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P61851

- SODC_DROME

UniProt

P61851 - SODC_DROME

Protein

Superoxide dismutase [Cu-Zn]

Gene

Sod

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Destroys 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 copper ion per subunit.
    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi45 – 451Copper; catalytic
    Metal bindingi47 – 471Copper; catalytic
    Metal bindingi62 – 621Copper; catalytic
    Metal bindingi62 – 621Zinc; structural
    Metal bindingi70 – 701Zinc; structural
    Metal bindingi79 – 791Zinc; structural
    Metal bindingi82 – 821Zinc; structural
    Metal bindingi119 – 1191Copper; catalytic

    GO - Molecular functioni

    1. antioxidant activity Source: FlyBase
    2. copper ion binding Source: RefGenome
    3. protein homodimerization activity Source: FlyBase
    4. superoxide dismutase activity Source: FlyBase
    5. zinc ion binding Source: RefGenome

    GO - Biological processi

    1. aging Source: FlyBase
    2. determination of adult lifespan Source: FlyBase
    3. removal of superoxide radicals Source: GOC
    4. response to oxidative stress Source: FlyBase

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_209269. Detoxification of Reactive Oxygen Species.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
    Gene namesi
    Name:Sod
    ORF Names:CG11793
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0003462. Sod.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: FlyBase
    2. peroxisome Source: FlyBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 153152Superoxide dismutase [Cu-Zn]PRO_0000164085Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531Phosphothreonine1 Publication
    Disulfide bondi56 ↔ 145
    Modified residuei59 – 591Phosphoserine1 Publication

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    PaxDbiP61851.
    PRIDEiP61851.

    Expressioni

    Gene expression databases

    BgeeiP61851.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi64623. 52 interactions.
    IntActiP61851. 1 interaction.
    MINTiMINT-280564.

    Structurei

    3D structure databases

    ProteinModelPortaliP61851.
    SMRiP61851. Positions 4-153.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Cu-Zn superoxide dismutase family.Curated

    Phylogenomic databases

    eggNOGiCOG2032.
    GeneTreeiENSGT00530000063226.
    InParanoidiP61851.
    KOiK04565.
    OrthoDBiEOG776SR4.
    PhylomeDBiP61851.

    Family and domain databases

    Gene3Di2.60.40.200. 1 hit.
    InterProiIPR018152. SOD_Cu/Zn_BS.
    IPR001424. SOD_Cu_Zn_dom.
    [Graphical view]
    PfamiPF00080. Sod_Cu. 1 hit.
    [Graphical view]
    PRINTSiPR00068. CUZNDISMTASE.
    SUPFAMiSSF49329. SSF49329. 1 hit.
    PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
    PS00332. SOD_CU_ZN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P61851-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVVKAVCVIN GDAKGTVFFE QESSGTPVKV SGEVCGLAKG LHGFHVHEFG    50
    DNTNGCMSSG PHFNPYGKEH GAPVDENRHL GDLGNIEATG DCPTKVNITD 100
    SKITLFGADS IIGRTVVVHA DADDLGQGGH ELSKSTGNAG ARIGCGVIGI 150
    AKV 153
    Length:153
    Mass (Da):15,699
    Last modified:January 23, 2007 - v2
    Checksum:i4A6AAAA1EB545E70
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti97 – 971N → K in CAA35210. (PubMed:2493630)Curated
    Sequence conflicti97 – 971N → K in AAD14963. (PubMed:8013910)Curated
    Sequence conflicti97 – 971N → K in AAA28905. (PubMed:3128462)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00367 mRNA. Translation: CAA68443.1.
    Z19591 Genomic DNA. Translation: CAA79639.1.
    M24421 Genomic DNA. Translation: AAA28906.1.
    X13780 Genomic DNA. Translation: CAA32028.1.
    X17332 Genomic DNA. Translation: CAA35210.1.
    AE014296 Genomic DNA. Translation: AAF50095.1.
    AY071435 mRNA. Translation: AAL49057.1.
    S72589 Genomic DNA. Translation: AAD14963.2.
    M18823 Genomic DNA. Translation: AAA28905.1.
    PIRiS02725. DSFFCZ.
    RefSeqiNP_476735.1. NM_057387.5.
    UniGeneiDm.926.

    Genome annotation databases

    EnsemblMetazoaiFBtr0076229; FBpp0075958; FBgn0003462.
    GeneIDi39251.
    KEGGidme:Dmel_CG11793.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00367 mRNA. Translation: CAA68443.1 .
    Z19591 Genomic DNA. Translation: CAA79639.1 .
    M24421 Genomic DNA. Translation: AAA28906.1 .
    X13780 Genomic DNA. Translation: CAA32028.1 .
    X17332 Genomic DNA. Translation: CAA35210.1 .
    AE014296 Genomic DNA. Translation: AAF50095.1 .
    AY071435 mRNA. Translation: AAL49057.1 .
    S72589 Genomic DNA. Translation: AAD14963.2 .
    M18823 Genomic DNA. Translation: AAA28905.1 .
    PIRi S02725. DSFFCZ.
    RefSeqi NP_476735.1. NM_057387.5.
    UniGenei Dm.926.

    3D structure databases

    ProteinModelPortali P61851.
    SMRi P61851. Positions 4-153.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 64623. 52 interactions.
    IntActi P61851. 1 interaction.
    MINTi MINT-280564.

    Proteomic databases

    PaxDbi P61851.
    PRIDEi P61851.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0076229 ; FBpp0075958 ; FBgn0003462 .
    GeneIDi 39251.
    KEGGi dme:Dmel_CG11793.

    Organism-specific databases

    CTDi 39251.
    FlyBasei FBgn0003462. Sod.

    Phylogenomic databases

    eggNOGi COG2032.
    GeneTreei ENSGT00530000063226.
    InParanoidi P61851.
    KOi K04565.
    OrthoDBi EOG776SR4.
    PhylomeDBi P61851.

    Enzyme and pathway databases

    Reactomei REACT_209269. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    GenomeRNAii 39251.
    NextBioi 812705.
    PROi P61851.

    Gene expression databases

    Bgeei P61851.

    Family and domain databases

    Gene3Di 2.60.40.200. 1 hit.
    InterProi IPR018152. SOD_Cu/Zn_BS.
    IPR001424. SOD_Cu_Zn_dom.
    [Graphical view ]
    Pfami PF00080. Sod_Cu. 1 hit.
    [Graphical view ]
    PRINTSi PR00068. CUZNDISMTASE.
    SUPFAMi SSF49329. SSF49329. 1 hit.
    PROSITEi PS00087. SOD_CU_ZN_1. 1 hit.
    PS00332. SOD_CU_ZN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Drosophila Cu-Zn superoxide dismutase cDNA sequence."
      Seto N.O.L., Hayashi S., Tener G.M.
      Nucleic Acids Res. 15:5483-5483(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The sequence of the Cu-Zn superoxide dismutase gene of Drosophila."
      Seto N.O.L., Hayashi S., Tener G.M.
      Nucleic Acids Res. 15:10601-10601(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning, sequence analysis and chromosomal localization of the Cu-Zn superoxide dismutase gene of Drosophila melanogaster."
      Seto N.O., Hayashi S., Tener G.M.
      Gene 75:85-92(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Drosophila melanogaster Cu,Zn superoxide dismutase gene sequence."
      Kwiatowski J., Patel M., Ayala F.J.
      Nucleic Acids Res. 17:1264-1264(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Canton-S.
    5. Phillips J.P.
      Submitted (DEC-1989) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: Canton-S.
    6. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    7. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    9. Cited for: PROTEIN SEQUENCE OF 2-153.
    10. "Complete amino acid sequence of copper-zinc superoxide dismutase from Drosophila melanogaster."
      Lee Y.M., Friedman D.J., Ayala F.J.
      Arch. Biochem. Biophys. 241:577-589(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-153.
    11. "Evidence for positive selection in the superoxide dismutase (Sod) region of Drosophila melanogaster."
      Hudson R.R., Bailey K., Skarecky D., Kwiatowski J., Ayala F.J.
      Genetics 136:1329-1340(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-153.
    12. "Isolation and chromosomal localization of genomic DNA sequences coding for cytoplasmic superoxide dismutase from Drosophila melanogaster."
      Kirkland K.C., Phillips J.P.
      Gene 61:415-419(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 91-122.
      Strain: Canton-S.
    13. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
      Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
      Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53 AND SER-59, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiSODC_DROME
    AccessioniPrimary (citable) accession number: P61851
    Secondary accession number(s): P00444, Q27770, Q9VTF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 96 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3