ETFB_RAT
ID ETFB_RAT Reviewed; 255 AA.
AC Q68FU3;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Electron transfer flavoprotein subunit beta {ECO:0000305};
DE Short=Beta-ETF {ECO:0000250|UniProtKB:P38117};
GN Name=Etfb {ECO:0000312|RGD:1303312};
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 [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 [2]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
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).
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. Required for
CC normal mitochondrial fatty acid oxidation and normal amino acid
CC metabolism. ETFB binds an AMP molecule that probably has a purely
CC structural role (By similarity). {ECO:0000250|UniProtKB:P38117,
CC ECO:0000269|PubMed:7334008}.
CC -!- SUBUNIT: Heterodimer composed of ETFA and ETFB (PubMed:7334008).
CC Identified in a complex that contains ETFA, ETFB and ETFRF1. Interacts
CC with ACADM (By similarity). {ECO:0000250|UniProtKB:P38117,
CC ECO:0000269|PubMed:7334008}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000305|PubMed:7334008}.
CC -!- DOMAIN: The recognition loop recognizes a hydrophobic patch at the
CC surface of interacting dehydrogenases and acts as a static anchor at
CC the interface. {ECO:0000250|UniProtKB:P38117}.
CC -!- PTM: Methylated. Trimethylation at Lys-200 and Lys-203 may negatively
CC regulate the activity in electron transfer from acyl-CoA
CC dehydrogenases. {ECO:0000250|UniProtKB:P38117}.
CC -!- SIMILARITY: Belongs to the ETF beta-subunit/FixA family. {ECO:0000305}.
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DR EMBL; BC079351; AAH79351.1; -; mRNA.
DR RefSeq; NP_001004220.1; NM_001004220.1.
DR AlphaFoldDB; Q68FU3; -.
DR SMR; Q68FU3; -.
DR BioGRID; 253995; 2.
DR STRING; 10116.ENSRNOP00000024083; -.
DR iPTMnet; Q68FU3; -.
DR PhosphoSitePlus; Q68FU3; -.
DR jPOST; Q68FU3; -.
DR PaxDb; Q68FU3; -.
DR PRIDE; Q68FU3; -.
DR Ensembl; ENSRNOT00000024083; ENSRNOP00000024083; ENSRNOG00000017851.
DR GeneID; 292845; -.
DR KEGG; rno:292845; -.
DR UCSC; RGD:1303312; rat.
DR CTD; 2109; -.
DR RGD; 1303312; Etfb.
DR eggNOG; KOG3180; Eukaryota.
DR GeneTree; ENSGT00390000009936; -.
DR HOGENOM; CLU_060196_0_0_1; -.
DR InParanoid; Q68FU3; -.
DR OMA; YNGGMVP; -.
DR OrthoDB; 1092876at2759; -.
DR PhylomeDB; Q68FU3; -.
DR TreeFam; TF314039; -.
DR Reactome; R-RNO-611105; Respiratory electron transport.
DR Reactome; R-RNO-8876725; Protein methylation.
DR PRO; PR:Q68FU3; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017851; Expressed in heart and 20 other tissues.
DR Genevisible; Q68FU3; RN.
DR GO; GO:0045251; C:electron transfer flavoprotein complex; ISO:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; cd01714; ETF_beta; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR000049; ET-Flavoprotein_bsu_CS.
DR InterPro; IPR014730; ETF_a/b_N.
DR InterPro; IPR012255; ETF_b.
DR InterPro; IPR033948; ETF_beta_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR21294; PTHR21294; 1.
DR Pfam; PF01012; ETF; 1.
DR PIRSF; PIRSF000090; Beta-ETF; 1.
DR SMART; SM00893; ETF; 1.
DR PROSITE; PS01065; ETF_BETA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Electron transport; Methylation; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q2TBV3"
FT CHAIN 2..255
FT /note="Electron transfer flavoprotein subunit beta"
FT /id="PRO_0000231526"
FT REGION 183..205
FT /note="Recognition loop"
FT /evidence="ECO:0000250|UniProtKB:P38117"
FT BINDING 9
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P38117"
FT BINDING 39..42
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P38117"
FT BINDING 66
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P38117"
FT BINDING 123..134
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P38117"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q2TBV3"
FT MOD_RES 200
FT /note="N6,N6,N6-trimethyllysine; by ETFBKMT; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q2TBV3"
FT MOD_RES 200
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCW4"
FT MOD_RES 200
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38117"
FT MOD_RES 203
FT /note="N6,N6,N6-trimethyllysine; by ETFBKMT"
FT /evidence="ECO:0000250|UniProtKB:Q2TBV3"
FT MOD_RES 210
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCW4"
FT MOD_RES 210
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCW4"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38117"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38117"
FT MOD_RES 238
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCW4"
FT MOD_RES 248
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCW4"
FT MOD_RES 248
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCW4"
SQ SEQUENCE 255 AA; 27687 MW; 3D916689B2CB6FAB CRC64;
MAELRALVAV KRVIDFAVKI RVKPDKSGVV TDGVKHSMNP FCEIAVEEAV RLKEKKLVKE
IIAVSCGPPQ CQETIRTALA MGADRGIHVE VPGAEAENLG PLQVARVLAK LAEKEKVDLL
FLGKQAIDDD CNQTGQMTAG LLDWPQGTFA SQVTLEGDKV KVEREIDGGL ETIRLKLPAV
VTADLRLNEP RYATLPNIMK AKKKKIEVIK AGDLGVDLTS KVSVISVEEP PQRLAGVKVE
TTEDLVAKLK EVGRI
