ID   CYP8_YEAST              Reviewed;         308 AA.
AC   P53728; D6W1K2; E9P900;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   04-NOV-2026, entry version 169.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP8;
DE            Short=PPIase CYP8;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase CYP8;
GN   Name=CPR8; OrderedLocusNames=YNR028W; ORFNames=N3255;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873; DOI=10.1038/387s093;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [2]
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   [3]
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 (By similarity). {ECO:0000250}.
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;
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DR   EMBL; Z71643; CAA96308.1; -; Genomic_DNA.
DR   EMBL; AY692954; AAT92973.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10568.1; -; Genomic_DNA.
DR   PIR; S63359; S63359.
DR   RefSeq; NP_014425.3; NM_001183205.3.
DR   AlphaFoldDB; P53728; -.
DR   SMR; P53728; -.
DR   BioGRID; 35852; 115.
DR   DIP; DIP-4261N; -.
DR   FunCoup; P53728; 64.
DR   IntAct; P53728; 4.
DR   STRING; 4932.YNR028W; -.
DR   iPTMnet; P53728; -.
DR   PaxDb; 4932-YNR028W; -.
DR   PeptideAtlas; P53728; -.
DR   EnsemblFungi; YNR028W_mRNA; YNR028W; YNR028W.
DR   GeneID; 855762; -.
DR   KEGG; sce:YNR028W; -.
DR   AGR; SGD:S000005311; -.
DR   SGD; S000005311; CPR8.
DR   VEuPathDB; FungiDB:YNR028W; -.
DR   eggNOG; KOG0880; Eukaryota.
DR   HOGENOM; CLU_012062_4_1_1; -.
DR   InParanoid; P53728; -.
DR   OMA; AHKDQTN; -.
DR   OrthoDB; 4051692at2759; -.
DR   BioCyc; YEAST:YNR028W-MONOMER; -.
DR   BioGRID-ORCS; 855762; 0 hits in 10 CRISPR screens.
DR   CD-CODE; E03F929F; Stress granule.
DR   PRO; PR:P53728; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53728; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
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; IPR002130; Cyclophilin-type_PPIase_dom.
DR   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF568; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE CPR4-RELATED; 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   Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..308
FT                   /note="Peptidyl-prolyl cis-trans isomerase CYP8"
FT                   /id="PRO_0000064175"
FT   DOMAIN          56..215
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   CONFLICT        8
FT                   /note="L -> P (in Ref. 3; AAT92973)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   308 AA;  34946 MW;  4E2E75B66134E6B0 CRC64;
     MKSFFLYLYV AFMFSCITAL PLPVDNKRAS SDSLDLKKKY APDPPITHNV NIGIVFTDPE
     SSEEAGRLIT IDLYGTMVPK TVMTFCQYVD SVKDRLASRH SYSPERDFDK ILPNGAIEGS
     SVSSSSIEET EMLAPKLPEE NHSLIHDRPG RVSMIKDDKG LKFIIETSET PLEGESVVFG
     QVTAGLKDLM DKLANVKTDE NGKPEQPITI GYISSQEHRI QHAKEAHEKY LQRLQDYQNG
     DLEKGITLKN YLYQGSQRKL EDAKYNQLHH PLPKIMLGIS VLLLFYVLAK YRKRIFNRSS
     KIVSIRED
//