKHDRKGR LSMANRGKDT NGSQFFITTT EEASWLDGKH VVFGQVVDGM DVVNYIQHVS 

       190        200 
RDANDKPLEA VKIAKCGEWT PELSS 

« Hide

References

« Hide 'large scale' references
[1]"A second cyclophilin-related gene in Saccharomyces cerevisiae."
Koser P., Sylvester D., Livi G.P., Bergsma D.J.
Nucleic Acids Res. 18:1643-1643(1990) [PubMed: 2183199] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The CYP2 gene of Saccharomyces cerevisiae encodes a cyclosporin A-sensitive peptidyl-prolyl cis-trans isomerase with an N-terminal signal sequence."
Koser P., Bergsma D.J., Cafferkey R., Eng W.-K., McLaughlin M.M., Ferrara A., Silverman C., Kasyan K., Bossard M.J., Johnson R.K., Porter T.G., Levy M.A., Livi G.P.
Gene 108:73-80(1991) [PubMed: 1761234] [Abstract]
Cited for: CHARACTERIZATION.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

X51497 Genomic DNA. Translation: CAA35865.1. Sequence problems.
U00061 Genomic DNA. Translation: AAB68386.1.
AY558279 Genomic DNA. Translation: AAS56605.1.
PIRS12324.
RefSeqNP_011924.1.

3D structure databases

HSSPHSSP built from PDB template 1CYN based on UniProtKB P23284.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:1280N.
IntActP23285. 6 interactions.

Genome annotation databases

EnsemblYHR057C. Saccharomyces cerevisiae. [Contig view]
GeneID856454.
GenomeReviewsGene locus YHR057C in contig U00093_GR.
KEGGsce:YHR057C.
NMPDRfig|4932.3.peg.3077.

Organism-specific databases

CYGDYHR057c.
SGDS000001099. CPR2.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP23285.
OMAP23285. MANAGED.

Enzyme and pathway databases

BRENDA5.2.1.8. 250.

Gene expression databases

GermOnlineYHR057C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR002130. PPIase_cyclophilin.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio982087.

Entry information

Entry nameCYPB_YEAST
AccessionPrimary (citable) accession number: P23285
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: June 16, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VIII

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents