P61851 · SODC_DROME
- ProteinSuperoxide dismutase [Cu-Zn]
- GeneSod1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids153 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic activity
- 2 H+ + 2 superoxide = H2O2 + O2
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 copper ion per subunit.
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 45 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 47 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 62 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 62 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 70 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 79 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 82 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: D | ||||||
Binding site | 119 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | peroxisome | |
Molecular Function | copper ion binding | |
Molecular Function | protein homodimerization activity | |
Molecular Function | superoxide dismutase activity | |
Biological Process | determination of adult lifespan | |
Biological Process | positive regulation of mitophagy | |
Biological Process | regulation of synaptic plasticity | |
Biological Process | regulation of terminal button organization | |
Biological Process | removal of superoxide radicals | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSuperoxide dismutase [Cu-Zn]
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP61851
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000164085 | 2-153 | Superoxide dismutase [Cu-Zn] | |||
Sequence: VVKAVCVINGDAKGTVFFEQESSGTPVKVSGEVCGLAKGLHGFHVHEFGDNTNGCMSSGPHFNPYGKEHGAPVDENRHLGDLGNIEATGDCPTKVNITDSKITLFGADSIIGRTVVVHADADDLGQGGHELSKSTGNAGARIGCGVIGIAKV | ||||||
Modified residue | 53 | Phosphothreonine | ||||
Sequence: T | ||||||
Disulfide bond | 56↔145 | |||||
Sequence: CMSSGPHFNPYGKEHGAPVDENRHLGDLGNIEATGDCPTKVNITDSKITLFGADSIIGRTVVVHADADDLGQGGHELSKSTGNAGARIGC | ||||||
Modified residue | 59 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length153
- Mass (Da)15,699
- Last updated2007-01-23 v2
- Checksum4A6AAAA1EB545E70
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 97 | in Ref. 4; CAA35210, 11; AAD14963 and 12; AAA28905 | ||||
Sequence: N → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y00367 EMBL· GenBank· DDBJ | CAA68443.1 EMBL· GenBank· DDBJ | mRNA | ||
Z19591 EMBL· GenBank· DDBJ | CAA79639.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M24421 EMBL· GenBank· DDBJ | AAA28906.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X13780 EMBL· GenBank· DDBJ | CAA32028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X17332 EMBL· GenBank· DDBJ | CAA35210.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014296 EMBL· GenBank· DDBJ | AAF50095.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY071435 EMBL· GenBank· DDBJ | AAL49057.1 EMBL· GenBank· DDBJ | mRNA | ||
S72589 EMBL· GenBank· DDBJ | AAD14963.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
M18823 EMBL· GenBank· DDBJ | AAA28905.1 EMBL· GenBank· DDBJ | Genomic DNA |