LOCUS       NP_569112                656 aa            linear   ROD 05-AUG-2024
DEFINITION  succinate dehydrogenase [ubiquinone] flavoprotein subunit,
            mitochondrial precursor [Rattus norvegicus].
ACCESSION   NP_569112
VERSION     NP_569112.1
DBSOURCE    REFSEQ: accession NM_130428.1
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 656)
  AUTHORS   Eprintsev,A.T., Fedorin,D.N. and Bakarev,M.Y.
  TITLE     [Molecular and biochemical studies of succinate dehydrogenase in
            rat liver under conditions of alloxan diabetes]
  JOURNAL   Biomed Khim 68 (4), 272-278 (2022)
   PUBMED   36005845
  REMARK    GeneRIF: [Molecular and biochemical studies of succinate
            dehydrogenase in rat liver under conditions of alloxan diabetes].',
            trans 'Molekuliarnye i biokhimicheskie issledovaniia
            suktsinatdegidrogenazy v pecheni krys v usloviiakh alloksanovogo
            diabeta.
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Signes,A. and Fernandez-Vizarra,E.
  TITLE     Assembly of mammalian oxidative phosphorylation complexes I-V and
            supercomplexes
  JOURNAL   Essays Biochem 62 (3), 255-270 (2018)
   PUBMED   30030361
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Grunewald,A., Rygiel,K.A., Hepplewhite,P.D., Morris,C.M., Picard,M.
            and Turnbull,D.M.
  TITLE     Mitochondrial DNA Depletion in Respiratory Chain-Deficient
            Parkinson Disease Neurons
  JOURNAL   Ann Neurol 79 (3), 366-378 (2016)
   PUBMED   26605748
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Guo,X., Li,D., Wu,Y., Chen,Y., Zhou,X., Wang,X., Huang,X., Li,X.,
            Yang,H. and Xing,J.
  TITLE     Genetic variants in genes of tricarboxylic acid cycle key enzymes
            are associated with prognosis of patients with non-small cell lung
            cancer
  JOURNAL   Lung Cancer 87 (2), 162-168 (2015)
   PUBMED   25576295
REFERENCE   5  (residues 1 to 656)
  AUTHORS   Claycombe,K.J., Roemmich,J.N., Johnson,L., Vomhof-DeKrey,E.E. and
            Johnson,W.T.
  TITLE     Skeletal muscle Sirt3 expression and mitochondrial respiration are
            regulated by a prenatal low-protein diet
  JOURNAL   J Nutr Biochem 26 (2), 184-189 (2015)
   PUBMED   25483313
  REMARK    GeneRIF: Data suggest activation/acetylation of Sdha in skeletal
            muscle can be regulated by diet; maternal low-protein leads to
            inactivation of Sdha; postnatal high-fat leads to further
            inactivation of Sdha; this increases susceptibility to type 2
            diabetes.
REFERENCE   6  (residues 1 to 656)
  AUTHORS   Schilling,B., Murray,J., Yoo,C.B., Row,R.H., Cusack,M.P.,
            Capaldi,R.A. and Gibson,B.W.
  TITLE     Proteomic analysis of succinate dehydrogenase and
            ubiquinol-cytochrome c reductase (Complex II and III) isolated by
            immunoprecipitation from bovine and mouse heart mitochondria
  JOURNAL   Biochim Biophys Acta 1762 (2), 213-222 (2006)
   PUBMED   16120479
REFERENCE   7  (residues 1 to 656)
  AUTHORS   Sun,F., Huo,X., Zhai,Y., Wang,A., Xu,J., Su,D., Bartlam,M. and
            Rao,Z.
  TITLE     Crystal structure of mitochondrial respiratory membrane protein
            complex II
  JOURNAL   Cell 121 (7), 1043-1057 (2005)
   PUBMED   15989954
REFERENCE   8  (residues 1 to 656)
  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   9  (residues 1 to 656)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
REFERENCE   10 (residues 1 to 656)
  AUTHORS   Bourgeron,T., Rustin,P., Chretien,D., Birch-Machin,M.,
            Bourgeois,M., Viegas-Pequignot,E., Munnich,A. and Rotig,A.
  TITLE     Mutation of a nuclear succinate dehydrogenase gene results in
            mitochondrial respiratory chain deficiency
  JOURNAL   Nat Genet 11 (2), 144-149 (1995)
   PUBMED   7550341
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB072907.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB072907.1, SRR8487231.147407.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [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..656
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..656
                     /product="succinate dehydrogenase [ubiquinone]
                     flavoprotein subunit, mitochondrial precursor"
                     /EC_number="1.3.5.1"
                     /note="succinate dehydrogenase [ubiquinone] flavoprotein
                     subunit, mitochondrial; fp; flavoprotein subunit of
                     complex II; succinate dehydrogenase complex, subunit A,
                     flavoprotein (Fp); malate dehydrogenase [quinone]
                     flavoprotein subunit"
                     /calculated_mol_wt=68076
     transit_peptide 1..34
                     /note="Mitochondrion.
                     /evidence=ECO:0000250|UniProtKB:Q0QF01; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
                     /calculated_mol_wt=3557
     mat_peptide     35..656
                     /product="Succinate dehydrogenase [ubiquinone]
                     flavoprotein subunit, mitochondrial. /id=PRO_0000010338"
                     /note="propagated from UniProtKB/Swiss-Prot (Q920L2.1)"
                     /calculated_mol_wt=68076
     Region          44..656
                     /region_name="PTZ00139"
                     /note="Succinate dehydrogenase [ubiquinone] flavoprotein
                     subunit; Provisional"
                     /db_xref="CDD:240286"
     Site            171
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P31040; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            174
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000250|UniProtKB:P31040; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            242
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            327
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P31040; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            415
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            472
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            477
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            490
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            509
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            530
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            542
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            590
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            600
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P31040; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            616
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            625
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            628
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     Site            639
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (Q920L2.1)"
     CDS             1..656
                     /gene="Sdha"
                     /coded_by="NM_130428.1:42..2012"
                     /db_xref="GeneID:157074"
                     /db_xref="RGD:621557"
ORIGIN      
        1 magvgavsrl lrgrrlalag atrgfhfsvg eskkasakvs daistqypvv dhefdavvvg
       61 aggaglraaf glseagfnta cltklfptrs htvaaqggin aalgnmeedn wrwhfydtvk
      121 gsdwlgdqda ihymteqapa svvelenygm pfsrtedgri yqrafggqsl kfgkggqahr
      181 cccvadrtgh sllhtlygrs lrydtsyfve yfaldllmen gecrgvialc iedgsihrir
      241 akntiiatgg ygrtyfscts ahtstgdgta mvtraglpcq dlefvqfhpt giygagclit
      301 egcrgeggil insqgerfme ryapvakdla srdvvsrsmt leiregrgcg pekdhvylql
      361 hhlppeqlat rlpgisetam ifagvdvtke pipvlptvhy nmggiptnyk gqvlkhvngq
      421 dqivpglyac geaacasvhg anrlgansll dlvvfgraca lsiaescrpg dkvppikana
      481 geesvmnldk lrfadgsvrt selrlsmqks mqshaavfrv gsvlqegcek vsqlygdlqh
      541 lktfdrgmvw ntdlvetlel qnlmlcalqt iygaearkes rgaharedyk vrideydysk
      601 piegqqkkpf aehwrkhtls yvdtktgkvt ldyrpvidkt lneadcatvp pairsy
//
