P08228 · SODC_MOUSE
- ProteinSuperoxide dismutase [Cu-Zn]
- GeneSod1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids154 (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.
Miscellaneous
A mouse model of ALS overexpressing human SOD1 variant 'Ala-94' exhibits disease onset at 89 days (males) and 99 days (females) (PubMed:29194436).
There is a marked suppression of DAO expression and activity in the reticulospinal tract of the spinal cord, but not in the kidney or cerebellum; transgenic mice accumulate D-serine, but not D-alanine or D-aspartate, in their spinal cord (PubMed:22203986, PubMed:29194436).
Simultanous presence of the amyotrophic lateral sclerosis-associated human DAO variant 'Trp-188' potentiates the development of disease (PubMed:29194436).
There is a marked suppression of DAO expression and activity in the reticulospinal tract of the spinal cord, but not in the kidney or cerebellum; transgenic mice accumulate D-serine, but not D-alanine or D-aspartate, in their spinal cord (PubMed:22203986, PubMed:29194436).
Simultanous presence of the amyotrophic lateral sclerosis-associated human DAO variant 'Trp-188' potentiates the development of disease (PubMed:29194436).
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
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP08228
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
40% reduction in hepatic GPX1 activity.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 7 variants from UniProt as well as other sources including ClinVar and dbSNP.
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_0000164062 | 2-154 | Superoxide dismutase [Cu-Zn] | |||
Sequence: AMKAVCVLKGDGPVQGTIHFEQKASGEPVVLSGQITGLTEGQHGFHVHQYGDNTQGCTSAGPHFNPHSKKHGGPADEERHVGDLGNVTAGKDGVANVSIEDRVISLSGEHSIIGRTMVVHEKQDDLGKGGNEESTKTGNAGSRLACGVIGIAQ | ||||||
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: CTSAGPHFNPHSKKHGGPADEERHVGDLGNVTAGKDGVANVSIEDRVISLSGEHSIIGRTMVVHEKQDDLGKGGNEESTKTGNAGSRLAC | ||||||
Modified residue | 92 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 99 | 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
Proteomic databases
2D gel databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer; non-disulfide-linked (PubMed:20727846).
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).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P08228 | Prdx5 P99029 | 2 | EBI-1635090, EBI-2735704 | |
BINARY | P08228 | Rac1 P63001 | 4 | EBI-1635090, EBI-413646 | |
BINARY | P08228 | Snca O55042 | 2 | EBI-1635090, EBI-2310271 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length154
- Mass (Da)15,943
- Last updated2007-01-23 v2
- ChecksumCAE548C66043BAC4
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 102 | in Ref. 2; AAA40121 | ||||
Sequence: D → H |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X06683 EMBL· GenBank· DDBJ | CAA29880.1 EMBL· GenBank· DDBJ | mRNA | ||
M60798 EMBL· GenBank· DDBJ | AAA40121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M60794 EMBL· GenBank· DDBJ | AAA40121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M60795 EMBL· GenBank· DDBJ | AAA40121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M60796 EMBL· GenBank· DDBJ | AAA40121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M60797 EMBL· GenBank· DDBJ | AAA40121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M35725 EMBL· GenBank· DDBJ | AAA37518.1 EMBL· GenBank· DDBJ | mRNA | ||
AK020624 EMBL· GenBank· DDBJ | BAB32154.1 EMBL· GenBank· DDBJ | mRNA | ||
AK077284 EMBL· GenBank· DDBJ | BAC36730.1 EMBL· GenBank· DDBJ | mRNA | ||
BC002066 EMBL· GenBank· DDBJ | AAH02066.1 EMBL· GenBank· DDBJ | mRNA | ||
BC048874 EMBL· GenBank· DDBJ | AAH48874.1 EMBL· GenBank· DDBJ | mRNA | ||
BC086886 EMBL· GenBank· DDBJ | AAH86886.1 EMBL· GenBank· DDBJ | mRNA |