CYP8_YEAST
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 03-AUG-2022, entry version 153.
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;
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; 113.
DR DIP; DIP-4261N; -.
DR IntAct; P53728; 4.
DR MINT; P53728; -.
DR STRING; 4932.YNR028W; -.
DR iPTMnet; P53728; -.
DR MaxQB; P53728; -.
DR PaxDb; P53728; -.
DR PRIDE; P53728; -.
DR EnsemblFungi; YNR028W_mRNA; YNR028W; YNR028W.
DR GeneID; 855762; -.
DR KEGG; sce:YNR028W; -.
DR SGD; S000005311; CPR8.
DR VEuPathDB; FungiDB:YNR028W; -.
DR eggNOG; KOG0880; Eukaryota.
DR HOGENOM; CLU_012062_4_1_1; -.
DR OMA; ETEMLAP; -.
DR BioCyc; YEAST:YNR028W-MON; -.
DR PRO; PR:P53728; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53728; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
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 GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 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
