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P35176

- CYPD_YEAST

UniProt

P35176 - CYPD_YEAST

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
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    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
    2. protein peptidyl-prolyl isomerization Source: GOC

    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
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    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. 36 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.
    GeneTreeiENSGT00750000117331.
    HOGENOMiHOG000065981.
    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

    MKLQFFSFIT LFACLFTTAI FAKEDTAEDP EITHKVYFDI NHGDKQIGRI    50
    VMGLYGLTTP QTVENFYQLT ISRDPKMGYL NSIFHRVIPN FMIQGGDFTH 100
    RSGIGGKSIF GNTFKDENFD VKHDKPGRLS MANRGKNTNG SQFFITTVPC 150
    PWLDGKHVVF GEVLDGMDVV HYIENVKTDS RNMPVKEVII VESGELETVP 200
    LDNKDAAKLQ EEIKAEASEA AHDEL 225
    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. 36 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 ENSGT00750000117331.
    HOGENOMi HOG000065981.
    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

    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 1, 2014
    This is version 129 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