ETFA_PONAB
ID ETFA_PONAB Reviewed; 333 AA.
AC Q5RC31;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Electron transfer flavoprotein subunit alpha, mitochondrial;
DE Short=Alpha-ETF;
DE Flags: Precursor;
GN Name=ETFA;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P13804, ECO:0000250|UniProtKB:Q99LC5}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P13804}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR858451; CAH90679.1; -; mRNA.
DR RefSeq; NP_001125371.1; NM_001131899.2.
DR AlphaFoldDB; Q5RC31; -.
DR SMR; Q5RC31; -.
DR STRING; 9601.ENSPPYP00000007571; -.
DR PRIDE; Q5RC31; -.
DR GeneID; 100172274; -.
DR KEGG; pon:100172274; -.
DR CTD; 2108; -.
DR eggNOG; KOG3954; Eukaryota.
DR InParanoid; Q5RC31; -.
DR OrthoDB; 1128607at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; ISS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Electron transport; FAD; Flavoprotein; Mitochondrion;
KW Phosphoprotein; Reference proteome; 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_0000008653"
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 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"
SQ SEQUENCE 333 AA; 35166 MW; 831A6B1E162EB826 CRC64;
MFRAAAPGQL RRAASLLRFQ STLVIAEHAD DSLAPITLNT ITAATRLGGE VSCLVAGTKC
DKVAQDLCKV AGIAKVLVAQ HDVYRGLLPE ELTPLILATQ KQFNYTHICA GASAFGKNLL
PRVAAKLEVA PISDIIAIKS PDTFVRTIYA GNALCTVKCD EKVKVFSVRG TSFEAAATSG
GSASSEKASS TSPVEISEWL DQKLTKSDRP ELTGAKVVVS GGRGLKSGEN FKLLYDLADQ
RHAAVGASRA AVDAGFVPND MQVGQTGKIV APELYIAVGI SGAIQHLAGM KDSKTIVAIN
KDPEAPIFQV ADYGIVADLF KVVPEMTEIL KKK
