GenomeNet

Database: UniProt/SWISS-PROT
Entry: SODM_MOUSE
LinkDB: SODM_MOUSE
Original site: SODM_MOUSE 
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   13-FEB-2019, entry version 192.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   multiple 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
RT   dismutase-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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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
RP   IDENTIFICATION 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   ACETYLATION AT LYS-122, DEACETYLATION BY SIRT3, AND MUTAGENESIS OF
RP   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.,
RA   Spitz D.R., 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
RP   SCALE ANALYSIS] AT LYS-68; LYS-75; LYS-122 AND LYS-130, AND
RP   IDENTIFICATION BY 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.,
RA   Zhang Y., 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;
RP   LYS-122; LYS-130 AND LYS-202, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE 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.,
RA   Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in
RT   mitochondria 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
CC       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.
CC       {ECO:0000250|UniProtKB:P04179};
CC   -!- SUBUNIT: Homotetramer.
CC   -!- INTERACTION:
CC       P54099:Polg; NbExp=2; IntAct=EBI-1635071, EBI-863636;
CC       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
CC       oxidation inhibits the catalytic activity (By similarity).
CC       {ECO:0000250|UniProtKB:P04179}.
CC   -!- PTM: Acetylation at Lys-122 decreases enzymatic activity.
CC       Deacetylated by SIRT3 upon exposure to ionizing radiations or
CC       after long fasting. {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
CC       family. {ECO:0000305}.
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   UniGene; Mm.290876; -.
DR   ProteinModelPortal; P09671; -.
DR   SMR; P09671; -.
DR   BioGrid; 203388; 2.
DR   IntAct; P09671; 7.
DR   MINT; P09671; -.
DR   STRING; 10090.ENSMUSP00000007012; -.
DR   iPTMnet; P09671; -.
DR   PhosphoSitePlus; P09671; -.
DR   SwissPalm; P09671; -.
DR   REPRODUCTION-2DPAGE; IPI00109109; -.
DR   REPRODUCTION-2DPAGE; P09671; -.
DR   SWISS-2DPAGE; P09671; -.
DR   EPD; P09671; -.
DR   jPOST; P09671; -.
DR   PaxDb; P09671; -.
DR   PeptideAtlas; P09671; -.
DR   PRIDE; P09671; -.
DR   TopDownProteomics; P09671; -.
DR   Ensembl; ENSMUST00000007012; ENSMUSP00000007012; ENSMUSG00000006818.
DR   GeneID; 20656; -.
DR   KEGG; mmu:20656; -.
DR   UCSC; uc008alv.1; mouse.
DR   CTD; 6648; -.
DR   MGI; MGI:98352; Sod2.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   GeneTree; ENSGT00390000011877; -.
DR   HOGENOM; HOG000013583; -.
DR   HOVERGEN; HBG004451; -.
DR   InParanoid; P09671; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 1353361at2759; -.
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   ChiTaRS; Sod2; mouse.
DR   PRO; PR:P09671; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   Bgee; ENSMUSG00000006818; Expressed in 339 organ(s), highest expression level in cardiac ventricle.
DR   ExpressionAtlas; P09671; baseline and differential.
DR   Genevisible; P09671; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:0046872; F:metal ion binding; IBA:GO_Central.
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:0001306; P:age-dependent response to oxidative stress; IMP:MGI.
DR   GO; GO:0001315; P:age-dependent response to reactive oxygen species; ISS:UniProtKB.
DR   GO; GO:0007568; P:aging; IBA:GO_Central.
DR   GO; GO:0008637; P:apoptotic mitochondrial changes; IMP:MGI.
DR   GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
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: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:0055072; P:iron ion homeostasis; 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: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: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 smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0048666; P:neuron development; IMP:MGI.
DR   GO; GO:0032364; P:oxygen homeostasis; ISO:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; 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 smooth muscle cell differentiation involved in phenotypic switching; ISO:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR   GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0050790; P:regulation of catalytic activity; 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:0009409; P:response to cold; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; ISO:MGI.
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: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; -; 1.
DR   Gene3D; 2.40.500.20; -; 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   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Direct protein sequencing; Manganese;
KW   Metal-binding; Mitochondrion; Nitration; Oxidoreductase;
KW   Reference proteome; Transit peptide; Ubl conjugation.
FT   TRANSIT       1     24       Mitochondrion.
FT   CHAIN        25    222       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032871.
FT   METAL        50     50       Manganese. {ECO:0000250}.
FT   METAL        98     98       Manganese. {ECO:0000250}.
FT   METAL       183    183       Manganese. {ECO:0000250}.
FT   METAL       187    187       Manganese. {ECO:0000250}.
FT   MOD_RES      58     58       Nitrated tyrosine.
FT                                {ECO:0000250|UniProtKB:P04179}.
FT   MOD_RES      68     68       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES      68     68       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES      75     75       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES      75     75       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     114    114       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     122    122       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753,
FT                                ECO:0000269|PubMed:21172655}.
FT   MOD_RES     122    122       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     130    130       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753,
FT                                ECO:0000244|PubMed:23806337}.
FT   MOD_RES     130    130       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     202    202       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MUTAGEN     122    122       K->R: Reverses IR-Induced increases in
FT                                superoxide and genomic Instability in
FT                                SIRT3-deficient mice.
FT                                {ECO:0000269|PubMed:21172655}.
FT   CONFLICT      5      5       A -> G (in Ref. 5; AAH18173).
FT                                {ECO:0000305}.
FT   CONFLICT     18     18       G -> V (in Ref. 1; CAA28645).
FT                                {ECO:0000305}.
FT   CONFLICT    138    138       V -> M (in Ref. 1 and 3). {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
//
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