ETFB_MOUSE
ID ETFB_MOUSE Reviewed; 255 AA.
AC Q9DCW4; Q810V3;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Electron transfer flavoprotein subunit beta {ECO:0000305};
DE Short=Beta-ETF {ECO:0000250|UniProtKB:P38117};
GN Name=Etfb {ECO:0000312|MGI:MGI:106098};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Macrophage;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Kidney, and Mammary tumor;
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 [3]
RP PROTEIN SEQUENCE OF 2-10 AND 210-220, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RA Kanor S., Quadroni M., Bienvenut W.V.;
RL Submitted (MAR-2006) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 77-106 AND 239-248, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-210 AND LYS-248, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-200; LYS-210; LYS-238 AND
RP LYS-248, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [8]
RP FUNCTION, 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 (By similarity). Required for normal
CC mitochondrial fatty acid oxidation and normal amino acid metabolism
CC (PubMed:25023281). ETFB binds an AMP molecule that probably has a
CC purely structural role (By similarity). {ECO:0000250|UniProtKB:P38117,
CC ECO:0000269|PubMed:25023281}.
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:0000250|UniProtKB:P38117}.
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; AK002407; BAB22076.1; -; mRNA.
DR EMBL; AK150293; BAE29447.1; -; mRNA.
DR EMBL; BC069877; AAH69877.1; -; mRNA.
DR EMBL; BC049237; AAH49237.1; -; mRNA.
DR CCDS; CCDS21171.1; -.
DR RefSeq; NP_080971.2; NM_026695.3.
DR AlphaFoldDB; Q9DCW4; -.
DR SMR; Q9DCW4; -.
DR BioGRID; 225938; 30.
DR ComplexPortal; CPX-865; Electron transfer flavoprotein complex.
DR IntAct; Q9DCW4; 5.
DR MINT; Q9DCW4; -.
DR STRING; 10090.ENSMUSP00000004729; -.
DR iPTMnet; Q9DCW4; -.
DR PhosphoSitePlus; Q9DCW4; -.
DR SwissPalm; Q9DCW4; -.
DR REPRODUCTION-2DPAGE; Q9DCW4; -.
DR CPTAC; non-CPTAC-3801; -.
DR EPD; Q9DCW4; -.
DR jPOST; Q9DCW4; -.
DR MaxQB; Q9DCW4; -.
DR PaxDb; Q9DCW4; -.
DR PeptideAtlas; Q9DCW4; -.
DR PRIDE; Q9DCW4; -.
DR ProteomicsDB; 275895; -.
DR TopDownProteomics; Q9DCW4; -.
DR Ensembl; ENSMUST00000004729; ENSMUSP00000004729; ENSMUSG00000004610.
DR GeneID; 110826; -.
DR KEGG; mmu:110826; -.
DR UCSC; uc009gmt.2; mouse.
DR CTD; 2109; -.
DR MGI; MGI:106098; Etfb.
DR VEuPathDB; HostDB:ENSMUSG00000004610; -.
DR eggNOG; KOG3180; Eukaryota.
DR GeneTree; ENSGT00390000009936; -.
DR HOGENOM; CLU_060196_0_0_1; -.
DR InParanoid; Q9DCW4; -.
DR OMA; YNGGMVP; -.
DR OrthoDB; 1092876at2759; -.
DR PhylomeDB; Q9DCW4; -.
DR TreeFam; TF314039; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-8876725; Protein methylation.
DR BioGRID-ORCS; 110826; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Etfb; mouse.
DR PRO; PR:Q9DCW4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DCW4; protein.
DR Bgee; ENSMUSG00000004610; Expressed in proximal tubule and 75 other tissues.
DR ExpressionAtlas; Q9DCW4; baseline and differential.
DR Genevisible; Q9DCW4; MM.
DR GO; GO:0045251; C:electron transfer flavoprotein complex; ISO:MGI.
DR GO; GO:0017133; C:mitochondrial electron transfer flavoprotein complex; TAS:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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:MGI.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IMP:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; ISO:MGI.
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|Ref.3"
FT CHAIN 2..255
FT /note="Electron transfer flavoprotein subunit beta"
FT /id="PRO_0000167871"
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|Ref.3"
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:0007744|PubMed:23576753"
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:0007744|PubMed:23576753"
FT MOD_RES 210
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
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:0007744|PubMed:23576753"
FT MOD_RES 248
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 248
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 2..4
FT /note="Missing (in Ref. 1; BAB22076)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 27623 MW; 89E7100B327822FF CRC64;
MAELRALVAV KRVIDFAVKI RVKPDKSGVV TDGVKHSMNP FCEIAVEEAV RLKEKKLVKE
IIAVSCGPSQ CQETIRTALA MGADRGIHVE IPGAQAESLG PLQVARVLAK LAEKEKVDLL
FLGKQAIDDD CNQTGQMTAG LLDWPQGTFA SQVTLEGDKV KVEREIDGGL ETLRLKLPAV
VTADLRLNEP RYATLPNIMK AKKKKIEVVK AGDLGVDLTS KVSVISVEEP PQRSAGVKVE
TTEDLVAKLK EVGRI
