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P35176

- CYPD_YEAST

UniProt

P35176 - CYPD_YEAST

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Protein

Peptidyl-prolyl cis-trans isomerase D

Gene

CPR5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 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.

Catalytic activityi

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

GO - Molecular functioni

  1. peptide binding Source: UniProtKB-KW
  2. peptidyl-prolyl cis-trans isomerase activity Source: SGD

GO - Biological processi

  1. protein folding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Enzyme and pathway databases

BioCyciYEAST:YDR304C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase D (EC:5.2.1.8)
Short name:
PPIase D
Alternative name(s):
Cyclophilin D
Rotamase D
Gene namesi
Name:CPR5
Synonyms:CYP5, CYPD
Ordered Locus Names:YDR304C
ORF Names:D9740.14
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR304c.
SGDiS000002712. CPR5.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 225203Peptidyl-prolyl cis-trans isomerase DPRO_0000025488Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP35176.
PaxDbiP35176.
PeptideAtlasiP35176.

2D gel databases

SWISS-2DPAGEP35176.

Expressioni

Gene expression databases

GenevestigatoriP35176.

Interactioni

Protein-protein interaction databases

BioGridi32356. 37 interactions.
DIPiDIP-5222N.
IntActiP35176. 1 interaction.
MINTiMINT-568324.
STRINGi4932.YDR304C.

Structurei

3D structure databases

ProteinModelPortaliP35176.
SMRiP35176. Positions 29-196.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 195159PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi222 – 2254Prevents secretion from ER

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119072.
HOGENOMiHOG000065981.
InParanoidiP35176.
KOiK03770.
OMAiVGSKFHR.
OrthoDBiEOG757D7G.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P35176-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLQFFSFIT LFACLFTTAI FAKEDTAEDP EITHKVYFDI NHGDKQIGRI
60 70 80 90 100
VMGLYGLTTP QTVENFYQLT ISRDPKMGYL NSIFHRVIPN FMIQGGDFTH
110 120 130 140 150
RSGIGGKSIF GNTFKDENFD VKHDKPGRLS MANRGKNTNG SQFFITTVPC
160 170 180 190 200
PWLDGKHVVF GEVLDGMDVV HYIENVKTDS RNMPVKEVII VESGELETVP
210 220
LDNKDAAKLQ EEIKAEASEA AHDEL
Length:225
Mass (Da):25,327
Last modified:February 1, 1994 - v1
Checksum:iF4861424C8443B58
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X73142 mRNA. Translation: CAA51658.1.
U28374 Genomic DNA. Translation: AAB64740.1.
AY557734 Genomic DNA. Translation: AAS56060.1.
BK006938 Genomic DNA. Translation: DAA12143.1.
PIRiS38324.
RefSeqiNP_010590.3. NM_001180612.3.

Genome annotation databases

EnsemblFungiiYDR304C; YDR304C; YDR304C.
GeneIDi851898.
KEGGisce:YDR304C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X73142 mRNA. Translation: CAA51658.1 .
U28374 Genomic DNA. Translation: AAB64740.1 .
AY557734 Genomic DNA. Translation: AAS56060.1 .
BK006938 Genomic DNA. Translation: DAA12143.1 .
PIRi S38324.
RefSeqi NP_010590.3. NM_001180612.3.

3D structure databases

ProteinModelPortali P35176.
SMRi P35176. Positions 29-196.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32356. 37 interactions.
DIPi DIP-5222N.
IntActi P35176. 1 interaction.
MINTi MINT-568324.
STRINGi 4932.YDR304C.

2D gel databases

SWISS-2DPAGE P35176.

Proteomic databases

MaxQBi P35176.
PaxDbi P35176.
PeptideAtlasi P35176.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR304C ; YDR304C ; YDR304C .
GeneIDi 851898.
KEGGi sce:YDR304C.

Organism-specific databases

CYGDi YDR304c.
SGDi S000002712. CPR5.

Phylogenomic databases

eggNOGi COG0652.
GeneTreei ENSGT00760000119072.
HOGENOMi HOG000065981.
InParanoidi P35176.
KOi K03770.
OMAi VGSKFHR.
OrthoDBi EOG757D7G.

Enzyme and pathway databases

BioCyci YEAST:YDR304C-MONOMER.

Miscellaneous databases

NextBioi 969898.

Gene expression databases

Genevestigatori P35176.

Family and domain databases

Gene3Di 2.40.100.10. 1 hit.
InterProi IPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view ]
Pfami PF00160. Pro_isomerase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSi PR00153. CSAPPISMRASE.
SUPFAMi SSF50891. SSF50891. 1 hit.
PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A Saccharomyces cerevisiae cyclophilin resident in the endoplasmic reticulum."
    Frigerio G., Pelham H.R.B.
    J. Mol. Biol. 233:183-188(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [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 nameiCYPD_YEAST
AccessioniPrimary (citable) accession number: P35176
Secondary accession number(s): D6VST3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 29, 2014
This is version 130 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3