ID   SODM_MOUSE              Reviewed;         222 AA.
AC   P09671; Q64670; Q8VEM5;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 3.
DT   27-MAR-2024, entry version 216.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=Sod2; Synonyms=Sod-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Placenta;
RX   PubMed=3797253; DOI=10.1093/nar/14.23.9539;
RA   Hallewell R.A., Mullenbach G.T., Stempien M.M., Bell G.I.;
RT   "Sequence of a cDNA coding for mouse manganese superoxide dismutase.";
RL   Nucleic Acids Res. 14:9539-9539(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ, and C3H/HeJ;
RX   PubMed=8406027; DOI=10.1016/0378-1119(93)90311-p;
RA   Sun Y., Hegamyer G., Colburn N.M.;
RT   "Sequence of manganese superoxide dismutase-encoding cDNAs from multiple
RT   mouse organs.";
RL   Gene 131:301-302(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7875582; DOI=10.1016/0378-1119(94)00666-g;
RA   Jones P.L., Kucera G., Gordon H.M., Boss J.M.;
RT   "Cloning and characterization of the murine manganous superoxide dismutase-
RT   encoding gene.";
RL   Gene 153:155-161(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7613035; DOI=10.1007/bf00352417;
RA   Disilvestre D., Kleeberger S.R., Johns J., Levitt R.C.;
RT   "Structure and DNA sequence of the mouse MnSOD gene.";
RL   Mamm. Genome 6:281-284(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 54-68; 76-108; 115-130 AND 203-216, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   ACETYLATION AT LYS-122, DEACETYLATION BY SIRT3, AND MUTAGENESIS OF LYS-122.
RX   PubMed=21172655; DOI=10.1016/j.molcel.2010.12.013;
RA   Tao R., Coleman M.C., Pennington J.D., Ozden O., Park S.H., Jiang H.,
RA   Kim H.S., Flynn C.R., Hill S., Hayes McDonald W., Olivier A.K., Spitz D.R.,
RA   Gius D.;
RT   "Sirt3-mediated deacetylation of evolutionarily conserved lysine 122
RT   regulates MnSOD activity in response to stress.";
RL   Mol. Cell 40:893-904(2010).
RN   [10]
RP   INDUCTION.
RX   PubMed=20668652; DOI=10.1371/journal.pone.0011786;
RA   Goitre L., Balzac F., Degani S., Degan P., Marchi S., Pinton P.,
RA   Retta S.F.;
RT   "KRIT1 regulates the homeostasis of intracellular reactive oxygen
RT   species.";
RL   PLoS ONE 5:E11786-E11786(2010).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-130, SUCCINYLATION [LARGE SCALE
RP   ANALYSIS] AT LYS-68; LYS-75; LYS-122 AND LYS-130, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast, and Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-75; LYS-114; LYS-122;
RP   LYS-130 AND LYS-202, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P04179};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P04179};
CC   -!- SUBUNIT: Homotetramer.
CC   -!- INTERACTION:
CC       P09671; P54099: Polg; NbExp=2; IntAct=EBI-1635071, EBI-863636;
CC       P09671; P02340: Tp53; NbExp=2; IntAct=EBI-1635071, EBI-474016;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- INDUCTION: Expression is regulated by KRIT1.
CC       {ECO:0000269|PubMed:20668652}.
CC   -!- PTM: Nitrated under oxidative stress. Nitration coupled with oxidation
CC       inhibits the catalytic activity (By similarity).
CC       {ECO:0000250|UniProtKB:P04179}.
CC   -!- PTM: Acetylation at Lys-122 decreases enzymatic activity. Deacetylated
CC       by SIRT3 upon exposure to ionizing radiations or after long fasting.
CC       {ECO:0000269|PubMed:21172655}.
CC   -!- PTM: Polyubiquitinated; leading to proteasomal degradation.
CC       Deubiquitinated by USP36 which increases protein stability.
CC       {ECO:0000250|UniProtKB:P04179}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; X04972; CAA28645.1; -; mRNA.
DR   EMBL; Z18857; CAA79308.1; -; mRNA.
DR   EMBL; L35528; AAB60902.1; -; Genomic_DNA.
DR   EMBL; L35525; AAB60902.1; JOINED; Genomic_DNA.
DR   EMBL; L35526; AAB60902.1; JOINED; Genomic_DNA.
DR   EMBL; L35527; AAB60902.1; JOINED; Genomic_DNA.
DR   EMBL; S78846; AAB34899.1; -; Genomic_DNA.
DR   EMBL; S78832; AAB34899.1; JOINED; Genomic_DNA.
DR   EMBL; S78842; AAB34899.1; JOINED; Genomic_DNA.
DR   EMBL; S78844; AAB34899.1; JOINED; Genomic_DNA.
DR   EMBL; AK002428; BAB22095.1; -; mRNA.
DR   EMBL; AK002534; BAB22170.1; -; mRNA.
DR   EMBL; AK012354; BAB28183.1; -; mRNA.
DR   EMBL; BC010548; AAH10548.1; -; mRNA.
DR   EMBL; BC018173; AAH18173.1; -; mRNA.
DR   CCDS; CCDS28399.1; -.
DR   PIR; I57023; I57023.
DR   RefSeq; NP_038699.2; NM_013671.3.
DR   AlphaFoldDB; P09671; -.
DR   SMR; P09671; -.
DR   BioGRID; 203388; 13.
DR   IntAct; P09671; 6.
DR   MINT; P09671; -.
DR   STRING; 10090.ENSMUSP00000007012; -.
DR   GlyGen; P09671; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P09671; -.
DR   PhosphoSitePlus; P09671; -.
DR   SwissPalm; P09671; -.
DR   REPRODUCTION-2DPAGE; IPI00109109; -.
DR   REPRODUCTION-2DPAGE; P09671; -.
DR   EPD; P09671; -.
DR   jPOST; P09671; -.
DR   PaxDb; 10090-ENSMUSP00000007012; -.
DR   PeptideAtlas; P09671; -.
DR   ProteomicsDB; 258709; -.
DR   Pumba; P09671; -.
DR   TopDownProteomics; P09671; -.
DR   Antibodypedia; 785; 1243 antibodies from 48 providers.
DR   DNASU; 20656; -.
DR   Ensembl; ENSMUST00000007012.6; ENSMUSP00000007012.5; ENSMUSG00000006818.6.
DR   GeneID; 20656; -.
DR   KEGG; mmu:20656; -.
DR   UCSC; uc008alv.1; mouse.
DR   AGR; MGI:98352; -.
DR   CTD; 6648; -.
DR   MGI; MGI:98352; Sod2.
DR   VEuPathDB; HostDB:ENSMUSG00000006818; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   GeneTree; ENSGT00390000011877; -.
DR   HOGENOM; CLU_031625_2_1_1; -.
DR   InParanoid; P09671; -.
DR   OMA; DSLINWD; -.
DR   OrthoDB; 4839at2759; -.
DR   PhylomeDB; P09671; -.
DR   TreeFam; TF105132; -.
DR   Reactome; R-MMU-2151201; Transcriptional activation of mitochondrial biogenesis.
DR   Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR   BioGRID-ORCS; 20656; 25 hits in 75 CRISPR screens.
DR   ChiTaRS; Sod2; mouse.
DR   PRO; PR:P09671; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; P09671; Protein.
DR   Bgee; ENSMUSG00000006818; Expressed in heart right ventricle and 305 other cell types or tissues.
DR   ExpressionAtlas; P09671; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IMP:CACAO.
DR   GO; GO:0019825; F:oxygen binding; ISO:MGI.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:MGI.
DR   GO; GO:0003069; P:acetylcholine-mediated vasodilation involved in regulation of systemic arterial blood pressure; IMP:MGI.
DR   GO; GO:0008637; P:apoptotic mitochondrial changes; IMP:MGI.
DR   GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR   GO; GO:0003032; P:detection of oxygen; IMP:MGI.
DR   GO; GO:0048773; P:erythrophore differentiation; IMP:MGI.
DR   GO; GO:0006749; P:glutathione metabolic process; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISO:MGI.
DR   GO; GO:0042743; P:hydrogen peroxide metabolic process; ISO:MGI.
DR   GO; GO:0032364; P:intracellular oxygen homeostasis; ISO:MGI.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR   GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:MGI.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR   GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:MGI.
DR   GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:MGI.
DR   GO; GO:1902631; P:negative regulation of membrane hyperpolarization; ISO:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR   GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0048666; P:neuron development; IMP:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR   GO; GO:0010729; P:positive regulation of hydrogen peroxide biosynthetic process; ISO:MGI.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:MGI.
DR   GO; GO:1905461; P:positive regulation of vascular associated smooth muscle cell apoptotic process; ISO:MGI.
DR   GO; GO:1905932; P:positive regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching; ISO:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; IMP:MGI.
DR   GO; GO:0019430; P:removal of superoxide radicals; IMP:MGI.
DR   GO; GO:0022904; P:respiratory electron transport chain; IMP:MGI.
DR   GO; GO:0014823; P:response to activity; IMP:MGI.
DR   GO; GO:0048678; P:response to axon injury; IMP:MGI.
DR   GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
DR   GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR   GO; GO:0010332; P:response to gamma radiation; IGI:MGI.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
DR   GO; GO:0055093; P:response to hyperoxia; IMP:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR   GO; GO:0035900; P:response to isolation stress; IEA:Ensembl.
DR   GO; GO:0033591; P:response to L-ascorbic acid; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0071000; P:response to magnetism; IEA:Ensembl.
DR   GO; GO:0010042; P:response to manganese ion; IEA:Ensembl.
DR   GO; GO:0031667; P:response to nutrient levels; ISO:MGI.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
DR   GO; GO:0000302; P:response to reactive oxygen species; IMP:MGI.
DR   GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
DR   GO; GO:0034021; P:response to silicon dioxide; IEA:Ensembl.
DR   GO; GO:0000303; P:response to superoxide; IMP:MGI.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR   GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
DR   GO; GO:0042554; P:superoxide anion generation; IMP:MGI.
DR   GO; GO:0006801; P:superoxide metabolic process; IMP:MGI.
DR   GO; GO:0042311; P:vasodilation; IMP:MGI.
DR   Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
DR   SWISS-2DPAGE; P09671; -.
DR   Genevisible; P09671; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Manganese; Metal-binding;
KW   Mitochondrion; Nitration; Oxidoreductase; Reference proteome;
KW   Transit peptide; Ubl conjugation.
FT   TRANSIT         1..24
FT                   /note="Mitochondrion"
FT   CHAIN           25..222
FT                   /note="Superoxide dismutase [Mn], mitochondrial"
FT                   /id="PRO_0000032871"
FT   BINDING         50
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         58
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
FT   MOD_RES         68
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         68
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         75
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         75
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         114
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         122
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21172655,
FT                   ECO:0007744|PubMed:23576753"
FT   MOD_RES         122
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         130
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753,
FT                   ECO:0007744|PubMed:23806337"
FT   MOD_RES         130
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         202
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MUTAGEN         122
FT                   /note="K->R: Reverses IR-Induced increases in superoxide
FT                   and genomic Instability in SIRT3-deficient mice."
FT                   /evidence="ECO:0000269|PubMed:21172655"
FT   CONFLICT        5
FT                   /note="A -> G (in Ref. 5; AAH18173)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        18
FT                   /note="G -> V (in Ref. 1; CAA28645)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="V -> M (in Ref. 1 and 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   222 AA;  24603 MW;  9AE804C55A8357D9 CRC64;
     MLCRAACSTG RRLGPVAGAA GSRHKHSLPD LPYDYGALEP HINAQIMQLH HSKHHAAYVN
     NLNATEEKYH EALAKGDVTT QVALQPALKF NGGGHINHTI FWTNLSPKGG GEPKGELLEA
     IKRDFGSFEK FKEKLTAVSV GVQGSGWGWL GFNKEQGRLQ IAACSNQDPL QGTTGLIPLL
     GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVTERYTAC KK
//