ID   CYP7_YEAST              Reviewed;         393 AA.
AC   P47103; D6VWK5; Q92323;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 198.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP7;
DE            Short=PPIase CYP7;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase CYP7;
GN   Name=CPR7; OrderedLocusNames=YJR032W; ORFNames=J1585;
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=8873448;
RX   DOI=10.1002/(sici)1097-0061(199608)12:10<943::aid-yea997>3.0.co;2-3;
RA   Duina A.A., Marsh J.A., Gaber R.F.;
RT   "Identification of two CyP-40-like cyclophilins in Saccharomyces
RT   cerevisiae, one of which is required for normal growth.";
RL   Yeast 12:943-952(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8619316; DOI=10.1002/yea.320111208;
RA   Zagulski M., Babinska B., Gromadka R., Migdalski A., Rytka J., Sulicka J.,
RA   Herbert C.J.;
RT   "The sequence of 24.3 kb from chromosome X reveals five complete open
RT   reading frames, all of which correspond to new genes, and a tandem
RT   insertion of a Ty1 transposon.";
RL   Yeast 11:1179-1186(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [4]
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   [5]
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   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. Plays a major role in negative regulation of the heat
CC       shock transcription factor (HSF).
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   -!- SUBUNIT: Interacts with RPD3 and CNS1.
CC   -!- INTERACTION:
CC       P47103; P33313: CNS1; NbExp=2; IntAct=EBI-5436, EBI-4806;
CC       P47103; P15108: HSC82; NbExp=2; IntAct=EBI-5436, EBI-8666;
CC       P47103; P02829: HSP82; NbExp=6; IntAct=EBI-5436, EBI-8659;
CC       P47103; P32561: RPD3; NbExp=2; IntAct=EBI-5436, EBI-15864;
CC   -!- MISCELLANEOUS: Present with 3230 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; U48868; AAC49415.1; -; Genomic_DNA.
DR   EMBL; Z49532; CAA89559.1; -; Genomic_DNA.
DR   EMBL; X87297; CAA60725.1; -; Genomic_DNA.
DR   EMBL; AY693103; AAT93122.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08821.1; -; Genomic_DNA.
DR   PIR; S57050; S57050.
DR   RefSeq; NP_012566.1; NM_001181690.1.
DR   PDB; 5JHE; X-ray; 1.80 A; A=1-393.
DR   AlphaFoldDB; P47103; -.
DR   SMR; P47103; -.
DR   BioGRID; 33785; 356.
DR   DIP; DIP-2312N; -.
DR   FunCoup; P47103; 97.
DR   IntAct; P47103; 11.
DR   MINT; P47103; -.
DR   STRING; 4932.YJR032W; -.
DR   iPTMnet; P47103; -.
DR   PaxDb; 4932-YJR032W; -.
DR   PeptideAtlas; P47103; -.
DR   EnsemblFungi; YJR032W_mRNA; YJR032W; YJR032W.
DR   GeneID; 853489; -.
DR   KEGG; sce:YJR032W; -.
DR   AGR; SGD:S000003793; -.
DR   SGD; S000003793; CPR7.
DR   VEuPathDB; FungiDB:YJR032W; -.
DR   eggNOG; KOG0546; Eukaryota.
DR   HOGENOM; CLU_012062_37_0_1; -.
DR   InParanoid; P47103; -.
DR   OMA; QFFITTY; -.
DR   OrthoDB; 407558at2759; -.
DR   BioCyc; YEAST:YJR032W-MONOMER; -.
DR   Reactome; R-SCE-8939211; ESR-mediated signaling.
DR   BioGRID-ORCS; 853489; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P47103; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47103; protein.
DR   GO; GO:0005829; C:cytosol; IPI:SGD.
DR   GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:SGD.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IDA:SGD.
DR   FunFam; 2.40.100.10:FF:000044; Cyclophilin 40; 1.
DR   FunFam; 1.25.40.10:FF:000029; peptidyl-prolyl cis-trans isomerase D; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_rpt.
DR   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE D-RELATED; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
DR   PDBsum; 5JHE; -.
PE   1: Evidence at protein level;
KW   3D-structure; Isomerase; Reference proteome; Repeat; Rotamase; TPR repeat.
FT   CHAIN           1..393
FT                   /note="Peptidyl-prolyl cis-trans isomerase CYP7"
FT                   /id="PRO_0000064174"
FT   DOMAIN          8..196
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REPEAT          240..273
FT                   /note="TPR 1"
FT   REPEAT          292..325
FT                   /note="TPR 2"
FT   REPEAT          330..363
FT                   /note="TPR 3"
FT   CONFLICT        237
FT                   /note="L -> F (in Ref. 1; AAC49415)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..5
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   STRAND          6..13
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   STRAND          16..25
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   TURN            27..29
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   HELIX           31..42
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   STRAND          61..66
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   TURN            67..69
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   STRAND          70..73
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   TURN            76..78
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   TURN            87..90
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   HELIX           100..105
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   STRAND          125..131
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   STRAND          140..142
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   STRAND          144..149
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   HELIX           152..154
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   TURN            155..157
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   STRAND          160..166
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   HELIX           168..175
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   STRAND          185..187
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   STRAND          189..196
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   HELIX           199..201
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   STRAND          205..208
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   HELIX           213..215
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   HELIX           222..224
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   HELIX           233..252
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   HELIX           256..273
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   HELIX           274..276
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   TURN            277..279
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   HELIX           281..304
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   HELIX           308..319
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   HELIX           326..342
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   HELIX           346..359
FT                   /evidence="ECO:0007829|PDB:5JHE"
FT   HELIX           366..385
FT                   /evidence="ECO:0007829|PDB:5JHE"
SQ   SEQUENCE   393 AA;  45134 MW;  1532F255E8016F4F CRC64;
     MIQDPLVYLD ISIDKKPIGR IVCKLFREKA PKTTENFYKL CAGDVKSPLK DQQYLSYKGN
     GFHRVVKNFM IQAGDIVFGT QKDSSSSSVG KGGCSIYADK EEVKTDDESF CYGNFEDENL
     GEFVEPFTLG MANLGSPNTN NSQFFITTYA APHLNGKHSI FGQVVHGKSV VRTIENCRVD
     SDGVPESDVR ISDCGVWEKT MGVPLYNASN DQIGGDVYEE YPDDDTHFGD DDFGKALEAA
     NIIKESGTLL FKKKDYSNAF FKYRKSLNYI NEYMPEPDVD KERNIQFINL KMKIYLNLSL
     VLFNLERYDD AIMYATYLLE MDNVPNRDQA KAYYRRGNSY LKKKRLDEAL QDYIFCKEKN
     PDDEVIEQRI EYVNRLIEEN KEKTRKNISK FFS
//