ETFA_RAT
ID ETFA_RAT Reviewed; 333 AA.
AC P13803; Q5M7W0;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 4.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=3415685; DOI=10.1016/s0006-291x(88)81084-2;
RA Shinzawa K., Inagaki T., Ohishi N., Ichihara C., Tsukagoshi N., Udaka S.,
RA Yagi K.;
RT "Molecular cloning of a cDNA for alpha-subunit of rat liver electron
RT transfer flavoprotein.";
RL Biochem. Biophys. Res. Commun. 155:300-304(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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; 127-139 AND 233-249, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=7334008; DOI=10.1093/oxfordjournals.jbchem.a133651;
RA Furuta S., Miyazawa S., Hashimoto T.;
RT "Purification and properties of rat liver acyl-CoA dehydrogenases and
RT electron transfer flavoprotein.";
RL J. Biochem. 90:1739-1750(1981).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Heterodimeric electron transfer flavoprotein that accepts
CC electrons from several mitochondrial dehydrogenases, including acyl-CoA
CC dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase
CC (PubMed:7334008). It transfers the electrons to the main mitochondrial
CC respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase)
CC (Probable). Required for normal mitochondrial fatty acid oxidation and
CC normal amino acid metabolism. {ECO:0000250|UniProtKB:P13804,
CC ECO:0000269|PubMed:7334008, ECO:0000305}.
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(PubMed:7334008).
CC Identified in a complex that contains ETFA, ETFB and ETFRF1.
CC Interaction with ETFRF1 promotes dissociation of the bound FAD and loss
CC of electron transfer activity (By similarity). Interacts with TASOR (By
CC similarity). {ECO:0000250|UniProtKB:P13804,
CC ECO:0000250|UniProtKB:Q99LC5, ECO:0000269|PubMed:7334008}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000305|PubMed:7334008}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA41130.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M22030; AAA41130.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BC088412; AAH88412.1; -; mRNA.
DR PIR; A31568; A31568.
DR RefSeq; NP_001009668.1; NM_001009668.1.
DR AlphaFoldDB; P13803; -.
DR SMR; P13803; -.
DR BioGRID; 256687; 1.
DR IntAct; P13803; 1.
DR STRING; 10116.ENSRNOP00000020544; -.
DR iPTMnet; P13803; -.
DR PhosphoSitePlus; P13803; -.
DR jPOST; P13803; -.
DR PaxDb; P13803; -.
DR PRIDE; P13803; -.
DR GeneID; 300726; -.
DR KEGG; rno:300726; -.
DR UCSC; RGD:628747; rat.
DR CTD; 2108; -.
DR RGD; 628747; Etfa.
DR VEuPathDB; HostDB:ENSRNOG00000015233; -.
DR eggNOG; KOG3954; Eukaryota.
DR HOGENOM; CLU_034178_0_1_1; -.
DR InParanoid; P13803; -.
DR OMA; WRPYAEQ; -.
DR OrthoDB; 1128607at2759; -.
DR PhylomeDB; P13803; -.
DR TreeFam; TF105763; -.
DR Reactome; R-RNO-611105; Respiratory electron transport.
DR PRO; PR:P13803; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000015233; Expressed in heart and 19 other tissues.
DR Genevisible; P13803; RN.
DR GO; GO:0045251; C:electron transfer flavoprotein complex; ISO:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; ISS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISO:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:RGD.
DR GO; GO:0009063; P:cellular amino acid catabolic process; ISO:RGD.
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:RGD.
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_0000008654"
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:0000250|UniProtKB:Q99LC5"
FT MOD_RES 59
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 62
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 69
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 69
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 85
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 85
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 93
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 101
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
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:0000250|UniProtKB:Q99LC5"
FT MOD_RES 158
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 164
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 187
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 203
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 203
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 216
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 226
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 226
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 232
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 232
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT MOD_RES 301
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LC5"
FT CONFLICT 109
FT /note="C -> V (in Ref. 1; AAA41130)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="G -> A (in Ref. 1; AAA41130)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="L -> Q (in Ref. 1; AAA41130)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 34951 MW; 635A3525666AFE85 CRC64;
MFRAAAPGQL RRAASLLRFQ STLVIAEHAN DSLAPITLNT ITAAGRLGGE VSCLVAGTKC
DKVVQDLCKV AGVAKVLVAQ HDAYKGLLPE ELTPLILETQ KQFSYTHICA GASAFGKNLL
PRVAAKLNVA PVSDIIEIKS PDTFVRTIYA GNALCTVKCD EKVKVFSVRG TSFEAAAASG
GSASSEKAPS SSSAGISEWL DQKLTKSDRP ELTGAKVVVS GGRGLKSGEN FKLLYDLADQ
LHAAVGASRA AVDAGFVPND MQVGQTGKIV APELYIAVGI SGAIQHLAGM KDSKTIVAIN
KDPEAPIFQV ADYGIVADLF KVVPEMTEIL KKK
