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P61851 (SODC_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Superoxide dismutase [Cu-Zn]

EC=1.15.1.1
Gene names
Name:Sod
ORF Names:CG11793
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Destroys 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 copper ion per subunit.

Binds 1 zinc ion per subunit.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9 Ref.10
Chain2 – 153152Superoxide dismutase [Cu-Zn]
PRO_0000164085

Sites

Metal binding451Copper; catalytic
Metal binding471Copper; catalytic
Metal binding621Copper; catalytic
Metal binding621Zinc; structural
Metal binding701Zinc; structural
Metal binding791Zinc; structural
Metal binding821Zinc; structural
Metal binding1191Copper; catalytic

Amino acid modifications

Modified residue531Phosphothreonine Ref.13
Modified residue591Phosphoserine Ref.13
Disulfide bond56 ↔ 145

Experimental info

Sequence conflict971N → K in CAA35210. Ref.4
Sequence conflict971N → K in AAD14963. Ref.11
Sequence conflict971N → K in AAA28905. Ref.12

Sequences

Sequence LengthMass (Da)Tools
P61851 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 4A6AAAA1EB545E70

FASTA15315,699
        10         20         30         40         50         60 
MVVKAVCVIN GDAKGTVFFE QESSGTPVKV SGEVCGLAKG LHGFHVHEFG DNTNGCMSSG 

        70         80         90        100        110        120 
PHFNPYGKEH GAPVDENRHL GDLGNIEATG DCPTKVNITD SKITLFGADS IIGRTVVVHA 

       130        140        150 
DADDLGQGGH ELSKSTGNAG ARIGCGVIGI AKV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[8]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[9]"Superoxide dismutase: an evolutionary puzzle."
Lee Y.M., Friedman D.J., Ayala F.J.
Proc. Natl. Acad. Sci. U.S.A. 82:824-828(1985) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRDSFFCZ. S02725.
RefSeqNP_476735.1. NM_057387.5.
UniGeneDm.926.

3D structure databases

ProteinModelPortalP61851.
SMRP61851. Positions 4-153.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid64623. 52 interactions.
IntActP61851. 1 interaction.
MINTMINT-280564.

Proteomic databases

PaxDbP61851.
PRIDEP61851.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0076229; FBpp0075958; FBgn0003462.
GeneID39251.
KEGGdme:Dmel_CG11793.

Organism-specific databases

CTD39251.
FlyBaseFBgn0003462. Sod.

Phylogenomic databases

eggNOGCOG2032.
GeneTreeENSGT00530000063226.
InParanoidP61851.
KOK04565.
OrthoDBEOG776SR4.
PhylomeDBP61851.

Gene expression databases

BgeeP61851.

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
SUPFAMSSF49329. SSF49329. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi39251.
NextBio812705.
PROP61851.

Entry information

Entry nameSODC_DROME
AccessionPrimary (citable) accession number: P61851
Secondary accession number(s): P00444, Q27770, Q9VTF6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase