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Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)

 SODM_MOUSE              Reviewed;         222 AA.
P09671; Q64670; Q8VEM5;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 3.
07-JUN-2017, entry version 180.
RecName: Full=Superoxide dismutase [Mn], mitochondrial;
EC=1.15.1.1;
Flags: Precursor;
Name=Sod2; Synonyms=Sod-2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=3797253; DOI=10.1093/nar/14.23.9539;
Hallewell R.A., Mullenbach G.T., Stempien M.M., Bell G.I.;
"Sequence of a cDNA coding for mouse manganese superoxide dismutase.";
Nucleic Acids Res. 14:9539-9539(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ, and C3H/HeJ;
PubMed=8406027; DOI=10.1016/0378-1119(93)90311-P;
Sun Y., Hegamyer G., Colburn N.M.;
"Sequence of manganese superoxide dismutase-encoding cDNAs from
multiple mouse organs.";
Gene 131:301-302(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7875582; DOI=10.1016/0378-1119(94)00666-G;
Jones P.L., Kucera G., Gordon H.M., Boss J.M.;
"Cloning and characterization of the murine manganous superoxide
dismutase-encoding gene.";
Gene 153:155-161(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7613035; DOI=10.1007/BF00352417;
Disilvestre D., Kleeberger S.R., Johns J., Levitt R.C.;
"Structure and DNA sequence of the mouse MnSOD gene.";
Mamm. Genome 6:281-284(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 54-68; 76-108; 115-130 AND 203-216, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
ACETYLATION AT LYS-122, DEACETYLATION BY SIRT3, AND MUTAGENESIS OF
LYS-122.
PubMed=21172655; DOI=10.1016/j.molcel.2010.12.013;
Tao R., Coleman M.C., Pennington J.D., Ozden O., Park S.H., Jiang H.,
Kim H.S., Flynn C.R., Hill S., Hayes McDonald W., Olivier A.K.,
Spitz D.R., Gius D.;
"Sirt3-mediated deacetylation of evolutionarily conserved lysine 122
regulates MnSOD activity in response to stress.";
Mol. Cell 40:893-904(2010).
[10]
INDUCTION.
PubMed=20668652; DOI=10.1371/journal.pone.0011786;
Goitre L., Balzac F., Degani S., Degan P., Marchi S., Pinton P.,
Retta S.F.;
"KRIT1 regulates the homeostasis of intracellular reactive oxygen
species.";
PLoS ONE 5:E11786-E11786(2010).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-130, SUCCINYLATION [LARGE
SCALE ANALYSIS] AT LYS-68; LYS-75; LYS-122 AND LYS-130, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast, and Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-75; LYS-114;
LYS-122; LYS-130 AND LYS-202, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
"Label-free quantitative proteomics of the lysine acetylome in
mitochondria identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
-!- FUNCTION: Destroys superoxide anion radicals which are normally
produced within the cells and which are toxic to biological
systems.
-!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
-!- SUBUNIT: Homotetramer.
-!- INTERACTION:
P54099:Polg; NbExp=2; IntAct=EBI-1635071, EBI-863636;
P02340:Tp53; NbExp=2; IntAct=EBI-1635071, EBI-474016;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- INDUCTION: Expression is regulated by KRIT1.
{ECO:0000269|PubMed:20668652}.
-!- PTM: Nitrated under oxidative stress. Nitration coupled with
oxidation inhibits the catalytic activity (By similarity).
{ECO:0000250}.
-!- PTM: Acetylation at Lys-122 decreases enzymatic activity.
Deacetylated by SIRT3 upon exposure to ionizing radiations or
after long fasting. {ECO:0000269|PubMed:21172655}.
-!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X04972; CAA28645.1; -; mRNA.
EMBL; Z18857; CAA79308.1; -; mRNA.
EMBL; L35528; AAB60902.1; -; Genomic_DNA.
EMBL; L35525; AAB60902.1; JOINED; Genomic_DNA.
EMBL; L35526; AAB60902.1; JOINED; Genomic_DNA.
EMBL; L35527; AAB60902.1; JOINED; Genomic_DNA.
EMBL; S78846; AAB34899.1; -; Genomic_DNA.
EMBL; S78832; AAB34899.1; JOINED; Genomic_DNA.
EMBL; S78842; AAB34899.1; JOINED; Genomic_DNA.
EMBL; S78844; AAB34899.1; JOINED; Genomic_DNA.
EMBL; AK002428; BAB22095.1; -; mRNA.
EMBL; AK002534; BAB22170.1; -; mRNA.
EMBL; AK012354; BAB28183.1; -; mRNA.
EMBL; BC010548; AAH10548.1; -; mRNA.
EMBL; BC018173; AAH18173.1; -; mRNA.
CCDS; CCDS28399.1; -.
PIR; I57023; I57023.
RefSeq; NP_038699.2; NM_013671.3.
UniGene; Mm.290876; -.
ProteinModelPortal; P09671; -.
SMR; P09671; -.
BioGrid; 203388; 2.
IntAct; P09671; 5.
MINT; MINT-1861884; -.
STRING; 10090.ENSMUSP00000007012; -.
iPTMnet; P09671; -.
PhosphoSitePlus; P09671; -.
SwissPalm; P09671; -.
REPRODUCTION-2DPAGE; IPI00109109; -.
REPRODUCTION-2DPAGE; P09671; -.
SWISS-2DPAGE; P09671; -.
EPD; P09671; -.
PaxDb; P09671; -.
PeptideAtlas; P09671; -.
PRIDE; P09671; -.
TopDownProteomics; P09671; -.
Ensembl; ENSMUST00000007012; ENSMUSP00000007012; ENSMUSG00000006818.
GeneID; 20656; -.
KEGG; mmu:20656; -.
UCSC; uc008alv.1; mouse.
CTD; 6648; -.
MGI; MGI:98352; Sod2.
eggNOG; KOG0876; Eukaryota.
eggNOG; COG0605; LUCA.
GeneTree; ENSGT00390000011877; -.
HOGENOM; HOG000013583; -.
HOVERGEN; HBG004451; -.
InParanoid; P09671; -.
KO; K04564; -.
OMA; KWGSFDK; -.
OrthoDB; EOG091G0MVL; -.
PhylomeDB; P09671; -.
TreeFam; TF105132; -.
Reactome; R-MMU-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
ChiTaRS; Sod2; mouse.
PRO; PR:P09671; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000006818; -.
CleanEx; MM_SOD2; -.
ExpressionAtlas; P09671; baseline and differential.
Genevisible; P09671; MM.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
GO; GO:0016491; F:oxidoreductase activity; IMP:CACAO.
GO; GO:0019825; F:oxygen binding; IEA:Ensembl.
GO; GO:0004784; F:superoxide dismutase activity; IDA:MGI.
GO; GO:0003069; P:acetylcholine-mediated vasodilation involved in regulation of systemic arterial blood pressure; IMP:MGI.
GO; GO:0001306; P:age-dependent response to oxidative stress; IMP:MGI.
GO; GO:0001315; P:age-dependent response to reactive oxygen species; ISS:UniProtKB.
GO; GO:0008637; P:apoptotic mitochondrial changes; IMP:MGI.
GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
GO; GO:0003032; P:detection of oxygen; IMP:MGI.
GO; GO:0048773; P:erythrophore differentiation; IMP:MGI.
GO; GO:0006749; P:glutathione metabolic process; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0030097; P:hemopoiesis; IMP:MGI.
GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:MGI.
GO; GO:0055072; P:iron ion homeostasis; IMP:MGI.
GO; GO:0001889; P:liver development; IMP:MGI.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:MGI.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0048666; P:neuron development; IMP:MGI.
GO; GO:0032364; P:oxygen homeostasis; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:MGI.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
GO; GO:0050790; P:regulation of catalytic activity; IMP:MGI.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IMP:MGI.
GO; GO:0019430; P:removal of superoxide radicals; IMP:MGI.
GO; GO:0022904; P:respiratory electron transport chain; IMP:MGI.
GO; GO:0014823; P:response to activity; IMP:MGI.
GO; GO:0048678; P:response to axon injury; IMP:MGI.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0009409; P:response to cold; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
GO; GO:0010332; P:response to gamma radiation; IGI:MGI.
GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
GO; GO:0055093; P:response to hyperoxia; IMP:MGI.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
GO; GO:0035900; P:response to isolation stress; IEA:Ensembl.
GO; GO:0033591; P:response to L-ascorbic acid; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071000; P:response to magnetism; IEA:Ensembl.
GO; GO:0010042; P:response to manganese ion; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
GO; GO:0000302; P:response to reactive oxygen species; IMP:MGI.
GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
GO; GO:0034021; P:response to silicon dioxide; IEA:Ensembl.
GO; GO:0000303; P:response to superoxide; IMP:MGI.
GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
GO; GO:0042554; P:superoxide anion generation; IMP:MGI.
GO; GO:0006801; P:superoxide metabolic process; IMP:MGI.
GO; GO:0042311; P:vasodilation; IMP:MGI.
InterPro; IPR001189; Mn/Fe_SOD.
InterPro; IPR019833; Mn/Fe_SOD_BS.
InterPro; IPR019832; Mn/Fe_SOD_C.
InterPro; IPR019831; Mn/Fe_SOD_N.
Pfam; PF02777; Sod_Fe_C; 1.
Pfam; PF00081; Sod_Fe_N; 1.
PIRSF; PIRSF000349; SODismutase; 1.
PRINTS; PR01703; MNSODISMTASE.
SUPFAM; SSF46609; SSF46609; 1.
SUPFAM; SSF54719; SSF54719; 1.
PROSITE; PS00088; SOD_MN; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing; Manganese;
Metal-binding; Mitochondrion; Nitration; Oxidoreductase;
Reference proteome; Transit peptide.
TRANSIT 1 24 Mitochondrion.
CHAIN 25 222 Superoxide dismutase [Mn], mitochondrial.
/FTId=PRO_0000032871.
METAL 50 50 Manganese. {ECO:0000250}.
METAL 98 98 Manganese. {ECO:0000250}.
METAL 183 183 Manganese. {ECO:0000250}.
METAL 187 187 Manganese. {ECO:0000250}.
MOD_RES 58 58 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P04179}.
MOD_RES 68 68 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 68 68 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 75 75 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 75 75 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 114 114 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 122 122 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753,
ECO:0000269|PubMed:21172655}.
MOD_RES 122 122 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 130 130 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753,
ECO:0000244|PubMed:23806337}.
MOD_RES 130 130 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 202 202 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MUTAGEN 122 122 K->R: Reverses IR-Induced increases in
superoxide and genomic Instability in
SIRT3-deficient mice.
{ECO:0000269|PubMed:21172655}.
CONFLICT 5 5 A -> G (in Ref. 5; AAH18173).
{ECO:0000305}.
CONFLICT 18 18 G -> V (in Ref. 1; CAA28645).
{ECO:0000305}.
CONFLICT 138 138 V -> M (in Ref. 1 and 3). {ECO:0000305}.
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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