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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • Cu cationBy similarityNote: Binds 1 copper ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi46Copper; catalyticBy similarity1
Metal bindingi48Copper; catalyticBy similarity1
Metal bindingi63Copper; catalyticBy similarity1
Metal bindingi63Zinc; structuralBy similarity1
Metal bindingi71Zinc; structuralBy similarity1
Metal bindingi80Zinc; structuralBy similarity1
Metal bindingi83Zinc; structuralBy similarity1
Metal bindingi120Copper; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAntioxidant, Oxidoreductase
LigandCopper, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Gene namesi
Name:SOD1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity1 Publication
ChainiPRO_00001640662 – 153Superoxide dismutase [Cu-Zn]Add BLAST152

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei4N6-succinyllysineBy similarity1
Lipidationi7S-palmitoyl cysteineBy similarity1
Modified residuei10N6-succinyllysineBy similarity1
Disulfide bondi57 ↔ 146By similarity
Modified residuei102PhosphoserineBy similarity1
Modified residuei105PhosphoserineBy similarity1
Modified residuei107PhosphoserineBy similarity1
Modified residuei122N6-acetyllysine; alternateBy similarity1
Modified residuei122N6-succinyllysine; alternateBy similarity1
Modified residuei136N6-acetyllysine; alternateBy similarity1
Modified residuei136N6-succinyllysine; alternateBy similarity1

Post-translational modificationi

Palmitoylation helps nuclear targeting and decreases catalytic activity.By similarity
Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PRIDEiP09212

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliP09212
SMRiP09212
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

HOGENOMiHOG000263447
HOVERGENiHBG000062
InParanoidiP09212
KOiK04565

Family and domain databases

CDDicd00305 Cu-Zn_Superoxide_Dismutase, 1 hit
Gene3Di2.60.40.200, 1 hit
InterProiView protein in InterPro
IPR036423 SOD-like_Cu/Zn_dom_sf
IPR024134 SOD_Cu/Zn_/chaperone
IPR018152 SOD_Cu/Zn_BS
IPR001424 SOD_Cu_Zn_dom
PANTHERiPTHR10003 PTHR10003, 1 hit
PfamiView protein in Pfam
PF00080 Sod_Cu, 1 hit
PRINTSiPR00068 CUZNDISMTASE
SUPFAMiSSF49329 SSF49329, 1 hit
PROSITEiView protein in PROSITE
PS00332 SOD_CU_ZN_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09212-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATKAVCVLK GDGPVEATIH FEQKGTGPVV VKGRITGLTE GLHEFHVHQF
60 70 80 90 100
GDNRQGCTSA GPHFNPLSKK HGGPKDEERH VGDLGNVTAG SNGVADVLIE
110 120 130 140 150
DSVISLSGDM SVIGRTLVVH EKEDDLGKGG NDESTKTGNA GSRLACGVIG

ISP
Length:153
Mass (Da):15,819
Last modified:January 23, 2007 - v3
Checksum:iB0A9C8DB56951EC9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti17A → G AA sequence (PubMed:3214553).Curated1
Sequence conflicti44E → G AA sequence (PubMed:3214553).Curated1
Sequence conflicti54R → T AA sequence (PubMed:3214553).Curated1
Sequence conflicti152S → A AA sequence (PubMed:3214553).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22644 mRNA Translation: CAA80357.1
PIRiS33162
RefSeqiNP_001076096.1, NM_001082627.1
UniGeneiOcu.2588

Genome annotation databases

GeneIDi100009313
KEGGiocu:100009313

Similar proteinsi

Entry informationi

Entry nameiSODC_RABIT
AccessioniPrimary (citable) accession number: P09212
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 133 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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