LOCUS       NP_542364                780 aa            linear   ROD 27-APR-2025
DEFINITION  aconitate hydratase, mitochondrial precursor [Mus musculus].
ACCESSION   NP_542364
VERSION     NP_542364.1
DBSOURCE    REFSEQ: accession NM_080633.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Ayyangar,U., Karkhanis,A., Tay,H., Afandi,A.F.B., Bhattacharjee,O.,
            Ks,L., Lee,S.H., Chan,J. and Raghavan,S.
  TITLE     Metabolic rewiring of macrophages by epidermal-derived lactate
            promotes sterile inflammation in the murine skin
  JOURNAL   EMBO J 43 (7), 1113-1134 (2024)
   PUBMED   38418556
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Zhu,J., Xu,F., Lai,H., Yuan,H., Li,X.Y., Hu,J., Li,W., Liu,L. and
            Wang,C.
  TITLE     ACO2 deficiency increases vulnerability to Parkinson's disease via
            dysregulating mitochondrial function and histone
            acetylation-mediated transcription of autophagy genes
  JOURNAL   Commun Biol 6 (1), 1201 (2023)
   PUBMED   38007539
  REMARK    GeneRIF: ACO2 deficiency increases vulnerability to Parkinson's
            disease via dysregulating mitochondrial function and histone
            acetylation-mediated transcription of autophagy genes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 780)
  AUTHORS   Mirhadi,S., Zhang,W., Pham,N.A., Karimzadeh,F., Pintilie,M.,
            Tong,J., Taylor,P., Krieger,J., Pitcher,B., Sykes,J.,
            Wybenga-Groot,L., Fladd,C., Xu,J., Wang,T., Cabanero,M., Li,M.,
            Weiss,J., Sakashita,S., Zaslaver,O., Yu,M., Caudy,A.A.,
            St-Pierre,J., Hawkins,C., Kislinger,T., Liu,G., Shepherd,F.A.,
            Tsao,M.S. and Moran,M.F.
  TITLE     Mitochondrial Aconitase ACO2 Links Iron Homeostasis with
            Tumorigenicity in Non-Small Cell Lung Cancer
  JOURNAL   Mol Cancer Res 21 (1), 36-50 (2023)
   PUBMED   36214668
  REMARK    GeneRIF: Mitochondrial Aconitase ACO2 Links Iron Homeostasis with
            Tumorigenicity in Non-Small Cell Lung Cancer.
REFERENCE   5  (residues 1 to 780)
  AUTHORS   Yook,J.S., You,M., Kim,J., Toney,A.M., Fan,R., Puniya,B.L.,
            Helikar,T., Vaulont,S., Deschemin,J.C., Okla,M., Xie,L.,
            Ghosh,M.C., Rouault,T.A., Lee,J. and Chung,S.
  TITLE     Essential role of systemic iron mobilization and redistribution for
            adaptive thermogenesis through HIF2-alpha/hepcidin axis
  JOURNAL   Proc Natl Acad Sci U S A 118 (40) (2021)
   PUBMED   34593646
REFERENCE   6  (residues 1 to 780)
  AUTHORS   Peters,L.L., Weier,H.U., Walensky,L.D., Snyder,S.H., Parra,M.,
            Mohandas,N. and Conboy,J.G.
  TITLE     Four paralogous protein 4.1 genes map to distinct chromosomes in
            mouse and human
  JOURNAL   Genomics 54 (2), 348-350 (1998)
   PUBMED   9828140
REFERENCE   7  (residues 1 to 780)
  AUTHORS   Ko,M.S., Threat,T.A., Wang,X., Horton,J.H., Cui,Y., Wang,X.,
            Pryor,E., Paris,J., Wells-Smith,J., Kitchen,J.R., Rowe,L.B.,
            Eppig,J., Satoh,T., Brant,L., Fujiwara,H., Yotsumoto,S. and
            Nakashima,H.
  TITLE     Genome-wide mapping of unselected transcripts from extraembryonic
            tissue of 7.5-day mouse embryos reveals enrichment in the t-complex
            and under-representation on the X chromosome
  JOURNAL   Hum Mol Genet 7 (12), 1967-1978 (1998)
   PUBMED   9811942
REFERENCE   8  (residues 1 to 780)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   9  (residues 1 to 780)
  AUTHORS   Welch,C.L., Xia,Y.R., Shechter,I., Farese,R., Mehrabian,M.,
            Mehdizadeh,S., Warden,C.H. and Lusis,A.J.
  TITLE     Genetic regulation of cholesterol homeostasis: chromosomal
            organization of candidate genes
  JOURNAL   J Lipid Res 37 (7), 1406-1421 (1996)
   PUBMED   8827514
  REMARK    Erratum:[J Lipid Res 1996 Oct;37(10):2269]
REFERENCE   10 (residues 1 to 780)
  AUTHORS   Warden,C.H., Mehrabian,M., He,K.Y., Yoon,M.Y., Diep,A., Xia,Y.R.,
            Wen,P.Z., Svenson,K.L., Sparkes,R.S. and Lusis,A.J.
  TITLE     Linkage mapping of 40 randomly isolated liver cDNA clones in the
            mouse
  JOURNAL   Genomics 18 (2), 295-307 (1993)
   PUBMED   8288233
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI987806.1, BY732916.1, CA750686.1, CO426953.1, CO429053.1 and
            BQ031215.1.
            
            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 :: AK145511.1, BC004645.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 38.26 cM"
     Protein         1..780
                     /product="aconitate hydratase, mitochondrial precursor"
                     /EC_number="4.2.1.3"
                     /note="aconitate hydratase, mitochondrial; citrate
                     hydro-lyase"
                     /calculated_mol_wt=82464
     transit_peptide 1..27
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q99KI0.1)"
                     /calculated_mol_wt=3018
     mat_peptide     28..780
                     /product="Aconitate hydratase, mitochondrial.
                     /id=PRO_0000000542"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99KI0.1)"
                     /calculated_mol_wt=82464
     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:0007744|PubMed:23576753,
                     ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q99KI0.1)"
     Site            138
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99KI0.1)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753,
                     ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q99KI0.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99KI0.1)"
     Site            517
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99KI0.1)"
     Site            523
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99KI0.1)"
     Region          524..560
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99KI0.1)"
     Site            559
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99798; propagated from
                     UniProtKB/Swiss-Prot (Q99KI0.1)"
     Site            573
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99798; propagated from
                     UniProtKB/Swiss-Prot (Q99KI0.1)"
     Site            605
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99KI0.1)"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q99KI0.1)"
     Site            723
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99KI0.1)"
     Site            730
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99KI0.1)"
     Site            736
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99KI0.1)"
     Site            739
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99KI0.1)"
     Site            743
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99KI0.1)"
     CDS             1..780
                     /gene="Aco2"
                     /gene_synonym="Aco-2; Aco3; D10Wsu183e; Irp1"
                     /coded_by="NM_080633.2:51..2393"
                     /db_xref="CCDS:CCDS27675.1"
                     /db_xref="GeneID:11429"
                     /db_xref="MGI:MGI:87880"
ORIGIN      
        1 mapysllvtr lqkalgvrqy hvasvlcqra kvamshfeps eyirydllek ninivrkrln
       61 rpltlsekiv yghlddpanq eiergktylr lrpdrvamqd ataqmamlqf issglpkvav
      121 pstihcdhli eaqvggekdl rrakdinqev ynflatagak ygvgfwrpgs giihqiilen
      181 yaypgvllig tdshtpnggg lggicigvgg adavdvmagi pwelkcpkvi gvkltgslsg
      241 wtspkdvilk vagiltvkgg tgaiveyhgp gvdsisctgm aticnmgaei gattsvfpyn
      301 hrmkkylskt grtdianlae 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 dfapgkplkc vikhpngtqe tillnhtfne tqiewfrags alnrmkelqq
//
