P08228 · SODC_MOUSE

  • Protein
    Superoxide dismutase [Cu-Zn]
  • Gene
    Sod1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Cu cation (UniProtKB | Rhea| CHEBI:23378 )

Note: Binds 1 copper ion per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site47Cu cation (UniProtKB | ChEBI); catalytic
Binding site49Cu cation (UniProtKB | ChEBI); catalytic
Binding site64Cu cation (UniProtKB | ChEBI); catalytic
Binding site64Zn2+ (UniProtKB | ChEBI); structural
Binding site72Zn2+ (UniProtKB | ChEBI); structural
Binding site81Zn2+ (UniProtKB | ChEBI); structural
Binding site84Zn2+ (UniProtKB | ChEBI); structural
Binding site121Cu cation (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentaxon cytoplasm
Cellular Componentcytoplasm
Cellular Componentcytoplasmic vesicle
Cellular Componentcytosol
Cellular Componentdendrite cytoplasm
Cellular Componentdense core granule
Cellular Componentextracellular region
Cellular Componentextracellular space
Cellular Componentlysosome
Cellular Componentmitochondrial intermembrane space
Cellular Componentmitochondrion
Cellular Componentmyelin sheath
Cellular Componentneuronal cell body
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentperoxisome
Cellular Componentplasma membrane
Cellular Componentprotein-containing complex
Cellular Componentsecretory granule
Molecular Functioncopper ion binding
Molecular Functionenzyme binding
Molecular Functionidentical protein binding
Molecular Functionprotein phosphatase 2B binding
Molecular Functionprotein-folding chaperone binding
Molecular Functionsmall GTPase binding
Molecular Functionsuperoxide dismutase activity
Molecular Functionzinc ion binding
Biological Processaction potential initiation
Biological Processanterograde axonal transport
Biological Processapoptotic process
Biological Processauditory receptor cell stereocilium organization
Biological Processdetermination of adult lifespan
Biological Processectopic germ cell programmed cell death
Biological Processembryo implantation
Biological Processgene expression
Biological Processglutathione metabolic process
Biological Processheart contraction
Biological Processhydrogen peroxide biosynthetic process
Biological Processintracellular iron ion homeostasis
Biological Processlocomotory behavior
Biological Processmuscle cell cellular homeostasis
Biological Processmyeloid cell homeostasis
Biological Processnegative regulation of apoptotic process
Biological Processnegative regulation of cholesterol biosynthetic process
Biological Processnegative regulation of developmental process
Biological Processnegative regulation of inflammatory response
Biological Processnegative regulation of neuron apoptotic process
Biological Processnegative regulation of reproductive process
Biological Processneurofilament cytoskeleton organization
Biological Processneuronal action potential
Biological Processovarian follicle development
Biological Processperipheral nervous system myelin maintenance
Biological Processpositive regulation of cytokine production
Biological Processpositive regulation of MAPK cascade
Biological Processpositive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
Biological Processpositive regulation of phagocytosis
Biological Processpositive regulation of superoxide anion generation
Biological Processreactive oxygen species metabolic process
Biological Processregulation of blood pressure
Biological Processregulation of mitochondrial membrane potential
Biological Processregulation of multicellular organism growth
Biological Processrelaxation of vascular associated smooth muscle
Biological Processremoval of superoxide radicals
Biological Processresponse to axon injury
Biological Processresponse to copper ion
Biological Processresponse to ethanol
Biological Processresponse to heat
Biological Processresponse to hydrogen peroxide
Biological Processresponse to nutrient levels
Biological Processresponse to oxidative stress
Biological Processresponse to reactive oxygen species
Biological Processresponse to superoxide
Biological Processresponse to xenobiotic stimulus
Biological Processretina homeostasis
Biological Processretrograde axonal transport
Biological Processsensory perception of sound
Biological Processspermatogenesis
Biological Processsuperoxide anion generation
Biological Processsuperoxide metabolic process
Biological Processtransmission of nerve impulse

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Superoxide dismutase [Cu-Zn]
  • EC number

Gene names

    • Name
      Sod1

Organism names

  • Taxonomic identifier
  • Strains
    • SWR/J
    • C57BL/6J
    • OF1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P08228

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.

Go to variant viewer

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, lipidation, disulfide bond.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00001640622-154Superoxide dismutase [Cu-Zn]
Modified residue4N6-succinyllysine
Lipidation7S-palmitoyl cysteine
Modified residue10N6-succinyllysine
Disulfide bond58↔147
Modified residue92N6-succinyllysine
Modified residue99Phosphoserine
Modified residue106Phosphoserine
Modified residue108Phosphoserine
Modified residue123N6-acetyllysine; alternate
Modified residue123N6-succinyllysine; alternate
Modified residue137N6-acetyllysine; alternate
Modified residue137N6-succinyllysine; alternate

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

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).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P08228Prdx5 P990292EBI-1635090, EBI-2735704
BINARY P08228Rac1 P630014EBI-1635090, EBI-413646
BINARY P08228Snca O550422EBI-1635090, EBI-2310271
View interactors in UniProtKB
View CPX-2898 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    154
  • Mass (Da)
    15,943
  • Last updated
    2007-01-23 v2
  • Checksum
    CAE548C66043BAC4
MAMKAVCVLKGDGPVQGTIHFEQKASGEPVVLSGQITGLTEGQHGFHVHQYGDNTQGCTSAGPHFNPHSKKHGGPADEERHVGDLGNVTAGKDGVANVSIEDRVISLSGEHSIIGRTMVVHEKQDDLGKGGNEESTKTGNAGSRLACGVIGIAQ

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict102in Ref. 2; AAA40121

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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