LOCUS       NP_001009668             333 aa            linear   ROD 02-JUN-2024
DEFINITION  electron transfer flavoprotein subunit alpha, mitochondrial [Rattus
            norvegicus].
ACCESSION   NP_001009668 XP_217155
VERSION     NP_001009668.1
DBSOURCE    REFSEQ: accession NM_001009668.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Malecki,J., Ho,A.Y., Moen,A., Dahl,H.A. and Falnes,P.O.
  TITLE     Human METTL20 is a mitochondrial lysine methyltransferase that
            targets the beta subunit of electron transfer flavoprotein
            (ETFbeta) and modulates its activity
  JOURNAL   J Biol Chem 290 (1), 423-434 (2015)
   PUBMED   25416781
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Zhao,X., Leon,I.R., Bak,S., Mogensen,M., Wrzesinski,K., Hojlund,K.
            and Jensen,O.N.
  TITLE     Phosphoproteome analysis of functional mitochondria isolated from
            resting human muscle reveals extensive phosphorylation of inner
            membrane protein complexes and enzymes
  JOURNAL   Mol Cell Proteomics 10 (1), M110.000299 (2011)
   PUBMED   20833797
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Ghisla,S. and Thorpe,C.
  TITLE     Acyl-CoA dehydrogenases. A mechanistic overview
  JOURNAL   Eur J Biochem 271 (3), 494-508 (2004)
   PUBMED   14728676
  REMARK    Review article
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Dwyer,T.M., Mortl,S., Kemter,K., Bacher,A., Fauq,A. and
            Frerman,F.E.
  TITLE     The intraflavin hydrogen bond in human electron transfer
            flavoprotein modulates redox potentials and may participate in
            electron transfer
  JOURNAL   Biochemistry 38 (30), 9735-9745 (1999)
   PUBMED   10423253
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Salazar,D., Zhang,L., deGala,G.D. and Frerman,F.E.
  TITLE     Expression and characterization of two pathogenic mutations in
            human electron transfer flavoprotein
  JOURNAL   J Biol Chem 272 (42), 26425-26433 (1997)
   PUBMED   9334218
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Shinzawa,K., Inagaki,T., Ohishi,N., Ichihara,C., Tsukagoshi,N.,
            Udaka,S. and Yagi,K.
  TITLE     Molecular cloning of a cDNA for alpha-subunit of rat liver electron
            transfer flavoprotein
  JOURNAL   Biochem Biophys Res Commun 155 (1), 300-304 (1988)
   PUBMED   3415685
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088412.1.
            
            On Jan 13, 2005 this sequence version replaced XP_217155.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088412.1, FQ219339.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..333
                     /product="electron transfer flavoprotein subunit alpha,
                     mitochondrial"
                     /note="electron transferring flavoprotein, alpha
                     polypeptide; alpha-ETF; electron-transfer-flavoprotein,
                     alpha polypeptide; electron transfer flavoprotein alpha
                     subunit"
                     /calculated_mol_wt=32837
     transit_peptide 1..19
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P13803.4)"
                     /calculated_mol_wt=2133
     mat_peptide     20..333
                     /product="Electron transfer flavoprotein subunit alpha,
                     mitochondrial. /id=PRO_0000008654"
                     /note="propagated from UniProtKB/Swiss-Prot (P13803.4)"
                     /calculated_mol_wt=32837
     Region          20..204
                     /region_name="Domain I.
                     /evidence=ECO:0000250|UniProtKB:P13804"
                     /note="propagated from UniProtKB/Swiss-Prot (P13803.4)"
     Region          21..332
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
     Site            59
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LC5; propagated from
                     UniProtKB/Swiss-Prot (P13803.4)"
     Site            62
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99LC5; propagated from
                     UniProtKB/Swiss-Prot (P13803.4)"
     Site            69
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LC5; propagated from
                     UniProtKB/Swiss-Prot (P13803.4)"
     Site            75
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99LC5; propagated from
                     UniProtKB/Swiss-Prot (P13803.4)"
     Site            85
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LC5; propagated from
                     UniProtKB/Swiss-Prot (P13803.4)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99LC5; propagated from
                     UniProtKB/Swiss-Prot (P13803.4)"
     Site            101
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99LC5; propagated from
                     UniProtKB/Swiss-Prot (P13803.4)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99LC5; propagated from
                     UniProtKB/Swiss-Prot (P13803.4)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13804; propagated from
                     UniProtKB/Swiss-Prot (P13803.4)"
     Site            158
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LC5; propagated from
                     UniProtKB/Swiss-Prot (P13803.4)"
     Site            164
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99LC5; propagated from
                     UniProtKB/Swiss-Prot (P13803.4)"
     Site            203
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LC5; propagated from
                     UniProtKB/Swiss-Prot (P13803.4)"
     Region          205..333
                     /region_name="Domain II.
                     /evidence=ECO:0000250|UniProtKB:P13804"
                     /note="propagated from UniProtKB/Swiss-Prot (P13803.4)"
     Site            226
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LC5; propagated from
                     UniProtKB/Swiss-Prot (P13803.4)"
     Site            232
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LC5; propagated from
                     UniProtKB/Swiss-Prot (P13803.4)"
     CDS             1..333
                     /gene="Etfa"
                     /gene_synonym="ETF"
                     /coded_by="NM_001009668.1:79..1080"
                     /db_xref="GeneID:300726"
                     /db_xref="RGD:628747"
ORIGIN      
        1 mfraaapgql rraasllrfq stlviaehan dslapitlnt itaagrlgge vsclvagtkc
       61 dkvvqdlckv agvakvlvaq hdaykgllpe eltpliletq kqfsythica gasafgknll
      121 prvaaklnva pvsdiieiks pdtfvrtiya gnalctvkcd ekvkvfsvrg tsfeaaaasg
      181 gsassekaps sssagisewl dqkltksdrp eltgakvvvs ggrglksgen fkllydladq
      241 lhaavgasra avdagfvpnd mqvgqtgkiv apelyiavgi sgaiqhlagm kdsktivain
      301 kdpeapifqv adygivadlf kvvpemteil kkk
//
