ETFB_ARATH
ID ETFB_ARATH Reviewed; 251 AA.
AC Q9LSW8; A8MRD3; Q2V317; Q8LFE0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Electron transfer flavoprotein subunit beta, mitochondrial;
DE Short=Beta-ETF;
DE Flags: Precursor;
GN Name=ETFB; OrderedLocusNames=At5g43430; ORFNames=MWF20.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [6]
RP FUNCTION, INDUCTION, INTERACTION WITH ETFA, AND DISRUPTION PHENOTYPE.
RX PubMed=16923016; DOI=10.1111/j.1365-313x.2006.02826.x;
RA Ishizaki K., Schauer N., Larson T.R., Graham I.A., Fernie A.R.,
RA Leaver C.J.;
RT "The mitochondrial electron transfer flavoprotein complex is essential for
RT survival of Arabidopsis in extended darkness.";
RL Plant J. 47:751-760(2006).
CC -!- FUNCTION: The electron transfer flavoprotein serves as a specific
CC electron acceptor for several dehydrogenases, including five 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 (ETF dehydrogenase) (By similarity). Involved
CC in leucine catabolism and in phytol degradation. {ECO:0000250,
CC ECO:0000269|PubMed:16923016}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per dimer. {ECO:0000250};
CC -!- COFACTOR:
CC Name=AMP; Xref=ChEBI:CHEBI:456215; Evidence={ECO:0000250};
CC Note=Binds 1 AMP per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14671022}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9LSW8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LSW8-2; Sequence=VSP_032174, VSP_032175;
CC Name=3;
CC IsoId=Q9LSW8-3; Sequence=VSP_032173;
CC -!- INDUCTION: Expressed constitutively. Not induced by dark treatment or
CC sucrose starvation. {ECO:0000269|PubMed:16923016}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant viability on extended exposure to
CC darkness and a reduced reproductive performance under normal growth
CC conditions. {ECO:0000269|PubMed:16923016}.
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; AB025638; BAA97422.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94960.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94961.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94962.1; -; Genomic_DNA.
DR EMBL; AY045657; AAK74015.1; -; mRNA.
DR EMBL; AF446867; AAL38600.1; -; mRNA.
DR EMBL; AY084901; AAM61464.1; -; mRNA.
DR RefSeq; NP_001032002.1; NM_001036925.2. [Q9LSW8-2]
DR RefSeq; NP_001078699.1; NM_001085230.2. [Q9LSW8-3]
DR RefSeq; NP_199156.1; NM_123709.4. [Q9LSW8-1]
DR AlphaFoldDB; Q9LSW8; -.
DR SMR; Q9LSW8; -.
DR BioGRID; 19613; 1.
DR IntAct; Q9LSW8; 1.
DR STRING; 3702.AT5G43430.1; -.
DR iPTMnet; Q9LSW8; -.
DR PaxDb; Q9LSW8; -.
DR PRIDE; Q9LSW8; -.
DR ProteomicsDB; 220595; -. [Q9LSW8-1]
DR EnsemblPlants; AT5G43430.1; AT5G43430.1; AT5G43430. [Q9LSW8-1]
DR EnsemblPlants; AT5G43430.2; AT5G43430.2; AT5G43430. [Q9LSW8-2]
DR EnsemblPlants; AT5G43430.3; AT5G43430.3; AT5G43430. [Q9LSW8-3]
DR GeneID; 834363; -.
DR Gramene; AT5G43430.1; AT5G43430.1; AT5G43430. [Q9LSW8-1]
DR Gramene; AT5G43430.2; AT5G43430.2; AT5G43430. [Q9LSW8-2]
DR Gramene; AT5G43430.3; AT5G43430.3; AT5G43430. [Q9LSW8-3]
DR KEGG; ath:AT5G43430; -.
DR Araport; AT5G43430; -.
DR TAIR; locus:2176446; AT5G43430.
DR eggNOG; KOG3180; Eukaryota.
DR HOGENOM; CLU_060196_0_0_1; -.
DR InParanoid; Q9LSW8; -.
DR OMA; YNGGMVP; -.
DR PhylomeDB; Q9LSW8; -.
DR PRO; PR:Q9LSW8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LSW8; baseline and differential.
DR Genevisible; Q9LSW8; AT.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0015996; P:chlorophyll catabolic process; IMP:TAIR.
DR GO; GO:0006552; P:leucine catabolic process; IMP:TAIR.
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 Alternative splicing; Electron transport; FAD; Flavoprotein; Mitochondrion;
KW Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..251
FT /note="Electron transfer flavoprotein subunit beta,
FT mitochondrial"
FT /id="PRO_0000324180"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_032173"
FT VAR_SEQ 178
FT /note="T -> S (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032174"
FT VAR_SEQ 179..251
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032175"
FT CONFLICT 91
FT /note="I -> S (in Ref. 4; AAM61464)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 251 AA; 27400 MW; 5C5B8146CA02AF7F CRC64;
MKILVAVKRV VDYAVKIRVK PDKTGVETQN VKMSMNPFCE IALEEALRIK EAGFAKEVIA
VSIGPSQCVD TLRTGLAMGA DRGIHVETNS IFLPLTIAKI LKSLADVENP GLIFLGKQAI
DDDCNQTGQM VAALLGWPQA TFASKVVLDK DKNVATVDRE VDGGLETLNV DLPAVITTDL
RLNQPRYASL PNIMKAKSKP IKKMTVQDLK VDIKSDIEIL EVTEPPKRKS GVMVSSVDEL
IDKLKNEAHV V
