P11964 · SODCP_PEA

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.

TypeIDPosition(s)Description
Binding site94Cu cation (UniProtKB | ChEBI); catalytic
Binding site96Cu cation (UniProtKB | ChEBI); catalytic
Binding site111Cu cation (UniProtKB | ChEBI); catalytic
Binding site111Zn2+ (UniProtKB | ChEBI); structural
Binding site119Zn2+ (UniProtKB | ChEBI); structural
Binding site128Zn2+ (UniProtKB | ChEBI); structural
Binding site131Zn2+ (UniProtKB | ChEBI); structural
Binding site168Cu cation (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentchloroplast
Molecular Functioncopper ion binding
Molecular Functionsuperoxide dismutase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      SODCP
    • Synonyms
      SOD2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > Hologalegina > IRL clade > Fabeae > Pisum

Accessions

  • Primary accession
    P11964

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant55

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for transit peptide, chain, disulfide bond.

TypeIDPosition(s)Description
Transit peptide1-48Chloroplast
ChainPRO_000003284849-202Superoxide dismutase [Cu-Zn], chloroplastic
Disulfide bond105↔194

Keywords

Interaction

Subunit

Homotetramer.

Structure

Family & Domains

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    202
  • Mass (Da)
    20,626
  • Last updated
    1989-10-01 v1
  • Checksum
    677BF4F185533A31
MASQTLVSPSPLSSHSLLRTSFSGVSVKLAPQFSTLATSNFKPLTVVAAAKKAVSVLKGTSAVEGVVTLTQDDEGPTTVNVRITGLTPGLHGFHLHEYGDTTNGCISTGPHFNPNKLTHGAPEDEIRHAGDLGNIVANAEGVAEATIVDNQIPLTGPNSVVGRALVVHELQDDLGKGGHELSLSTGNAGGRLACGVVGLTPV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
J04087
EMBL· GenBank· DDBJ
AAA33688.1
EMBL· GenBank· DDBJ
mRNA
X56435
EMBL· GenBank· DDBJ
CAA39819.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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