CYPC_YEAST
ID CYPC_YEAST Reviewed; 182 AA.
AC P25719; D6W0K5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase C, mitochondrial;
DE Short=PPIase C;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin C;
DE AltName: Full=PPI-III;
DE AltName: Full=Rotamase C;
DE Flags: Precursor;
GN Name=CPR3; Synonyms=CYP3; OrderedLocusNames=YML078W;
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], AND PROTEIN SEQUENCE OF 21-35.
RX PubMed=1547957; DOI=10.1016/0378-1119(92)90606-p;
RA McLaughlin M.M., Bossard M.J., Koser P.L., Cafferkey R., Morris R.A.,
RA Miles L.M., Strickler J., Bergsma D.J., Levy M.A., Livi G.P.;
RT "The yeast cyclophilin multigene family: purification, cloning and
RT characterization of a new isoform.";
RL Gene 111:85-92(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1454795; DOI=10.1073/pnas.89.23.11169;
RA Davis E.S., Becker A., Heitman J., Hall M.N., Brennan M.B.;
RT "A yeast cyclophilin gene essential for lactate metabolism at high
RT temperature.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11169-11173(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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 PARTIAL PROTEIN SEQUENCE OF 21-63, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8431466; DOI=10.1016/0167-4838(93)90209-a;
RA Hasumi H., Nishikawa T.;
RT "Purification and properties of multiple molecular forms of yeast peptidyl
RT prolyl cis-trans isomerase.";
RL Biochim. Biophys. Acta 1161:161-167(1993).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7603990; DOI=10.1073/pnas.92.14.6319;
RA Matouschek A., Rospert S., Schmid K., Glick B.S., Schatz G.;
RT "Cyclophilin catalyzes protein folding in yeast mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:6319-6323(1995).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ARG-73 AND HIS-144.
RX PubMed=10025965; DOI=10.1016/s0014-5793(98)01735-9;
RA Scholz C., Maier P., Dolinski K., Heitman J., Schmid F.X.;
RT "R73A and H144Q mutants of the yeast mitochondrial cyclophilin Cpr3 exhibit
RT a low prolyl isomerase activity in both peptide and protein-folding
RT assays.";
RL FEBS Lett. 443:367-369(1999).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
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).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. This isozyme is required for growth on lactate at high
CC temperature. {ECO:0000269|PubMed:10025965, ECO:0000269|PubMed:7603990,
CC ECO:0000269|PubMed:8431466}.
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; Evidence={ECO:0000269|PubMed:8431466};
CC -!- ACTIVITY REGULATION: Inhibited by the immunosuppressant drug
CC cyclosporin A and by SDZ NIM811, a PPIase inhibitor.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:7603990}.
CC -!- MISCELLANEOUS: Present with 1960 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; M84758; AAA34548.1; -; Genomic_DNA.
DR EMBL; X56962; CAA40282.1; -; Genomic_DNA.
DR EMBL; Z46373; CAA86500.1; -; Genomic_DNA.
DR EMBL; AY557761; AAS56087.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09819.1; -; Genomic_DNA.
DR PIR; S30507; S30507.
DR RefSeq; NP_013633.1; NM_001182437.1.
DR AlphaFoldDB; P25719; -.
DR SMR; P25719; -.
DR BioGRID; 35063; 76.
DR DIP; DIP-6534N; -.
DR IntAct; P25719; 2.
DR MINT; P25719; -.
DR STRING; 4932.YML078W; -.
DR iPTMnet; P25719; -.
DR MaxQB; P25719; -.
DR PaxDb; P25719; -.
DR PRIDE; P25719; -.
DR EnsemblFungi; YML078W_mRNA; YML078W; YML078W.
DR GeneID; 854897; -.
DR KEGG; sce:YML078W; -.
DR SGD; S000004543; CPR3.
DR VEuPathDB; FungiDB:YML078W; -.
DR eggNOG; KOG0865; Eukaryota.
DR GeneTree; ENSGT00940000176670; -.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; P25719; -.
DR OMA; MRAPIVN; -.
DR BioCyc; YEAST:YML078W-MON; -.
DR PRO; PR:P25719; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P25719; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA: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:0006915; P:apoptotic process; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IDA:SGD.
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; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Isomerase; Mitochondrion; Reference proteome;
KW Rotamase; Transit peptide.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1547957"
FT CHAIN 21..182
FT /note="Peptidyl-prolyl cis-trans isomerase C,
FT mitochondrial"
FT /id="PRO_0000025487"
FT DOMAIN 25..181
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MUTAGEN 73
FT /note="R->A: Strongly reduces in vitro PPIase activity and
FT in vivo protein folding activity. Reduces binding to
FT cyclosporin A 2-fold."
FT /evidence="ECO:0000269|PubMed:10025965"
FT MUTAGEN 144
FT /note="H->Q: Strongly reduces in vitro PPIase activity and
FT in vivo protein folding activity. Reduces binding to
FT cyclosporin A 2-fold."
FT /evidence="ECO:0000269|PubMed:10025965"
SQ SEQUENCE 182 AA; 19919 MW; 96C9A5B75250EF55 CRC64;
MFKRSIIQQS RLFSNSASRL GKKVFFDPAV NGTKIGRIEF ELYDNVVPKT AENFRALCTG
EKGWGYKGVP FHRIIPDFMI QGGDTDLTNG FGGKSIYGSK FADENFVKKH DKAGLLSMAN
AGPNTNGSQF FITTVPCPWL DGKHVVFGEV TKGMDIVKAI ESYGTASGKP RAEIVIEEAG
EL
