ETFA_MOUSE
ID ETFA_MOUSE Reviewed; 333 AA.
AC Q99LC5; Q3THD7; Q3V000; Q4V9X5; Q8BMD3; Q8BMU7;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Electron transfer flavoprotein subunit alpha, mitochondrial;
DE Short=Alpha-ETF;
DE Flags: Precursor;
GN Name=Etfa;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J;
RC TISSUE=Ovary, Placenta, Small intestine, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 86-117 AND 233-249, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-69, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-59; LYS-69; LYS-85; LYS-158; LYS-187; LYS-203; LYS-216;
RP LYS-226; LYS-232 AND LYS-301, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-62; LYS-69; LYS-75;
RP LYS-85; LYS-101; LYS-139; LYS-158; LYS-164; LYS-203; LYS-226 AND LYS-232,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [7]
RP INTERACTION WITH TASOR, AND TISSUE SPECIFICITY.
RX PubMed=31112734; DOI=10.1016/j.yexcr.2019.05.018;
RA Gresakova V., Novosadova V., Prochazkova M., Bhargava S., Jenickova I.,
RA Prochazka J., Sedlacek R.;
RT "Fam208a orchestrates interaction protein network essential for early
RT embryonic development and cell division.";
RL Exp. Cell Res. 382:111437-111437(2019).
CC -!- FUNCTION: Heterodimeric electron transfer flavoprotein that accepts
CC electrons from several mitochondrial dehydrogenases, including 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). Required for normal
CC mitochondrial fatty acid oxidation and normal amino acid metabolism.
CC {ECO:0000250|UniProtKB:P13804}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P13804};
CC Note=Binds 1 FAD per dimer. {ECO:0000250|UniProtKB:P13804};
CC -!- SUBUNIT: Heterodimer composed of ETFA and ETFB. Identified in a complex
CC that contains ETFA, ETFB and ETFRF1. Interaction with ETFRF1 promotes
CC dissociation of the bound FAD and loss of electron transfer activity
CC (By similarity). Interacts with TASOR (PubMed:31112734).
CC {ECO:0000250|UniProtKB:P13804, ECO:0000269|PubMed:31112734}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P13804}.
CC -!- TISSUE SPECIFICITY: Expressed in the spermatogonia, spermatocytes,
CC ovary and granular cells within the cerebellum.
CC {ECO:0000269|PubMed:31112734}.
CC -!- DOMAIN: Domain I shares an identical polypeptide fold with the beta
CC subunit ETFB though there is no sequence similarity.
CC {ECO:0000250|UniProtKB:P13804}.
CC -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC {ECO:0000305}.
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DR EMBL; AK028118; BAC25758.1; -; mRNA.
DR EMBL; AK032830; BAC28046.1; -; mRNA.
DR EMBL; AK133525; BAE21705.1; -; mRNA.
DR EMBL; AK167572; BAE39635.1; -; mRNA.
DR EMBL; AK168321; BAE40260.1; -; mRNA.
DR EMBL; BC003432; AAH03432.1; -; mRNA.
DR EMBL; BC096645; AAH96645.1; -; mRNA.
DR CCDS; CCDS23204.1; -.
DR RefSeq; NP_663590.3; NM_145615.4.
DR AlphaFoldDB; Q99LC5; -.
DR SMR; Q99LC5; -.
DR BioGRID; 225952; 25.
DR ComplexPortal; CPX-865; Electron transfer flavoprotein complex.
DR IntAct; Q99LC5; 6.
DR MINT; Q99LC5; -.
DR STRING; 10090.ENSMUSP00000034866; -.
DR iPTMnet; Q99LC5; -.
DR PhosphoSitePlus; Q99LC5; -.
DR SwissPalm; Q99LC5; -.
DR REPRODUCTION-2DPAGE; Q99LC5; -.
DR UCD-2DPAGE; Q99LC5; -.
DR EPD; Q99LC5; -.
DR jPOST; Q99LC5; -.
DR MaxQB; Q99LC5; -.
DR PaxDb; Q99LC5; -.
DR PeptideAtlas; Q99LC5; -.
DR PRIDE; Q99LC5; -.
DR ProteomicsDB; 275786; -.
DR Antibodypedia; 14895; 375 antibodies from 33 providers.
DR Ensembl; ENSMUST00000034866; ENSMUSP00000034866; ENSMUSG00000032314.
DR GeneID; 110842; -.
DR KEGG; mmu:110842; -.
DR UCSC; uc009psl.2; mouse.
DR CTD; 2108; -.
DR MGI; MGI:106092; Etfa.
DR VEuPathDB; HostDB:ENSMUSG00000032314; -.
DR eggNOG; KOG3954; Eukaryota.
DR GeneTree; ENSGT00390000013422; -.
DR HOGENOM; CLU_034178_0_1_1; -.
DR InParanoid; Q99LC5; -.
DR OMA; WRPYAEQ; -.
DR OrthoDB; 1128607at2759; -.
DR PhylomeDB; Q99LC5; -.
DR TreeFam; TF105763; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR BioGRID-ORCS; 110842; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Etfa; mouse.
DR PRO; PR:Q99LC5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q99LC5; protein.
DR Bgee; ENSMUSG00000032314; Expressed in cardiac muscle tissue and 266 other tissues.
DR Genevisible; Q99LC5; MM.
DR GO; GO:0045251; C:electron transfer flavoprotein complex; ISO:MGI.
DR GO; GO:0017133; C:mitochondrial electron transfer flavoprotein complex; TAS:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0009055; F:electron transfer activity; ISS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:MGI.
DR GO; GO:0009063; P:cellular amino acid catabolic process; ISO:MGI.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISS:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; ISO:MGI.
DR CDD; cd01715; ETF_alpha; 1.
DR Gene3D; 3.40.50.620; -; 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; PTHR43153; 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; SSF52467; SSF52467; 1.
DR PROSITE; PS00696; ETF_ALPHA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Electron transport; FAD;
KW Flavoprotein; Mitochondrion; Phosphoprotein; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 20..333
FT /note="Electron transfer flavoprotein subunit alpha,
FT mitochondrial"
FT /id="PRO_0000008652"
FT REGION 20..204
FT /note="Domain I"
FT /evidence="ECO:0000250|UniProtKB:P13804"
FT REGION 205..333
FT /note="Domain II"
FT /evidence="ECO:0000250|UniProtKB:P13804"
FT BINDING 223
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P13804"
FT BINDING 248
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P13804"
FT BINDING 263..266
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P13804"
FT BINDING 281..286
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P13804"
FT BINDING 300
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P13804"
FT BINDING 318..319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P13804"
FT MOD_RES 59
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 59
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 62
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 69
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 69
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 85
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 85
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 93
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 101
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13804"
FT MOD_RES 158
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 158
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 164
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 187
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 203
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 203
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 216
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 226
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 226
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 232
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 232
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 301
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 20
FT /note="Q -> R (in Ref. 1; BAE40260)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="K -> E (in Ref. 1; BAE21705)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="R -> P (in Ref. 1; BAC25758)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="A -> T (in Ref. 2; AAH03432)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="I -> V (in Ref. 1; BAC28046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 35009 MW; 635F34ADCDA254C0 CRC64;
MFRAAAPGQL RRAASLLRFQ STLVIAEHAN DSLAPITLNT ITAAGRLGGE VSCLVAGTKC
DKVVQDLCKV AGVAKVLVAQ HDAYKGLLPE ELTPLILETQ KQFSYTHICA GASAFGKNLL
PRVAAKLNVA PVSDIIEIKS PDTFVRTIYA GNALCTVKCD EKVKVFSVRG TSFEAAATSG
GSASSEKAPS SSSVGISEWL DQKLTKSDRP ELTGAKVVVS GGRGLKSGEN FKLLYDLADQ
LHAAVGASRA AVDAGFVPND MQVGQTGKIV APELYIAVGI SGAIQHLAGM KDSKTIVAIN
KDPEAPIFQV ADYGIVADLF KVVPEMTEIL KKK
