ID ETFA_YEAST Reviewed; 344 AA.
AC Q12480; D6W415;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 178.
DE RecName: Full=Probable electron transfer flavoprotein subunit alpha, mitochondrial;
DE Short=Alpha-ETF;
DE AltName: Full=Altered inheritance rate of mitochondria protein 45;
DE Flags: Precursor;
GN Name=AIM45; OrderedLocusNames=YPR004C; ORFNames=LPZ4C, YP9723.04C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
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 [4]
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: 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 -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 2950 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC {ECO:0000305}.
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DR EMBL; Z71255; CAA95044.1; -; Genomic_DNA.
DR EMBL; Z48951; CAA88782.1; -; Genomic_DNA.
DR EMBL; U31900; AAA97583.1; -; Genomic_DNA.
DR EMBL; AY692635; AAT92654.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11431.1; -; Genomic_DNA.
DR PIR; S52817; S52817.
DR RefSeq; NP_015329.1; NM_001184101.1.
DR AlphaFoldDB; Q12480; -.
DR SMR; Q12480; -.
DR BioGRID; 36181; 86.
DR DIP; DIP-5574N; -.
DR IntAct; Q12480; 10.
DR STRING; 4932.YPR004C; -.
DR MaxQB; Q12480; -.
DR PaxDb; 4932-YPR004C; -.
DR PeptideAtlas; Q12480; -.
DR EnsemblFungi; YPR004C_mRNA; YPR004C; YPR004C.
DR GeneID; 856112; -.
DR KEGG; sce:YPR004C; -.
DR AGR; SGD:S000006208; -.
DR SGD; S000006208; AIM45.
DR VEuPathDB; FungiDB:YPR004C; -.
DR eggNOG; KOG3954; Eukaryota.
DR GeneTree; ENSGT00390000013422; -.
DR HOGENOM; CLU_034178_0_1_1; -.
DR InParanoid; Q12480; -.
DR OMA; WRPYAEQ; -.
DR OrthoDB; 5481222at2759; -.
DR BioCyc; YEAST:G3O-34166-MONOMER; -.
DR Reactome; R-SCE-611105; Respiratory electron transport.
DR BioGRID-ORCS; 856112; 0 hits in 10 CRISPR screens.
DR PRO; PR:Q12480; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12480; Protein.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR CDD; cd01715; ETF_alpha; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR014730; ETF_a/b_N.
DR InterPro; IPR001308; ETF_a/FixB.
DR InterPro; IPR033947; ETF_alpha_N.
DR InterPro; IPR014731; ETF_asu_C.
DR InterPro; IPR018206; ETF_asu_C_CS.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR43153; ELECTRON TRANSFER FLAVOPROTEIN ALPHA; 1.
DR PANTHER; PTHR43153:SF1; ELECTRON TRANSFER FLAVOPROTEIN SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF01012; ETF; 1.
DR Pfam; PF00766; ETF_alpha; 1.
DR PIRSF; PIRSF000089; Electra_flavoP_a; 1.
DR SMART; SM00893; ETF; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR PROSITE; PS00696; ETF_ALPHA; 1.
PE 1: Evidence at protein level;
KW Electron transport; FAD; Flavoprotein; Mitochondrion; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..344
FT /note="Probable electron transfer flavoprotein subunit
FT alpha, mitochondrial"
FT /id="PRO_0000008660"
FT BINDING 284..312
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 344 AA; 36803 MW; 9F89DF4E769F5D10 CRC64;
MFKSLAAVLP RASKAKFLQK NYASTLAFIE SSKDGSVSRS SLSLLAAAQK LSNPITAVIT
GSKAEKTAEA LKSSYSCSNL EKLVIFEDSK LDTCLPEQLT PLLVKLLKGG DYSHFVVSNS
SVGKSVLPRV GALLDVQPVC EVTVIKDPKT FIRPIYAGNI ISTIECQAEK KLLIIRASAF
PPIAEGSMDS VTIEKRTDIP PCDLNVTWVK TILTKSERPE LTSAQNVVTG GRALKDKETF
EKLLSPLADV LHAAIGATRA SVDNGLCDNS LQIGQTGKVV APNLYIAIGV SGAVQHLAGM
KDSKVIVAIN NDPDAPIFNV ADYGLQGDLY KIVPELTEKL GKYK
//
