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Protein

Superoxide dismutase [Mn], mitochondrial

Gene

Sod2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Mn2+By similarityNote: Binds 1 Mn2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501ManganeseBy similarity
Metal bindingi98 – 981ManganeseBy similarity
Metal bindingi183 – 1831ManganeseBy similarity
Metal bindingi187 – 1871ManganeseBy similarity

GO - Molecular functioni

  • DNA binding Source: Ensembl
  • identical protein binding Source: MGI
  • manganese ion binding Source: UniProtKB
  • oxidoreductase activity Source: CACAO
  • oxygen binding Source: Ensembl
  • superoxide dismutase activity Source: UniProtKB

GO - Biological processi

  • age-dependent response to oxidative stress Source: MGI
  • age-dependent response to reactive oxygen species Source: UniProtKB
  • apoptotic mitochondrial changes Source: MGI
  • cellular response to ethanol Source: Ensembl
  • detection of oxygen Source: MGI
  • erythrophore differentiation Source: MGI
  • glutathione metabolic process Source: MGI
  • heart development Source: MGI
  • hemopoiesis Source: MGI
  • hydrogen peroxide biosynthetic process Source: Ensembl
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
  • intrinsic apoptotic signaling pathway in response to oxidative stress Source: MGI
  • iron ion homeostasis Source: MGI
  • liver development Source: MGI
  • locomotory behavior Source: MGI
  • mitochondrion organization Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of fat cell differentiation Source: MGI
  • negative regulation of fibroblast proliferation Source: MGI
  • negative regulation of neuron apoptotic process Source: MGI
  • negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: MGI
  • neuron development Source: MGI
  • oxygen homeostasis Source: MGI
  • positive regulation of nitric oxide biosynthetic process Source: MGI
  • post-embryonic development Source: MGI
  • protein homotetramerization Source: MGI
  • regulation of blood pressure Source: MGI
  • regulation of catalytic activity Source: MGI
  • regulation of mitochondrial membrane potential Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • release of cytochrome c from mitochondria Source: MGI
  • removal of superoxide radicals Source: MGI
  • respiratory electron transport chain Source: MGI
  • response to activity Source: MGI
  • response to axon injury Source: MGI
  • response to cadmium ion Source: Ensembl
  • response to cold Source: Ensembl
  • response to drug Source: Ensembl
  • response to electrical stimulus Source: Ensembl
  • response to gamma radiation Source: MGI
  • response to hydrogen peroxide Source: MGI
  • response to hyperoxia Source: MGI
  • response to hypoxia Source: Ensembl
  • response to immobilization stress Source: Ensembl
  • response to isolation stress Source: Ensembl
  • response to L-ascorbic acid Source: Ensembl
  • response to lipopolysaccharide Source: Ensembl
  • response to magnetism Source: Ensembl
  • response to manganese ion Source: Ensembl
  • response to oxidative stress Source: MGI
  • response to reactive oxygen species Source: MGI
  • response to selenium ion Source: Ensembl
  • response to silicon dioxide Source: Ensembl
  • response to superoxide Source: MGI
  • response to zinc ion Source: Ensembl
  • superoxide anion generation Source: MGI
  • superoxide metabolic process Source: UniProtKB
  • vasodilation Source: MGI
  • vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_308972. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn], mitochondrial (EC:1.15.1.1)
Gene namesi
Name:Sod2
Synonyms:Sod-2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:98352. Sod2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrial inner membrane Source: MGI
  • mitochondrial nucleoid Source: Ensembl
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi122 – 1221K → R: Reverses IR-Induced increases in superoxide and genomic Instability in SIRT3-deficient mice. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424MitochondrionAdd
BLAST
Chaini25 – 222198Superoxide dismutase [Mn], mitochondrialPRO_0000032871Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581Nitrated tyrosineBy similarity
Modified residuei68 – 681N6-acetyllysine; alternate1 Publication
Modified residuei68 – 681N6-succinyllysine; alternate1 Publication
Modified residuei75 – 751N6-acetyllysine; alternate1 Publication
Modified residuei75 – 751N6-succinyllysine; alternate1 Publication
Modified residuei114 – 1141N6-acetyllysine1 Publication
Modified residuei122 – 1221N6-acetyllysine; alternate2 Publications
Modified residuei122 – 1221N6-succinyllysine; alternate1 Publication
Modified residuei130 – 1301N6-acetyllysine; alternate2 Publications
Modified residuei130 – 1301N6-succinyllysine; alternate1 Publication
Modified residuei202 – 2021N6-acetyllysine1 Publication

Post-translational modificationi

Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity (By similarity).By similarity
Acetylation at Lys-122 decreases enzymatic activity. Deacetylated by SIRT3 upon exposure to ionizing radiations or after long fasting.1 Publication

Keywords - PTMi

Acetylation, Nitration

Proteomic databases

MaxQBiP09671.
PaxDbiP09671.
PRIDEiP09671.

2D gel databases

REPRODUCTION-2DPAGEIPI00109109.
P09671.
SWISS-2DPAGEP09671.

PTM databases

PhosphoSiteiP09671.

Expressioni

Inductioni

Expression is regulated by KRIT1.1 Publication

Gene expression databases

BgeeiP09671.
CleanExiMM_SOD2.
ExpressionAtlasiP09671. baseline and differential.
GenevisibleiP09671. MM.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
PolgP540992EBI-1635071,EBI-863636
Tp53P023402EBI-1635071,EBI-474016

Protein-protein interaction databases

BioGridi203388. 2 interactions.
IntActiP09671. 5 interactions.
MINTiMINT-1861884.
STRINGi10090.ENSMUSP00000007012.

Structurei

3D structure databases

ProteinModelPortaliP09671.
SMRiP09671. Positions 25-222.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0605.
GeneTreeiENSGT00390000011877.
HOGENOMiHOG000013583.
HOVERGENiHBG004451.
InParanoidiP09671.
KOiK04564.
OMAiGTEWAEW.
OrthoDBiEOG7FV3R5.
PhylomeDBiP09671.
TreeFamiTF105132.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09671-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLCRAACSTG RRLGPVAGAA GSRHKHSLPD LPYDYGALEP HINAQIMQLH
60 70 80 90 100
HSKHHAAYVN NLNATEEKYH EALAKGDVTT QVALQPALKF NGGGHINHTI
110 120 130 140 150
FWTNLSPKGG GEPKGELLEA IKRDFGSFEK FKEKLTAVSV GVQGSGWGWL
160 170 180 190 200
GFNKEQGRLQ IAACSNQDPL QGTTGLIPLL GIDVWEHAYY LQYKNVRPDY
210 220
LKAIWNVINW ENVTERYTAC KK
Length:222
Mass (Da):24,603
Last modified:July 15, 1998 - v3
Checksum:i9AE804C55A8357D9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51A → G in AAH18173 (PubMed:16141072).Curated
Sequence conflicti18 – 181G → V in CAA28645 (PubMed:3797253).Curated
Sequence conflicti138 – 1381V → M (PubMed:3797253).Curated
Sequence conflicti138 – 1381V → M (PubMed:7875582).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04972 mRNA. Translation: CAA28645.1.
Z18857 mRNA. Translation: CAA79308.1.
L35528
, L35525, L35526, L35527 Genomic DNA. Translation: AAB60902.1.
S78846
, S78832, S78842, S78844 Genomic DNA. Translation: AAB34899.1.
AK002428 mRNA. Translation: BAB22095.1.
AK002534 mRNA. Translation: BAB22170.1.
AK012354 mRNA. Translation: BAB28183.1.
BC010548 mRNA. Translation: AAH10548.1.
BC018173 mRNA. Translation: AAH18173.1.
CCDSiCCDS28399.1.
PIRiI57023.
RefSeqiNP_038699.2. NM_013671.3.
UniGeneiMm.290876.

Genome annotation databases

EnsembliENSMUST00000007012; ENSMUSP00000007012; ENSMUSG00000006818.
GeneIDi20656.
KEGGimmu:20656.
UCSCiuc008alv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04972 mRNA. Translation: CAA28645.1.
Z18857 mRNA. Translation: CAA79308.1.
L35528
, L35525, L35526, L35527 Genomic DNA. Translation: AAB60902.1.
S78846
, S78832, S78842, S78844 Genomic DNA. Translation: AAB34899.1.
AK002428 mRNA. Translation: BAB22095.1.
AK002534 mRNA. Translation: BAB22170.1.
AK012354 mRNA. Translation: BAB28183.1.
BC010548 mRNA. Translation: AAH10548.1.
BC018173 mRNA. Translation: AAH18173.1.
CCDSiCCDS28399.1.
PIRiI57023.
RefSeqiNP_038699.2. NM_013671.3.
UniGeneiMm.290876.

3D structure databases

ProteinModelPortaliP09671.
SMRiP09671. Positions 25-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203388. 2 interactions.
IntActiP09671. 5 interactions.
MINTiMINT-1861884.
STRINGi10090.ENSMUSP00000007012.

PTM databases

PhosphoSiteiP09671.

2D gel databases

REPRODUCTION-2DPAGEIPI00109109.
P09671.
SWISS-2DPAGEP09671.

Proteomic databases

MaxQBiP09671.
PaxDbiP09671.
PRIDEiP09671.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000007012; ENSMUSP00000007012; ENSMUSG00000006818.
GeneIDi20656.
KEGGimmu:20656.
UCSCiuc008alv.1. mouse.

Organism-specific databases

CTDi6648.
MGIiMGI:98352. Sod2.

Phylogenomic databases

eggNOGiCOG0605.
GeneTreeiENSGT00390000011877.
HOGENOMiHOG000013583.
HOVERGENiHBG004451.
InParanoidiP09671.
KOiK04564.
OMAiGTEWAEW.
OrthoDBiEOG7FV3R5.
PhylomeDBiP09671.
TreeFamiTF105132.

Enzyme and pathway databases

ReactomeiREACT_308972. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiSod2. mouse.
NextBioi299085.
PROiP09671.
SOURCEiSearch...

Gene expression databases

BgeeiP09671.
CleanExiMM_SOD2.
ExpressionAtlasiP09671. baseline and differential.
GenevisibleiP09671. MM.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a cDNA coding for mouse manganese superoxide dismutase."
    Hallewell R.A., Mullenbach G.T., Stempien M.M., Bell G.I.
    Nucleic Acids Res. 14:9539-9539(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  2. "Sequence of manganese superoxide dismutase-encoding cDNAs from multiple mouse organs."
    Sun Y., Hegamyer G., Colburn N.M.
    Gene 131:301-302(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c and C3H.
  3. "Cloning and characterization of the murine manganous superoxide dismutase-encoding gene."
    Jones P.L., Kucera G., Gordon H.M., Boss J.M.
    Gene 153:155-161(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Structure and DNA sequence of the mouse MnSOD gene."
    Disilvestre D., Kleeberger S.R., Johns J., Levitt R.C.
    Mamm. Genome 6:281-284(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Kidney.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary gland.
  7. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 54-68; 76-108; 115-130 AND 203-216, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  8. "Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress."
    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.
    Mol. Cell 40:893-904(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-122, DEACETYLATION BY SIRT3, MUTAGENESIS OF LYS-122.
  9. "KRIT1 regulates the homeostasis of intracellular reactive oxygen species."
    Goitre L., Balzac F., Degani S., Degan P., Marchi S., Pinton P., Retta S.F.
    PLoS ONE 5:E11786-E11786(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    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.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-130, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-75; LYS-122 AND LYS-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  11. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-75; LYS-114; LYS-122; LYS-130 AND LYS-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSODM_MOUSE
AccessioniPrimary (citable) accession number: P09671
Secondary accession number(s): Q64670, Q8VEM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 15, 1998
Last modified: July 22, 2015
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.