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P09671

- SODM_MOUSE

UniProt

P09671 - SODM_MOUSE

Protein

Superoxide dismutase [Mn], mitochondrial

Gene

Sod2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (15 Jul 1998)
      Previous versions | rss
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    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

    Binds 1 manganese 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

    1. DNA binding Source: Ensembl
    2. manganese ion binding Source: UniProtKB
    3. oxygen binding Source: Ensembl
    4. protein binding Source: IntAct
    5. superoxide dismutase activity Source: UniProtKB

    GO - Biological processi

    1. age-dependent response to oxidative stress Source: MGI
    2. age-dependent response to reactive oxygen species Source: UniProtKB
    3. apoptotic mitochondrial changes Source: MGI
    4. cellular response to ethanol Source: Ensembl
    5. detection of oxygen Source: MGI
    6. erythrophore differentiation Source: MGI
    7. glutathione metabolic process Source: MGI
    8. heart development Source: MGI
    9. hemopoiesis Source: MGI
    10. hydrogen peroxide biosynthetic process Source: Ensembl
    11. intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
    12. intrinsic apoptotic signaling pathway in response to oxidative stress Source: MGI
    13. iron ion homeostasis Source: MGI
    14. liver development Source: MGI
    15. locomotory behavior Source: MGI
    16. mitochondrion organization Source: MGI
    17. negative regulation of fat cell differentiation Source: MGI
    18. negative regulation of fibroblast proliferation Source: MGI
    19. negative regulation of neuron apoptotic process Source: Ensembl
    20. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: Ensembl
    21. neuron development Source: MGI
    22. oxygen homeostasis Source: Ensembl
    23. positive regulation of nitric oxide biosynthetic process Source: MGI
    24. post-embryonic development Source: MGI
    25. protein homotetramerization Source: Ensembl
    26. regulation of blood pressure Source: MGI
    27. regulation of catalytic activity Source: MGI
    28. regulation of mitochondrial membrane potential Source: MGI
    29. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    30. release of cytochrome c from mitochondria Source: MGI
    31. removal of superoxide radicals Source: MGI
    32. respiratory electron transport chain Source: MGI
    33. response to activity Source: MGI
    34. response to axon injury Source: MGI
    35. response to cadmium ion Source: Ensembl
    36. response to drug Source: Ensembl
    37. response to electrical stimulus Source: Ensembl
    38. response to gamma radiation Source: MGI
    39. response to hydrogen peroxide Source: MGI
    40. response to hyperoxia Source: MGI
    41. response to hypoxia Source: Ensembl
    42. response to L-ascorbic acid Source: Ensembl
    43. response to lipopolysaccharide Source: Ensembl
    44. response to manganese ion Source: Ensembl
    45. response to oxidative stress Source: MGI
    46. response to reactive oxygen species Source: MGI
    47. response to selenium ion Source: Ensembl
    48. response to silicon dioxide Source: Ensembl
    49. response to superoxide Source: MGI
    50. response to zinc ion Source: Ensembl
    51. superoxide anion generation Source: MGI
    52. superoxide metabolic process Source: UniProtKB
    53. vasodilation Source: MGI
    54. vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure Source: MGI

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_189141. 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: Chromosome 17

    Organism-specific databases

    MGIiMGI:98352. Sod2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: MGI
    2. mitochondrial nucleoid Source: Ensembl
    3. mitochondrion Source: MGI

    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.3 Publications

    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

    ArrayExpressiP09671.
    BgeeiP09671.
    CleanExiMM_SOD2.
    GenevestigatoriP09671.

    Interactioni

    Subunit structurei

    Homotetramer.

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi203388. 1 interaction.
    IntActiP09671. 5 interactions.
    MINTiMINT-1861884.

    Structurei

    3D structure databases

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

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0605.
    HOGENOMiHOG000013583.
    HOVERGENiHBG004451.
    InParanoidiP09671.
    KOiK04564.
    OMAiTERYTAC.
    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

    MLCRAACSTG RRLGPVAGAA GSRHKHSLPD LPYDYGALEP HINAQIMQLH    50
    HSKHHAAYVN NLNATEEKYH EALAKGDVTT QVALQPALKF NGGGHINHTI 100
    FWTNLSPKGG GEPKGELLEA IKRDFGSFEK FKEKLTAVSV GVQGSGWGWL 150
    GFNKEQGRLQ IAACSNQDPL QGTTGLIPLL GIDVWEHAYY LQYKNVRPDY 200
    LKAIWNVINW ENVTERYTAC KK 222
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS28399.1.
    PIRi I57023.
    RefSeqi NP_038699.2. NM_013671.3.
    UniGenei Mm.290876.

    3D structure databases

    ProteinModelPortali P09671.
    SMRi P09671. Positions 25-222.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203388. 1 interaction.
    IntActi P09671. 5 interactions.
    MINTi MINT-1861884.

    PTM databases

    PhosphoSitei P09671.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00109109.
    P09671.
    SWISS-2DPAGE P09671.

    Proteomic databases

    MaxQBi P09671.
    PaxDbi P09671.
    PRIDEi P09671.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000007012 ; ENSMUSP00000007012 ; ENSMUSG00000006818 .
    GeneIDi 20656.
    KEGGi mmu:20656.
    UCSCi uc008alv.1. mouse.

    Organism-specific databases

    CTDi 6648.
    MGIi MGI:98352. Sod2.

    Phylogenomic databases

    eggNOGi COG0605.
    HOGENOMi HOG000013583.
    HOVERGENi HBG004451.
    InParanoidi P09671.
    KOi K04564.
    OMAi TERYTAC.
    OrthoDBi EOG7FV3R5.
    PhylomeDBi P09671.
    TreeFami TF105132.

    Enzyme and pathway databases

    Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    ChiTaRSi SOD2. mouse.
    NextBioi 299085.
    PROi P09671.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09671.
    Bgeei P09671.
    CleanExi MM_SOD2.
    Genevestigatori P09671.

    Family and domain databases

    InterProi IPR001189. Mn/Fe_SOD.
    IPR019833. Mn/Fe_SOD_BS.
    IPR019832. Mn/Fe_SOD_C.
    IPR019831. Mn/Fe_SOD_N.
    [Graphical view ]
    PANTHERi PTHR11404. PTHR11404. 1 hit.
    Pfami PF02777. Sod_Fe_C. 1 hit.
    PF00081. Sod_Fe_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000349. SODismutase. 1 hit.
    PRINTSi PR01703. MNSODISMTASE.
    SUPFAMi SSF46609. SSF46609. 1 hit.
    SSF54719. SSF54719. 1 hit.
    PROSITEi PS00088. SOD_MN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 152 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