ID   CYPD_YEAST              Reviewed;         225 AA.
AC   P35176; D6VST3;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase D {ECO:0000305};
DE            Short=PPIase D;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin D {ECO:0000303|PubMed:8377189};
DE   AltName: Full=Cyclosporin-sensitive proline rotamase 5 {ECO:0000303|PubMed:9371805};
DE   AltName: Full=Rotamase D;
DE   Flags: Precursor;
GN   Name=CPR5 {ECO:0000303|PubMed:9371805};
GN   Synonyms=CYP5, CYPD {ECO:0000303|PubMed:8377189};
GN   OrderedLocusNames=YDR304C {ECO:0000312|SGD:S000002712};
GN   ORFNames=D9740.14;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX   PubMed=8377189; DOI=10.1006/jmbi.1993.1497;
RA   Frigerio G., Pelham H.R.B.;
RT   "A Saccharomyces cerevisiae cyclophilin resident in the endoplasmic
RT   reticulum.";
RL   J. Mol. Biol. 233:183-188(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   INDUCTION.
RX   PubMed=9371805; DOI=10.1073/pnas.94.24.13093;
RA   Dolinski K., Muir S., Cardenas M., Heitman J.;
RT   "All cyclophilins and FK506 binding proteins are, individually and
RT   collectively, dispensable for viability in Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:13093-13098(1997).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=29897761; DOI=10.1021/acs.jproteome.8b00032;
RA   He C., Jia C., Zhang Y., Xu P.;
RT   "Enrichment-based proteogenomics identifies microproteins, missing
RT   proteins, and novel smORFs in Saccharomyces cerevisiae.";
RL   J. Proteome Res. 17:2335-2344(2018).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000269|PubMed:8377189}.
CC   -!- INDUCTION: Induced by ER stress caused by treatment with tunicamycin.
CC       {ECO:0000269|PubMed:9371805}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X73142; CAA51658.1; -; mRNA.
DR   EMBL; U28374; AAB64740.1; -; Genomic_DNA.
DR   EMBL; AY557734; AAS56060.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12143.1; -; Genomic_DNA.
DR   PIR; S38324; S38324.
DR   RefSeq; NP_010590.3; NM_001180612.3.
DR   AlphaFoldDB; P35176; -.
DR   SMR; P35176; -.
DR   BioGRID; 32356; 134.
DR   DIP; DIP-5222N; -.
DR   IntAct; P35176; 1.
DR   MINT; P35176; -.
DR   STRING; 4932.YDR304C; -.
DR   GlyCosmos; P35176; 1 site, No reported glycans.
DR   GlyGen; P35176; 1 site.
DR   iPTMnet; P35176; -.
DR   MaxQB; P35176; -.
DR   PaxDb; 4932-YDR304C; -.
DR   PeptideAtlas; P35176; -.
DR   EnsemblFungi; YDR304C_mRNA; YDR304C; YDR304C.
DR   GeneID; 851898; -.
DR   KEGG; sce:YDR304C; -.
DR   AGR; SGD:S000002712; -.
DR   SGD; S000002712; CPR5.
DR   VEuPathDB; FungiDB:YDR304C; -.
DR   eggNOG; KOG0880; Eukaryota.
DR   GeneTree; ENSGT00940000167766; -.
DR   HOGENOM; CLU_012062_4_1_1; -.
DR   InParanoid; P35176; -.
DR   OMA; TVKQTSW; -.
DR   OrthoDB; 339082at2759; -.
DR   BioCyc; YEAST:YDR304C-MONOMER; -.
DR   BioGRID-ORCS; 851898; 5 hits in 10 CRISPR screens.
DR   PRO; PR:P35176; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P35176; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:SGD.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   SWISS-2DPAGE; P35176; -.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Isomerase; Reference proteome;
KW   Rotamase; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..225
FT                   /note="Peptidyl-prolyl cis-trans isomerase D"
FT                   /id="PRO_0000025488"
FT   DOMAIN          37..195
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   MOTIF           222..225
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   225 AA;  25327 MW;  F4861424C8443B58 CRC64;
     MKLQFFSFIT LFACLFTTAI FAKEDTAEDP EITHKVYFDI NHGDKQIGRI VMGLYGLTTP
     QTVENFYQLT ISRDPKMGYL NSIFHRVIPN FMIQGGDFTH RSGIGGKSIF GNTFKDENFD
     VKHDKPGRLS MANRGKNTNG SQFFITTVPC PWLDGKHVVF GEVLDGMDVV HYIENVKTDS
     RNMPVKEVII VESGELETVP LDNKDAAKLQ EEIKAEASEA AHDEL
//