CYPB_YEAST
ID CYPB_YEAST Reviewed; 205 AA.
AC P23285; D3DL06;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase B;
DE Short=PPIase B;
DE EC=5.2.1.8 {ECO:0000269|PubMed:1761234};
DE AltName: Full=Cyclophilin B;
DE AltName: Full=Cyclophilin-related protein;
DE AltName: Full=Rotamase B;
DE Flags: Precursor;
GN Name=CPR2; Synonyms=CRG, CYP2, SCC2; OrderedLocusNames=YHR057C;
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=2183199; DOI=10.1093/nar/18.6.1643;
RA Koser P., Sylvester D., Livi G.P., Bergsma D.J.;
RT "A second cyclophilin-related gene in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 18:1643-1643(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1761234; DOI=10.1016/0378-1119(91)90489-x;
RA Koser P., Bergsma D.J., Cafferkey R., Eng W.-K., McLaughlin M.M.,
RA Ferrara A., Silverman C., Kasyan K., Bossard M.J., Johnson R.K.,
RA Porter T.G., Levy M.A., Livi G.P.;
RT "The CYP2 gene of Saccharomyces cerevisiae encodes a cyclosporin A-
RT sensitive peptidyl-prolyl cis-trans isomerase with an N-terminal signal
RT sequence.";
RL Gene 108:73-80(1991).
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. {ECO:0000305|PubMed:1761234}.
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:1761234};
CC -!- ACTIVITY REGULATION: Cyclosporin A (CsA) inhibits CYPB.
CC {ECO:0000269|PubMed:1761234}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MISCELLANEOUS: Present with 339 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B
CC subfamily. {ECO:0000305}.
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DR EMBL; X51497; CAA35865.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U00061; AAB68386.1; -; Genomic_DNA.
DR EMBL; AY558279; AAS56605.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06750.1; -; Genomic_DNA.
DR PIR; S12324; S12324.
DR RefSeq; NP_011924.1; NM_001179187.1.
DR AlphaFoldDB; P23285; -.
DR SMR; P23285; -.
DR BioGRID; 36489; 86.
DR DIP; DIP-1280N; -.
DR IntAct; P23285; 3.
DR MINT; P23285; -.
DR STRING; 4932.YHR057C; -.
DR MaxQB; P23285; -.
DR PaxDb; P23285; -.
DR PRIDE; P23285; -.
DR EnsemblFungi; YHR057C_mRNA; YHR057C; YHR057C.
DR GeneID; 856454; -.
DR KEGG; sce:YHR057C; -.
DR SGD; S000001099; CPR2.
DR VEuPathDB; FungiDB:YHR057C; -.
DR eggNOG; KOG0880; Eukaryota.
DR GeneTree; ENSGT00940000167766; -.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; P23285; -.
DR OMA; VMKMQSF; -.
DR BioCyc; YEAST:YHR057C-MON; -.
DR PRO; PR:P23285; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P23285; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000324; C:fungal-type vacuole; HDA: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: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; 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 Isomerase; Reference proteome; Rotamase; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..205
FT /note="Peptidyl-prolyl cis-trans isomerase B"
FT /id="PRO_0000025486"
FT DOMAIN 39..198
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 205 AA; 22769 MW; 616EAEB434837A6D CRC64;
MKFSGLWCWL LLFLSVNVIA SDVGELIDQD DEVITQKVFF DIEHGEEKVG RIVIGLYGKV
CPKTAKNFYK LSTTTNSKKG FIGSTFHRVI PNFMVQGGDF TDGTGVGGKS IYGDTFPDEN
FTLKHDRKGR LSMANRGKDT NGSQFFITTT EEASWLDGKH VVFGQVVDGM DVVNYIQHVS
RDANDKPLEA VKIAKCGEWT PELSS
