ETFB_BOVIN
ID ETFB_BOVIN Reviewed; 255 AA.
AC Q2TBV3;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Electron transfer flavoprotein subunit beta {ECO:0000305};
DE Short=Beta-ETF {ECO:0000250|UniProtKB:P38117};
GN Name=ETFB {ECO:0000250|UniProtKB:P38117};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-14, SUBCELLULAR LOCATION, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND METHYLATION AT LYS-200 AND LYS-203.
RX PubMed=25023281; DOI=10.1074/jbc.m114.580464;
RA Rhein V.F., Carroll J., He J., Ding S., Fearnley I.M., Walker J.E.;
RT "Human METTL20 methylates lysine residues adjacent to the recognition loop
RT of the electron transfer flavoprotein in mitochondria.";
RL J. Biol. Chem. 289:24640-24651(2014).
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. Required for normal mitochondrial fatty acid
CC oxidation and normal amino acid metabolism. ETFB binds an AMP molecule
CC that probably has a purely structural role.
CC {ECO:0000250|UniProtKB:P38117}.
CC -!- SUBUNIT: Heterodimer composed of ETFA and ETFB. Identified in a complex
CC that contains ETFA, ETFB and ETFRF1. Interacts with ACADM.
CC {ECO:0000250|UniProtKB:P38117}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000305|PubMed:25023281}.
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 (PubMed:25023281). Trimethylation at Lys-200 and Lys-
CC 203 may negatively regulate the activity in electron transfer from
CC acyl-CoA dehydrogenases. {ECO:0000250|UniProtKB:P38117,
CC ECO:0000269|PubMed:25023281}.
CC -!- SIMILARITY: Belongs to the ETF beta-subunit/FixA family. {ECO:0000305}.
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DR EMBL; BC109603; AAI09604.1; -; mRNA.
DR RefSeq; NP_001033671.1; NM_001038582.1.
DR AlphaFoldDB; Q2TBV3; -.
DR SMR; Q2TBV3; -.
DR STRING; 9913.ENSBTAP00000027250; -.
DR iPTMnet; Q2TBV3; -.
DR PaxDb; Q2TBV3; -.
DR PeptideAtlas; Q2TBV3; -.
DR PRIDE; Q2TBV3; -.
DR GeneID; 617210; -.
DR KEGG; bta:617210; -.
DR CTD; 2109; -.
DR eggNOG; KOG3180; Eukaryota.
DR HOGENOM; CLU_060196_0_0_1; -.
DR InParanoid; Q2TBV3; -.
DR OrthoDB; 1092876at2759; -.
DR TreeFam; TF314039; -.
DR Proteomes; UP000009136; Unplaced.
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:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISS:UniProtKB.
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; Direct protein sequencing; Electron transport; Methylation;
KW Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25023281"
FT CHAIN 2..255
FT /note="Electron transfer flavoprotein subunit beta"
FT /id="PRO_0000231524"
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:0000269|PubMed:25023281"
FT MOD_RES 200
FT /note="N6,N6,N6-trimethyllysine; by ETFBKMT; alternate"
FT /evidence="ECO:0000269|PubMed:25023281"
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:0000269|PubMed:25023281"
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; 27699 MW; 0B96D6893DEF3C6A CRC64;
MAELRALVAV KRVIDFAVKI RVKPDKTGVV TDGVKHSMNP FCEIAVEEAV RLKEKKLVKE
IIAVSCGPAQ CQETIRTALA MGADRGIHVE VPAAEANHLG PLQVARVLAK LAEKEKVDLV
LLGKQAIDDD CNQTGQMTAG FLDWPQGTFA SQVTLEGDKI KVEREIDGGL ETLRLKLPAV
VTADLRLNEP RYATLPNIMK AKKKKIEVIK AGDLGVDLTS KLSVISVEDP PQRTAGVKVE
TTEDLVAKLK EIGRI
