PPID_YEAST
ID PPID_YEAST Reviewed; 371 AA.
AC P53691; D6VYL7; Q6Q5K7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CPR6;
DE Short=PPIase CPR6;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase CPR6;
GN Name=CPR6; OrderedLocusNames=YLR216C; ORFNames=L8167.24;
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 [MRNA].
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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).
RN [5]
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.
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.
CC -!- INTERACTION:
CC P53691; P02829: HSP82; NbExp=13; IntAct=EBI-5429, EBI-8659;
CC P53691; P32561: RPD3; NbExp=2; IntAct=EBI-5429, EBI-15864;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 18600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D
CC subfamily. {ECO:0000305}.
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DR EMBL; U48867; AAC49414.1; -; mRNA.
DR EMBL; U14913; AAB67445.1; -; Genomic_DNA.
DR EMBL; AY557959; AAS56285.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09533.1; -; Genomic_DNA.
DR PIR; S48567; S48567.
DR RefSeq; NP_013317.1; NM_001182103.1.
DR AlphaFoldDB; P53691; -.
DR SMR; P53691; -.
DR BioGRID; 31484; 175.
DR DIP; DIP-1274N; -.
DR IntAct; P53691; 34.
DR MINT; P53691; -.
DR STRING; 4932.YLR216C; -.
DR iPTMnet; P53691; -.
DR MaxQB; P53691; -.
DR PaxDb; P53691; -.
DR PRIDE; P53691; -.
DR EnsemblFungi; YLR216C_mRNA; YLR216C; YLR216C.
DR GeneID; 850914; -.
DR KEGG; sce:YLR216C; -.
DR SGD; S000004206; CPR6.
DR VEuPathDB; FungiDB:YLR216C; -.
DR eggNOG; KOG0546; Eukaryota.
DR GeneTree; ENSGT00940000154672; -.
DR HOGENOM; CLU_012062_37_0_1; -.
DR InParanoid; P53691; -.
DR OMA; CKDFGNK; -.
DR BioCyc; YEAST:YLR216C-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:P53691; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P53691; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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:0043022; F:ribosome binding; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0006457; P:protein folding; IDA:SGD.
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; IPR019734; TPR_repeat.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00028; TPR; 1.
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; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isomerase; Reference proteome; Repeat; Rotamase; TPR repeat.
FT CHAIN 1..371
FT /note="Peptidyl-prolyl cis-trans isomerase CPR6"
FT /id="PRO_0000064173"
FT DOMAIN 7..174
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REPEAT 219..252
FT /note="TPR 1"
FT REPEAT 270..303
FT /note="TPR 2"
FT REPEAT 308..341
FT /note="TPR 3"
FT CONFLICT 12
FT /note="I -> V (in Ref. 4; AAS56285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 371 AA; 42072 MW; 188666D94866DDDD CRC64;
MTRPKTFFDI SIGGKPQGRI VFELYNDIVP KTAENFLKLC EGNAGMAKTK PDVPLSYKGS
IFHRVIKDFM CQFGDFTNFN GTGGESIYDE KFEDENFTVK HDKPFLLSMA NAGPNTNGSQ
AFITCVPTPH LDGKHVVFGE VIQGKRIVRL IENQQCDQEN NKPLRDVKID DCGVLPDDYQ
VPENAEATPT DEYGDNYEDV LKQDEKVDLK NFDTVLKAIE TVKNIGTEQF KKQNYSVALE
KYVKCDKFLK EYFPEDLEKE QIEKINQLKV SIPLNIAICA LKLKDYKQVL VASSEVLYAE
AADEKAKAKA LYRRGLAYYH VNDTDMALND LEMATTFQPN DAAILKAIHN TKLKRKQQNE
KAKKSLSKMF S
