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 27-MAR-2024, entry version 123. 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}. 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; 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 GlyGen; Q68FU3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q68FU3; -. DR PhosphoSitePlus; Q68FU3; -. DR jPOST; Q68FU3; -. DR PaxDb; 10116-ENSRNOP00000024083; -. DR Ensembl; ENSRNOT00000024083.6; ENSRNOP00000024083.3; ENSRNOG00000017851.6. DR Ensembl; ENSRNOT00055009110; ENSRNOP00055006953; ENSRNOG00055005654. DR Ensembl; ENSRNOT00060018335; ENSRNOP00060014293; ENSRNOG00060010826. DR Ensembl; ENSRNOT00065049449; ENSRNOP00065040573; ENSRNOG00065028670. DR GeneID; 292845; -. DR KEGG; rno:292845; -. DR UCSC; RGD:1303312; rat. DR AGR; RGD:1303312; -. 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; EINQPRI; -. DR OrthoDB; 5476365at2759; -. 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 cell types or tissues. DR GO; GO:0045251; C:electron transfer flavoprotein complex; ISO:RGD. DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. 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: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; HUPs; 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; ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT; 1. DR PANTHER; PTHR21294:SF8; ELECTRON TRANSFER FLAVOPROTEIN SUBUNIT BETA; 1. DR Pfam; PF01012; ETF; 1. DR PIRSF; PIRSF000090; Beta-ETF; 1. DR SMART; SM00893; ETF; 1. DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1. DR PROSITE; PS01065; ETF_BETA; 1. DR Genevisible; Q68FU3; RN. 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 //