Q8HXQ2 · SODC_MACFU
- ProteinSuperoxide dismutase [Cu-Zn]
- GeneSOD1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids154 (go to sequence)
- Protein existenceEvidence at transcript 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 | 47 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 49 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 64 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 64 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 72 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 81 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 84 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: D | ||||||
Binding site | 121 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSuperoxide dismutase [Cu-Zn]
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Macaca
Accessions
- Primary accessionQ8HXQ2
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, lipidation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000164060 | 2-154 | Superoxide dismutase [Cu-Zn] | |||
Sequence: AMKAVCVLKGDSPVQGTINFEQKESNGPVKVWGSITGLTEGLHGFHVHQFGDNTQGCTSAGPHFNPLSRQHGGPKDEERHVGDLGNVTAGKDGVAKVSFEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESKKTGNAGGRLACGVIGIAQ | ||||||
Modified residue | 4 | N6-succinyllysine | ||||
Sequence: K | ||||||
Lipidation | 7 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 10 | N6-succinyllysine | ||||
Sequence: K | ||||||
Disulfide bond | 58↔147 | |||||
Sequence: CTSAGPHFNPLSRQHGGPKDEERHVGDLGNVTAGKDGVAKVSFEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESKKTGNAGGRLAC | ||||||
Modified residue | 92 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 99 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 103 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 106 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 108 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 123 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 123 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 137 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 137 | N6-succinyllysine; alternate | ||||
Sequence: K |
Post-translational modification
Palmitoylation helps nuclear targeting and decreases catalytic activity.
Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity.
Keywords
- PTM
Interaction
Subunit
Homodimer; non-disulfide-linked (By similarity).
Heterodimer with SOD1. The heterodimer CCS:SOD1 interacts with SLC31A1; this heterotrimer is Cu1+-mediated and its maintenance is regulated through SOD1 activation (By similarity).
Heterodimer with SOD1. The heterodimer CCS:SOD1 interacts with SLC31A1; this heterotrimer is Cu1+-mediated and its maintenance is regulated through SOD1 activation (By similarity).
Structure
Sequence
- Sequence statusComplete
- Length154
- Mass (Da)15,983
- Last updated2007-01-23 v3
- Checksum7B77BC2ED8CDDC2F