P61851 (SODC_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Cu-Zn]
EC=1.15.1.1

Gene names

Name:	Sod
ORF Names:	CG11793

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	153 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Disulfide bond Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	determination of adult lifespan Inferred from mutant phenotype PubMed 11707932PubMed 18508973PubMed 9858546. Source: FlyBase response to oxidative stress Inferred from mutant phenotype PubMed 18508973. Source: FlyBase superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome mitochondrion Inferred from Biological aspect of Ancestor. Source: RefGenome nucleus Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	antioxidant activity Non-traceable author statement PubMed 12539239. Source: FlyBase copper ion binding Inferred from Biological aspect of Ancestor. Source: RefGenome superoxide dismutase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.9 Ref.10
	Chain	2 – 153	152	Superoxide dismutase [Cu-Zn]		PRO_0000164085
Sites
	Metal binding	45	1	Copper; catalytic
	Metal binding	47	1	Copper; catalytic
	Metal binding	62	1	Copper; catalytic
	Metal binding	62	1	Zinc; structural
	Metal binding	70	1	Zinc; structural
	Metal binding	79	1	Zinc; structural
	Metal binding	82	1	Zinc; structural
	Metal binding	119	1	Copper; catalytic
Amino acid modifications
	Modified residue	53	1	Phosphothreonine Ref.13
	Modified residue	59	1	Phosphoserine Ref.13
	Disulfide bond	56 ↔ 145
Experimental info
	Sequence conflict	97	1	N → K in CAA35210. Ref.4
	Sequence conflict	97	1	N → K in AAD14963. Ref.11
	Sequence conflict	97	1	N → K in AAA28905. Ref.12

Sequences

	Sequence		Length	Mass (Da)
	P61851 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 4A6AAAA1EB545E70	FASTA	153	15,699
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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.
PIR	DSFFCZ. S02725.
RefSeq	NP_476735.1. NM_057387.5.
UniGene	Dm.926.
3D structure databases
ProteinModelPortal	P61851.
SMR	P61851. Positions 4-153.
ModBase	Search...
Protein-protein interaction databases
IntAct	P61851. 1 interaction.
MINT	MINT-280564.
Proteomic databases
PaxDb	P61851.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0076229; FBpp0075958; FBgn0003462.
GeneID	39251.
KEGG	dme:Dmel_CG11793.
Organism-specific databases
CTD	39251.
FlyBase	FBgn0003462. Sod.
Phylogenomic databases
eggNOG	COG2032.
GeneTree	ENSGT00530000063226.
InParanoid	P61851.
KO	K04565.
OMA	APRFESS.
OrthoDB	EOG43TXBZ.
PhylomeDB	P61851.
Gene expression databases
Bgee	P61851.
GermOnline	CG11793. Drosophila melanogaster.
Family and domain databases
Gene3D	2.60.40.200. 1 hit.
InterPro	IPR024134. SOD_Cu/Zn_/chaperones. IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn_dom. [Graphical view]
PANTHER	PTHR10003. PTHR10003. 1 hit.
Pfam	PF00080. Sod_Cu. 1 hit. [Graphical view]
PRINTS	PR00068. CUZNDISMTASE.
SUPFAM	SSF49329. SOD_Cu_Zn. 1 hit.
PROSITE	PS00087. SOD_CU_ZN_1. 1 hit. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	39251.
NextBio	812705.

Entry information

Entry name

SODC_DROME

Accession

Primary (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:	April 3, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project