ID   ETFB_PIG                Reviewed;         255 AA.
AC   Q6UAQ8;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 99.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Mohsen A.-W.A., Hoard H., Daniels J.K., Anderson B.D., Willard J.M.A.,
RA   Keller D.M., Vockley J.;
RT   "Cloning of cDNAs encoding the mature form of porcine electron transfer
RT   flavoprotein alpha and beta subunits.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=6847633; DOI=10.1042/bj2090541;
RA   Husain M., Steenkamp D.J.;
RT   "Electron transfer flavoprotein from pig liver mitochondria. A simple
RT   purification and re-evaluation of some of the molecular properties.";
RL   Biochem. J. 209:541-545(1983).
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 (PubMed:6847633).
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:6847633}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000305|PubMed:6847633}.
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; AY374470; AAQ84565.1; -; mRNA.
DR   RefSeq; NP_001192208.1; NM_001205279.1.
DR   AlphaFoldDB; Q6UAQ8; -.
DR   SMR; Q6UAQ8; -.
DR   STRING; 9823.ENSSSCP00000003505; -.
DR   PeptideAtlas; Q6UAQ8; -.
DR   PRIDE; Q6UAQ8; -.
DR   Ensembl; ENSSSCT00000003588; ENSSSCP00000003505; ENSSSCG00000003229.
DR   Ensembl; ENSSSCT00005004209; ENSSSCP00005002494; ENSSSCG00005002746.
DR   Ensembl; ENSSSCT00015032774; ENSSSCP00015013004; ENSSSCG00015024715.
DR   Ensembl; ENSSSCT00025036328; ENSSSCP00025015187; ENSSSCG00025026830.
DR   Ensembl; ENSSSCT00030000167; ENSSSCP00030000143; ENSSSCG00030000084.
DR   Ensembl; ENSSSCT00035072688; ENSSSCP00035029488; ENSSSCG00035054483.
DR   Ensembl; ENSSSCT00040029520; ENSSSCP00040012348; ENSSSCG00040022011.
DR   Ensembl; ENSSSCT00045014580; ENSSSCP00045010115; ENSSSCG00045008640.
DR   Ensembl; ENSSSCT00050070941; ENSSSCP00050030498; ENSSSCG00050052088.
DR   Ensembl; ENSSSCT00055011322; ENSSSCP00055008945; ENSSSCG00055005814.
DR   Ensembl; ENSSSCT00060024382; ENSSSCP00060010243; ENSSSCG00060018172.
DR   Ensembl; ENSSSCT00065107826; ENSSSCP00065048094; ENSSSCG00065077928.
DR   Ensembl; ENSSSCT00070050545; ENSSSCP00070042720; ENSSSCG00070025281.
DR   GeneID; 396614; -.
DR   KEGG; ssc:396614; -.
DR   CTD; 2109; -.
DR   VGNC; VGNC:87802; ETFB.
DR   eggNOG; KOG3180; Eukaryota.
DR   GeneTree; ENSGT00390000009936; -.
DR   HOGENOM; CLU_060196_0_0_1; -.
DR   InParanoid; Q6UAQ8; -.
DR   OMA; YNGGMVP; -.
DR   OrthoDB; 1092876at2759; -.
DR   TreeFam; TF314039; -.
DR   Reactome; R-SSC-611105; Respiratory electron transport.
DR   Reactome; R-SSC-8876725; Protein methylation.
DR   Proteomes; UP000008227; Chromosome 6.
DR   Proteomes; UP000314985; Unassembled WGS sequence.
DR   Bgee; ENSSSCG00000003229; Expressed in psoas major muscle and 47 other tissues.
DR   ExpressionAtlas; Q6UAQ8; baseline.
DR   Genevisible; Q6UAQ8; SS.
DR   GO; GO:0045251; C:electron transfer flavoprotein complex; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISS:UniProtKB.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:Ensembl.
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_0000231525"
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;  27764 MW;  30C3786463FB5AB0 CRC64;
     MAELRALVAV KRVIDFAVKI RVKPDRTGVV MDGVKHSMNP FCEIAVEEAV RLKEKKLVKE
     VIAVSCGPAQ CQETIRTALA MGADRGIHVE VPAAEAHHLG PLQVARVLAK LAQKEKVDLV
     LLGKQAIDDD CNQTGQMTAG FLDWPQGTFA SQVTLEGDKV KVEREIDGGL ETLRLKLPAV
     VTADLRLNEP RYATLPNIMK AKKKKIEVIK AGDLGVDLTS KLSVVSVEDP PQRVAGVKVE
     TTEDLVAKLR EIGRI