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P09671 (SODM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Superoxide dismutase [Mn], mitochondrial

EC=1.15.1.1
Gene names
Name:Sod2
Synonyms:Sod-2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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+ = O2 + H2O2.

Cofactor

Binds 1 manganese ion per subunit By similarity.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion matrix.

Induction

Expression is regulated by KRIT1. Ref.9

Post-translational modification

Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity By similarity.

Acetylation at Lys-122 decreases enzymatic activity. Deacetylated by SIRT3 upon exposure to ionizing radiations or after long fasting. Ref.8

Sequence similarities

Belongs to the iron/manganese superoxide dismutase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandManganese
Metal-binding
   Molecular functionOxidoreductase
   PTMAcetylation
Nitration
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processage-dependent response to oxidative stress

Inferred from mutant phenotype PubMed 11226230. Source: MGI

age-dependent response to reactive oxygen species

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic mitochondrial changes

Inferred from mutant phenotype PubMed 11226230. Source: MGI

cellular response to ethanol

Inferred from electronic annotation. Source: Ensembl

detection of oxygen

Inferred from mutant phenotype PubMed 11156968. Source: MGI

erythrophore differentiation

Inferred from mutant phenotype PubMed 15205258. Source: MGI

glutathione metabolic process

Inferred from mutant phenotype PubMed 10049502. Source: MGI

heart development

Inferred from mutant phenotype PubMed 7493016. Source: MGI

hemopoiesis

Inferred from mutant phenotype PubMed 16219542PubMed 8790408. Source: MGI

hydrogen peroxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from mutant phenotype PubMed 15642323. Source: MGI

intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from mutant phenotype PubMed 15642323. Source: MGI

iron ion homeostasis

Inferred from mutant phenotype PubMed 15205258. Source: MGI

liver development

Inferred from mutant phenotype PubMed 17367743. Source: MGI

locomotory behavior

Inferred from mutant phenotype PubMed 8790408. Source: MGI

mitochondrion organization

Inferred from mutant phenotype PubMed 11527927PubMed 15205258PubMed 8790408. Source: MGI

negative regulation of fat cell differentiation

Inferred from mutant phenotype PubMed 16219542. Source: MGI

negative regulation of fibroblast proliferation

Inferred from direct assay PubMed 18218638. Source: MGI

negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

neuron development

Inferred from mutant phenotype PubMed 8790408. Source: MGI

oxygen homeostasis

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from mutant phenotype PubMed 15637112. Source: MGI

post-embryonic development

Inferred from mutant phenotype PubMed 7493016PubMed 8790408. Source: MGI

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

regulation of blood pressure

Inferred from mutant phenotype PubMed 17023572. Source: MGI

regulation of catalytic activity

Inferred from mutant phenotype PubMed 9927656. Source: MGI

regulation of mitochondrial membrane potential

Inferred from mutant phenotype PubMed 17367743. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

release of cytochrome c from mitochondria

Inferred from mutant phenotype PubMed 10212301PubMed 15642323. Source: MGI

removal of superoxide radicals

Inferred from mutant phenotype PubMed 16873728. Source: MGI

respiratory electron transport chain

Inferred from mutant phenotype PubMed 11226230PubMed 19478076. Source: MGI

response to L-ascorbic acid

Inferred from electronic annotation. Source: Ensembl

response to activity

Inferred from mutant phenotype PubMed 15781740. Source: MGI

response to axon injury

Inferred from mutant phenotype PubMed 16677818. Source: MGI

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

response to gamma radiation

Inferred from genetic interaction PubMed 15182862. Source: MGI

response to hydrogen peroxide

Inferred from mutant phenotype PubMed 15642323. Source: MGI

response to hyperoxia

Inferred from mutant phenotype PubMed 11796207. Source: MGI

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to manganese ion

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from mutant phenotype PubMed 15182862PubMed 19478076. Source: MGI

response to reactive oxygen species

Inferred from mutant phenotype PubMed 15205258PubMed 16219542PubMed 17145560PubMed 9462746PubMed 9927656. Source: MGI

response to selenium ion

Inferred from electronic annotation. Source: Ensembl

response to silicon dioxide

Inferred from electronic annotation. Source: Ensembl

response to superoxide

Inferred from mutant phenotype PubMed 11156968PubMed 15642323. Source: MGI

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

superoxide anion generation

Inferred from mutant phenotype PubMed 10212301PubMed 15781740PubMed 16677818. Source: MGI

superoxide metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

vasodilation

Inferred from mutant phenotype PubMed 15637112. Source: MGI

vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure

Inferred from mutant phenotype PubMed 16873728. Source: MGI

   Cellular_componentmitochondrial inner membrane

Inferred from direct assay PubMed 12865426. Source: MGI

mitochondrial nucleoid

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay PubMed 11583975PubMed 12931191PubMed 14651853PubMed 16103131PubMed 17597094PubMed 18614015PubMed 22474353. Source: MGI

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: Ensembl

manganese ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

oxygen binding

Inferred from electronic annotation. Source: Ensembl

superoxide dismutase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2424Mitochondrion
Chain25 – 222198Superoxide dismutase [Mn], mitochondrial
PRO_0000032871

Sites

Metal binding501Manganese By similarity
Metal binding981Manganese By similarity
Metal binding1831Manganese By similarity
Metal binding1871Manganese By similarity

Amino acid modifications

Modified residue581Nitrated tyrosine By similarity
Modified residue681N6-acetyllysine; alternate Ref.11
Modified residue681N6-succinyllysine; alternate Ref.10
Modified residue751N6-acetyllysine; alternate Ref.11
Modified residue751N6-succinyllysine; alternate Ref.10
Modified residue1141N6-acetyllysine Ref.11
Modified residue1221N6-acetyllysine; alternate Ref.8 Ref.11
Modified residue1221N6-succinyllysine; alternate Ref.10
Modified residue1301N6-acetyllysine; alternate Ref.10 Ref.11
Modified residue1301N6-succinyllysine; alternate Ref.10
Modified residue2021N6-acetyllysine Ref.11

Experimental info

Mutagenesis1221K → R: Reverses IR-Induced increases in superoxide and genomic Instability in SIRT3-deficient mice. Ref.8
Sequence conflict51A → G in AAH18173. Ref.5
Sequence conflict181G → V in CAA28645. Ref.1
Sequence conflict1381V → M Ref.1
Sequence conflict1381V → M Ref.3

Sequences

Sequence LengthMass (Da)Tools
P09671 [UniParc].

Last modified July 15, 1998. Version 3.
Checksum: 9AE804C55A8357D9

FASTA22224,603
        10         20         30         40         50         60 
MLCRAACSTG RRLGPVAGAA GSRHKHSLPD LPYDYGALEP HINAQIMQLH HSKHHAAYVN 

        70         80         90        100        110        120 
NLNATEEKYH EALAKGDVTT QVALQPALKF NGGGHINHTI FWTNLSPKGG GEPKGELLEA 

       130        140        150        160        170        180 
IKRDFGSFEK FKEKLTAVSV GVQGSGWGWL GFNKEQGRLQ IAACSNQDPL QGTTGLIPLL 

       190        200        210        220 
GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVTERYTAC KK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04972 mRNA. Translation: CAA28645.1.
Z18857 mRNA. Translation: CAA79308.1.
L35528 expand/collapse EMBL AC list , L35525, L35526, L35527 Genomic DNA. Translation: AAB60902.1.
S78846 expand/collapse EMBL AC list , 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.
PIRI57023.
RefSeqNP_038699.2. NM_013671.3.
UniGeneMm.290876.

3D structure databases

ProteinModelPortalP09671.
SMRP09671. Positions 25-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203388. 1 interaction.
IntActP09671. 5 interactions.
MINTMINT-1861884.

PTM databases

PhosphoSiteP09671.

2D gel databases

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

Proteomic databases

PaxDbP09671.
PRIDEP09671.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000007012; ENSMUSP00000007012; ENSMUSG00000006818.
GeneID20656.
KEGGmmu:20656.
UCSCuc008alv.1. mouse.

Organism-specific databases

CTD6648.
MGIMGI:98352. Sod2.

Phylogenomic databases

eggNOGCOG0605.
HOGENOMHOG000013583.
HOVERGENHBG004451.
InParanoidP09671.
KOK04564.
OMAEQVYDHQ.
OrthoDBEOG7FV3R5.
PhylomeDBP09671.
TreeFamTF105132.

Gene expression databases

ArrayExpressP09671.
BgeeP09671.
CleanExMM_SOD2.
GenevestigatorP09671.

Family and domain databases

InterProIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERPTHR11404. PTHR11404. 1 hit.
PfamPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFPIRSF000349. SODismutase. 1 hit.
PRINTSPR01703. MNSODISMTASE.
SUPFAMSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSOD2. mouse.
NextBio299085.
PROP09671.
SOURCESearch...

Entry information

Entry nameSODM_MOUSE
AccessionPrimary (citable) accession number: P09671
Secondary accession number(s): Q64670, Q8VEM5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot