ID   CYPR_YEAST              Reviewed;         318 AA.
AC   P25334; D6VR72; P25658;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase CPR4;
DE            Short=PPIase CPR4;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   Name=CPR4; Synonyms=CYP4, SCC3; OrderedLocusNames=YCR069W;
GN   ORFNames=YCR69W/YCR70W;
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 [GENOMIC DNA].
RX   PubMed=1803821; DOI=10.1002/yea.320070909;
RA   Franco L., Jimenez A., Demolder J., Molemans F., Contreras R.;
RT   "The nucleotide sequence of a third cyclophilin-homologous gene from
RT   Saccharomyces cerevisiae.";
RL   Yeast 7:971-979(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
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).
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: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; X59720; CAA42275.1; -; Genomic_DNA.
DR   EMBL; AY558152; AAS56478.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07541.1; -; Genomic_DNA.
DR   PIR; S26658; CSBYC3.
DR   RefSeq; NP_009995.1; NM_001178780.1.
DR   AlphaFoldDB; P25334; -.
DR   SMR; P25334; -.
DR   BioGRID; 31045; 49.
DR   IntAct; P25334; 5.
DR   MINT; P25334; -.
DR   STRING; 4932.YCR069W; -.
DR   GlyCosmos; P25334; 1 site, No reported glycans.
DR   GlyGen; P25334; 1 site.
DR   iPTMnet; P25334; -.
DR   MaxQB; P25334; -.
DR   PaxDb; 4932-YCR069W; -.
DR   PeptideAtlas; P25334; -.
DR   EnsemblFungi; YCR069W_mRNA; YCR069W; YCR069W.
DR   GeneID; 850433; -.
DR   KEGG; sce:YCR069W; -.
DR   AGR; SGD:S000000665; -.
DR   SGD; S000000665; CPR4.
DR   VEuPathDB; FungiDB:YCR069W; -.
DR   eggNOG; KOG0880; Eukaryota.
DR   HOGENOM; CLU_012062_4_1_1; -.
DR   InParanoid; P25334; -.
DR   OMA; LYEPNPP; -.
DR   OrthoDB; 1966837at2759; -.
DR   BioCyc; YEAST:YCR069W-MONOMER; -.
DR   BioGRID-ORCS; 850433; 5 hits in 10 CRISPR screens.
DR   PRO; PR:P25334; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25334; Protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0016020; C:membrane; 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   CDD; cd00317; cyclophilin; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
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; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Isomerase; Membrane; Reference proteome; Rotamase; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..318
FT                   /note="Peptidyl-prolyl cis-trans isomerase CPR4"
FT                   /id="PRO_0000025494"
FT   TRANSMEM        286..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          55..225
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   318 AA;  35780 MW;  E23AE2763BF5DEE4 CRC64;
     MWLKSLLLCL YSLVLCQVHA APSSGKQITS KDVDLQKKYE PSPPATHRGI ITIEYFDPVS
     KSMKEADLTF ELYGTVVPKT VNNFAMLAHG VKAVIEGKDP NDIHTYSYRK TKINKVYPNK
     YIQGGVVAPD VGPFTVYGPK FDDENFYLKH DRPERLAMAY FGPDSNTSEF IITTKADGNE
     ELDGKSVVFG QITSGLDQLM DAIQYTETDE YGKPQHELRF LYFVLEILKI SNILDLHAAY
     TEKVEKFRNG DVSVGSTLEN IFRNDKAYTP LTTSTGTTAY DLNHPISRAL MCLTVLGLCF
     IAYKGMHEKP HTVSLRHK
//