LOCUS       NP_077374                780 aa            linear   ROD 01-JUN-2024
DEFINITION  aconitate hydratase, mitochondrial precursor [Rattus norvegicus].
ACCESSION   NP_077374
VERSION     NP_077374.2
DBSOURCE    REFSEQ: accession NM_024398.2
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 780)
  AUTHORS   Wei,J., Zhang,J., Wei,J., Hu,M., Chen,X., Qin,X., Chen,J., Lei,F.
            and Qin,Y.
  TITLE     Identification of AGXT2, SHMT1, and ACO2 as important biomarkers of
            acute kidney injury by WGCNA
  JOURNAL   PLoS One 18 (2), e0281439 (2023)
   PUBMED   36735737
  REMARK    GeneRIF: Identification of AGXT2, SHMT1, and ACO2 as important
            biomarkers of acute kidney injury by WGCNA.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Kim,S.J., Cheresh,P., Williams,D., Cheng,Y., Ridge,K.,
            Schumacker,P.T., Weitzman,S., Bohr,V.A. and Kamp,D.W.
  TITLE     Mitochondria-targeted Ogg1 and aconitase-2 prevent oxidant-induced
            mitochondrial DNA damage in alveolar epithelial cells
  JOURNAL   J Biol Chem 289 (9), 6165-6176 (2014)
   PUBMED   24429287
  REMARK    GeneRIF: Ogg1 chaperoning of Aco-2 in preventing oxidant-mediated
            mtDNA damage and apoptosis may afford an innovative target for the
            molecular events underlying oxidant-induced toxicity.
REFERENCE   3  (residues 1 to 780)
  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   4  (residues 1 to 780)
  AUTHORS   Zhuravliova,E., Barbakadze,T., Zaalishvili,E., Chipashvili,M.,
            Koshoridze,N. and Mikeladze,D.
  TITLE     Social isolation in rats inhibits oxidative metabolism, decreases
            the content of mitochondrial K-Ras and activates mitochondrial
            hexokinase
  JOURNAL   Behav Brain Res 205 (2), 377-383 (2009)
   PUBMED   19616040
REFERENCE   5  (residues 1 to 780)
  AUTHORS   Lin,G., Brownsey,R.W. and MacLeod,K.M.
  TITLE     Regulation of mitochondrial aconitase by phosphorylation in
            diabetic rat heart
  JOURNAL   Cell Mol Life Sci 66 (5), 919-932 (2009)
   PUBMED   19153662
  REMARK    GeneRIF: These results demonstrate the regulation of mitochondrial
            aconitase activity by protein kinase C-dependent phosphorylation.
REFERENCE   6  (residues 1 to 780)
  AUTHORS   Andersson,U., Leighton,B., Young,M.E., Blomstrand,E. and
            Newsholme,E.A.
  TITLE     Inactivation of aconitase and oxoglutarate dehydrogenase in
            skeletal muscle in vitro by superoxide anions and/or nitric oxide
  JOURNAL   Biochem Biophys Res Commun 249 (2), 512-516 (1998)
   PUBMED   9712727
REFERENCE   7  (residues 1 to 780)
  AUTHORS   Mirel,D.B., Marder,K., Graziano,J., Freyer,G., Zhao,Q., Mayeux,R.
            and Wilhelmsen,K.C.
  TITLE     Characterization of the human mitochondrial aconitase gene (ACO2)
  JOURNAL   Gene 213 (1-2), 205-218 (1998)
   PUBMED   9630632
REFERENCE   8  (residues 1 to 780)
  AUTHORS   Chernyshev,V.V., Mavlikaev,R.G., Burtsev,V.I., Dutko,Iu.S. and
            Zhidkov,V.A.
  TITLE     [Aerosol vaccination of broilers against Newcastle disease]
  JOURNAL   Veterinariia (12), 78-80 (1978)
   PUBMED   734909
REFERENCE   9  (residues 1 to 780)
  AUTHORS   Masini,A., Guarriero-Bobyleva,V., Pincelli-Gatti,A. and Cennamo,C.
  TITLE     Developmental changes of rat liver cytoplasmic and mitochondrial
            aconitate hydratases
  JOURNAL   Ital J Biochem 27 (5), 300-304 (1978)
   PUBMED   755797
REFERENCE   10 (residues 1 to 780)
  AUTHORS   Slaughter,C.A., Hopkinson,D.A. and Harris,H.
  TITLE     Aconitase polymorphism in man
  JOURNAL   Ann Hum Genet 39 (2), 193-202 (1975)
   PUBMED   1052766
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061999.1.
            
            On Jan 1, 2004 this sequence version replaced NP_077374.1.
            
            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 :: BC061999.1, AJ243266.1 [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..780
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..780
                     /product="aconitate hydratase, mitochondrial precursor"
                     /EC_number="4.2.1.3"
                     /note="aconitate hydratase, mitochondrial; citrate
                     hydro-lyase; aconitase 2, mitochondrial; mitochondrial
                     aconitase (nuclear aco2 gene)"
                     /calculated_mol_wt=82462
     transit_peptide 1..27
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q9ER34.2)"
                     /calculated_mol_wt=2990
     mat_peptide     28..780
                     /product="Aconitate hydratase, mitochondrial.
                     /id=PRO_0000000544"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ER34.2)"
                     /calculated_mol_wt=82462
     Region          45..775
                     /region_name="aconitase_mito"
                     /note="aconitate hydratase, mitochondrial; TIGR01340"
                     /db_xref="CDD:273561"
     Site            50
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99KI0; propagated from
                     UniProtKB/Swiss-Prot (Q9ER34.2)"
     Site            138
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99KI0; propagated from
                     UniProtKB/Swiss-Prot (Q9ER34.2)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99KI0; propagated from
                     UniProtKB/Swiss-Prot (Q9ER34.2)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99KI0; propagated from
                     UniProtKB/Swiss-Prot (Q9ER34.2)"
     Site            517
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99KI0; propagated from
                     UniProtKB/Swiss-Prot (Q9ER34.2)"
     Site            523
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99KI0; propagated from
                     UniProtKB/Swiss-Prot (Q9ER34.2)"
     Region          524..560
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ER34.2)"
     Site            559
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ER34.2)"
     Site            573
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99798; propagated from
                     UniProtKB/Swiss-Prot (Q9ER34.2)"
     Site            605
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99798; propagated from
                     UniProtKB/Swiss-Prot (Q9ER34.2)"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99KI0; propagated from
                     UniProtKB/Swiss-Prot (Q9ER34.2)"
     Site            723
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99KI0; propagated from
                     UniProtKB/Swiss-Prot (Q9ER34.2)"
     Site            730
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99KI0; propagated from
                     UniProtKB/Swiss-Prot (Q9ER34.2)"
     Site            736
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99KI0; propagated from
                     UniProtKB/Swiss-Prot (Q9ER34.2)"
     Site            743
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99KI0; propagated from
                     UniProtKB/Swiss-Prot (Q9ER34.2)"
     CDS             1..780
                     /gene="Aco2"
                     /coded_by="NM_024398.2:5..2347"
                     /db_xref="GeneID:79250"
                     /db_xref="RGD:621360"
ORIGIN      
        1 mapysllvtr lqkalgvrqy hvasalcqra kvamshfeps eyirydllek ninivrkrln
       61 rpltlsekiv yghlddpanq eiergktylr lrpdrvamqd ataqmamlqf issglpkvav
      121 pstihcdhli eaqlggekdl rrakdinqev ynflatagak ygvgfwrpgs giihqiilen
      181 yaypgvllig tdshtpnggg lggicigvgg adavdvmagi pwelkcpkvi gvkltgtlsg
      241 wtspkdvilk vagiltvkgg tgaiveyhgp gvdsisctgm aticnmgaei gattsvfpyn
      301 hrmkkylskt gradianlae efkdhlvpdp gcqydqviei nlnelkphin gpftpdlahp
      361 vadvgtvaek egwpldirvg ligsctnssy edmgrsaava kqalahglkc ksqftitpgs
      421 eqiratierd gyaqilrdvg givlanacgp cigqwdrkdi kkgekntivt synrnftgrn
      481 danpethafv tspeivtala iagtlkfnpe tdfltgkdgk kfkleapdad elprsdfdpg
      541 qdtyqhppkd ssgqrvdvsp tsqrlqllep fdkwdgkdle dlqilikvkg kcttdhisaa
      601 gpwlkfrghl dnisnnllig ainiengkan svrnavtqef gpvpdtaryy kkhgirwvvi
      661 gdenygegss rehaaleprh lggraiitks farihetnlk kqgllpltfa dpsdynkihp
      721 vdkltiqglk dfapgkplnc iikhpngtqe tillnhtfne tqiewfrags alnrmkelqq
//
