ETFB_YEAST
ID ETFB_YEAST Reviewed; 261 AA.
AC P42940; D6VUZ0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Probable electron transfer flavoprotein subunit beta;
DE Short=Beta-ETF;
DE AltName: Full=Changed intracellular redox state protein 1;
GN Name=CIR1; OrderedLocusNames=YGR207C; ORFNames=G7742;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8904340;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<273::aid-yea898>3.0.co;2-1;
RA Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A.,
RA Rodrigues-Pousada C.;
RT "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII
RT reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the
RT yeast PMT and EF1G genes, of the human and bacterial electron-transferring
RT flavoproteins (beta-chain) and of the Escherichia coli phosphoserine
RT phosphohydrolase, and five new ORFs.";
RL Yeast 12:273-280(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 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 [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).
RN [7]
RP INTERACTION WITH YHF1.
RX PubMed=15961414; DOI=10.1093/hmg/ddi214;
RA Gonzalez-Cabo P., Vazquez-Manrique R.P., Garcia-Gimeno M.A., Sanz P.,
RA Palau F.;
RT "Frataxin interacts functionally with mitochondrial electron transport
RT chain proteins.";
RL Hum. Mol. Genet. 14:2091-2098(2005).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=21253464; DOI=10.2174/1874285801004010075;
RA Lopes J., Pinto M.J., Rodrigues A., Vasconcelos F., Oliveira R.;
RT "The Saccharomyces cerevisiae genes, AIM45, YGR207c/CIR1 and YOR356w/CIR2,
RT are involved in cellular redox state under stress conditions.";
RL Open Microbiol. J. 4:75-82(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: The electron transfer flavoprotein serves as a specific
CC electron acceptor for several dehydrogenases, including five acyl-CoA
CC dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers
CC the electrons to the main mitochondrial respiratory chain via ETF-
CC ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per dimer. {ECO:0000250};
CC -!- COFACTOR:
CC Name=AMP; Xref=ChEBI:CHEBI:456215; Evidence={ECO:0000250};
CC Note=Binds 1 AMP per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (By similarity).
CC Interacts with YFH1. {ECO:0000250, ECO:0000269|PubMed:15961414}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Displays higher growth rate and higher
CC sensitivity to superoxide and heat stress, on nonfermentable carbon
CC sources. Leads to decreased intracellular oxidation upon heat shock.
CC Under conditions of mitochondrial perturbation by antimycin A, displays
CC increased peroxisomal proliferation. {ECO:0000269|PubMed:21253464}.
CC -!- MISCELLANEOUS: Present with 2400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ETF beta-subunit/FixA family. {ECO:0000305}.
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DR EMBL; Z49133; CAA89000.1; -; Genomic_DNA.
DR EMBL; Z72992; CAA97234.1; -; Genomic_DNA.
DR EMBL; AY558378; AAS56704.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08301.1; -; Genomic_DNA.
DR PIR; S53930; S53930.
DR RefSeq; NP_011723.1; NM_001181336.1.
DR AlphaFoldDB; P42940; -.
DR SMR; P42940; -.
DR BioGRID; 33460; 43.
DR DIP; DIP-3865N; -.
DR IntAct; P42940; 1.
DR MINT; P42940; -.
DR STRING; 4932.YGR207C; -.
DR iPTMnet; P42940; -.
DR MaxQB; P42940; -.
DR PaxDb; P42940; -.
DR PRIDE; P42940; -.
DR EnsemblFungi; YGR207C_mRNA; YGR207C; YGR207C.
DR GeneID; 853121; -.
DR KEGG; sce:YGR207C; -.
DR SGD; S000003439; CIR1.
DR VEuPathDB; FungiDB:YGR207C; -.
DR eggNOG; KOG3180; Eukaryota.
DR GeneTree; ENSGT00390000009936; -.
DR HOGENOM; CLU_060196_0_1_1; -.
DR InParanoid; P42940; -.
DR OMA; YNGGMVP; -.
DR BioCyc; YEAST:G3O-30890-MON; -.
DR Reactome; R-SCE-611105; Respiratory electron transport.
DR PRO; PR:P42940; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P42940; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR CDD; cd01714; ETF_beta; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR000049; ET-Flavoprotein_bsu_CS.
DR InterPro; IPR014730; ETF_a/b_N.
DR InterPro; IPR012255; ETF_b.
DR InterPro; IPR033948; ETF_beta_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR21294; PTHR21294; 1.
DR Pfam; PF01012; ETF; 1.
DR PIRSF; PIRSF000090; Beta-ETF; 1.
DR SMART; SM00893; ETF; 1.
DR PROSITE; PS01065; ETF_BETA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Electron transport; FAD; Flavoprotein; Mitochondrion;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..261
FT /note="Probable electron transfer flavoprotein subunit
FT beta"
FT /id="PRO_0000167874"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 261 AA; 28759 MW; FF202BEC144B97E0 CRC64;
MSAKQQLRIL VPVKRVVDFQ IKPRVNKTLT GIETSGIKFS INPFDDIAVE EAIRIKEKNK
SLVESTHAVS IGSAKAQDIL RNCLAKGIDT CSLIDSVGKE NIEPLAIAKI LKAVVEKKGS
NLVLMGKQAI DDDCNNTGQM LAGLLNWPQA TNAAKVEFLD NGRVQVTREI DDGEEVIEAS
LPMVITTDLR LNTPRYVGLP KLMKAKKKPI EKLDIAKDFP EINIEPQLKI VSMEEPKTKS
PGVKLNSVDE LIEKLKEVKA I
