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Protein

Superoxide dismutase [Cu-Zn]

Gene

Sod

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

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

Protein has several cofactor binding sites:
  • Cu cationNote: Binds 1 copper ion per subunit.
  • Zn2+Note: 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: GO_Central
  3. protein homodimerization activity Source: FlyBase
  4. superoxide dismutase activity Source: FlyBase
  5. zinc ion binding Source: GO_Central

GO - Biological processi

  1. age-dependent response to oxidative stress Source: FlyBase
  2. aging Source: FlyBase
  3. determination of adult lifespan Source: FlyBase
  4. regulation of mitochondrion degradation Source: FlyBase
  5. removal of superoxide radicals Source: GOC
  6. response to oxidative stress Source: FlyBase
Complete GO annotation...

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
Complete GO annotation...

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.
ExpressionAtlasiP61851. differential.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi64623. 52 interactions.
IntActiP61851. 3 interactions.
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

        10         20         30         40         50
MVVKAVCVIN GDAKGTVFFE QESSGTPVKV SGEVCGLAKG LHGFHVHEFG
60 70 80 90 100
DNTNGCMSSG PHFNPYGKEH GAPVDENRHL GDLGNIEATG DCPTKVNITD
110 120 130 140 150
SKITLFGADS IIGRTVVVHA DADDLGQGGH ELSKSTGNAG ARIGCGVIGI

AKV
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi64623. 52 interactions.
IntActiP61851. 3 interactions.
MINTiMINT-280564.

Proteomic databases

PaxDbiP61851.
PRIDEiP61851.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi39251.
FlyBaseiFBgn0003462. Sod.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_209269. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

GenomeRNAii39251.
NextBioi812705.
PROiP61851.

Gene expression databases

BgeeiP61851.
ExpressionAtlasiP61851. differential.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 100 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

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.