CYP7_YEAST
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 03-AUG-2022, entry version 181.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 PDBsum; 5JHE; -.
DR AlphaFoldDB; P47103; -.
DR SMR; P47103; -.
DR BioGRID; 33785; 349.
DR DIP; DIP-2312N; -.
DR IntAct; P47103; 11.
DR MINT; P47103; -.
DR STRING; 4932.YJR032W; -.
DR MaxQB; P47103; -.
DR PaxDb; P47103; -.
DR PRIDE; P47103; -.
DR EnsemblFungi; YJR032W_mRNA; YJR032W; YJR032W.
DR GeneID; 853489; -.
DR KEGG; sce:YJR032W; -.
DR SGD; S000003793; CPR7.
DR VEuPathDB; FungiDB:YJR032W; -.
DR eggNOG; KOG0546; Eukaryota.
DR HOGENOM; CLU_012062_37_0_1; -.
DR InParanoid; P47103; -.
DR OMA; FFITTYP; -.
DR BioCyc; YEAST:YJR032W-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:P47103; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47103; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IDA:SGD.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.40.100.10; -; 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; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00515; TPR_1; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50891; SSF50891; 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.
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 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 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
