Q8HXQ2 · SODC_MACFU

Function

function

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

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.

115420406080100120140
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 Componentcytoplasm
Cellular Componentcytoplasmic vesicle
Cellular Componentcytosol
Cellular Componentdendrite cytoplasm
Cellular Componentmitochondrion
Cellular Componentneuronal cell body
Cellular Componentnucleus
Cellular Componentperoxisome
Cellular Componentprotein-containing complex
Molecular Functioncopper ion binding
Molecular Functionprotein phosphatase 2B binding
Molecular Functionprotein-folding chaperone binding
Molecular Functionsuperoxide dismutase activity
Molecular Functionzinc ion binding
Biological Processauditory receptor cell stereocilium organization
Biological Processembryo implantation
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 neuron apoptotic process
Biological Processneurofilament cytoskeleton organization
Biological Processovarian follicle development
Biological Processperipheral nervous system myelin maintenance
Biological Processpositive regulation of cytokine production
Biological Processpositive regulation of MAPK cascade
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 ethanol
Biological Processresponse to heat
Biological Processresponse to hydrogen peroxide
Biological Processresponse to superoxide
Biological Processretina homeostasis
Biological Processsensory perception of sound
Biological Processspermatogenesis
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
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Macaca

Accessions

  • Primary accession
    Q8HXQ2

PTM/Processing

Features

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

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00001640602-154Superoxide dismutase [Cu-Zn]
Modified residue4N6-succinyllysine
Lipidation7S-palmitoyl cysteine
Modified residue10N6-succinyllysine
Disulfide bond58↔147
Modified residue92N6-succinyllysine
Modified residue99Phosphoserine
Modified residue103Phosphoserine
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

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).

Structure

Family & Domains

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    154
  • Mass (Da)
    15,983
  • Last updated
    2007-01-23 v3
  • Checksum
    7B77BC2ED8CDDC2F
MAMKAVCVLKGDSPVQGTINFEQKESNGPVKVWGSITGLTEGLHGFHVHQFGDNTQGCTSAGPHFNPLSRQHGGPKDEERHVGDLGNVTAGKDGVAKVSFEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESKKTGNAGGRLACGVIGIAQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB087269
EMBL· GenBank· DDBJ
BAC20348.1
EMBL· GenBank· DDBJ
mRNA

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