ETFD_RAT
ID ETFD_RAT Reviewed; 616 AA.
AC Q6UPE1;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial;
DE Short=ETF-QO;
DE Short=ETF-ubiquinone oxidoreductase;
DE EC=1.5.5.1;
DE AltName: Full=Electron-transferring-flavoprotein dehydrogenase;
DE Short=ETF dehydrogenase;
DE Flags: Precursor;
GN Name=Etfdh;
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 [MRNA], TRANSIT PEPTIDE CLEAVAGE SITE, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=Sprague-Dawley;
RX PubMed=16248429; DOI=10.1360/03yc0258;
RA Huang S., Song W., Lin Q.;
RT "cDNA cloning, functional expression and cellular localization of rat liver
RT mitochondrial electron-transfer flavoprotein-ubiquinone oxidoreductase
RT protein.";
RL Sci. China, Ser. C, Life Sci. 48:357-367(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550, AND IDENTIFICATION BY
RP 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: Accepts electrons from ETF and reduces ubiquinone.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + reduced [electron-transfer flavoprotein] = a
CC ubiquinol + H(+) + oxidized [electron-transfer flavoprotein];
CC Xref=Rhea:RHEA:24052, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307; EC=1.5.5.1;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16248429}.
CC -!- SIMILARITY: Belongs to the ETF-QO/FixC family. {ECO:0000305}.
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DR EMBL; AY365022; AAQ67364.1; -; mRNA.
DR AlphaFoldDB; Q6UPE1; -.
DR SMR; Q6UPE1; -.
DR STRING; 10116.ENSRNOP00000013262; -.
DR CarbonylDB; Q6UPE1; -.
DR iPTMnet; Q6UPE1; -.
DR jPOST; Q6UPE1; -.
DR PaxDb; Q6UPE1; -.
DR PRIDE; Q6UPE1; -.
DR UCSC; RGD:735052; rat.
DR RGD; 735052; Etfdh.
DR eggNOG; KOG2415; Eukaryota.
DR InParanoid; Q6UPE1; -.
DR PhylomeDB; Q6UPE1; -.
DR Reactome; R-RNO-611105; Respiratory electron transport.
DR PRO; PR:Q6UPE1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISO:RGD.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:RGD.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISO:RGD.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; ISO:RGD.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:RGD.
DR GO; GO:0048038; F:quinone binding; ISO:RGD.
DR GO; GO:0048039; F:ubiquinone binding; ISO:RGD.
DR GO; GO:0022900; P:electron transport chain; ISO:RGD.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR040156; ETF-QO.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR10617; PTHR10617; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Acetylation; Electron transport; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transit peptide; Transport; Ubiquinone.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:16248429"
FT CHAIN 33..616
FT /note="Electron transfer flavoprotein-ubiquinone
FT oxidoreductase, mitochondrial"
FT /id="PRO_0000008664"
FT INTRAMEM 108..129
FT /evidence="ECO:0000250"
FT INTRAMEM 427..446
FT /evidence="ECO:0000250"
FT DOMAIN 576..605
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 70..84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 304
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 560
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 585
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 588
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 591
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q921G7"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q921G7"
FT MOD_RES 222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q921G7"
FT MOD_RES 356
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q921G7"
FT MOD_RES 415
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q921G7"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 616 AA; 68198 MW; 30575E165673B679 CRC64;
MLVRLTKLSC PAYQWFHALK IKKCLPLCAP RCSSTSAVPQ ITTHYTIHPR EKDKRWEGVN
MERFAEEADV VIVGAGPAGL SAAIRLKQLA AEQEKDIRVC LVEKAAQIGA HTLSGACLDP
AAFKELFPDW KEKGAPLNTP VTEDRFAILT EKHRIPVPIL PGLPMNNHGN YIVRLGHLVS
WMGEQAEALG VEVYPGYAAA EVLYHEDGSV KGIATNDVGI QKDGAPKTTF ERGLELHAKV
TIFAEGCHGH LAKQFYKKFD LRASCDAQTY GIGLKELWVI DEKKWKPGRV DHTVGWPLDR
HTYGGSFLYH LNEGEPLVAV GFVVGLDYQN PYLSPFREFQ RWKHHPSIRP TLEGGKRIAY
GARALNEGGL QSIPKLTFPG GLLIGCSPGF MNVPKIKGTH TAMKSGSLAA EAIFKQLTSE
NLQSKTAGLH VTEYEDNLKQ SWVWKELHAV RNIRPSCHGI LGVYGGMIYT GIFYWILRGM
EPWTLKHKGS DSEQLKPAKD CTPIEYPKPD GQISFDLLSS VALSGTNHEH DQPAHLTLKD
DSIPVNRNLS IYDGPEQRFC PAGVYEFVPL EQGDGFRLQI NAQNCVHCKT CDIKDPSQNI
NWVVPEGGGG PAYNGM
