Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

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

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Gene namesi
Name:SOD1
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001640512 – 153Superoxide dismutase [Cu-Zn]Add BLAST152

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei4N6-succinyllysineBy similarity1
Lipidationi7S-palmitoyl cysteineBy similarity1
Modified residuei10N6-succinyllysineBy similarity1
Disulfide bondi57 ↔ 146By similarity
Modified residuei91N6-succinyllysineBy similarity1
Modified residuei98PhosphoserineBy similarity1
Modified residuei102PhosphoserineBy similarity1
Modified residuei107PhosphoserineBy similarity1
Modified residuei122N6-acetyllysine; alternateBy similarity1
Modified residuei122N6-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

PRIDEiQ8WNN6.

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

HOVERGENiHBG000062.
InParanoidiQ8WNN6.
KOiK04565.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8WNN6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMKAVCVLK GQGPVEGTIH FVQKGSGPVV VSGTITGLTE GEHGFHVHQF
60 70 80 90 100
EDXTQGCTSA GPHFNPLSKK HGGPKDQERH VGDLGNVTAG KDGVAIVSIE
110 120 130 140 150
DSLIALSGDY SIIGRTMVVH EKRDDLGKGD NEESTQTGNA GSRLACGVIG

IAQ
Length:153
Mass (Da):15,913
Last modified:March 1, 2002 - v1
Checksum:i0D7900E59C57E6B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF346417 mRNA. Translation: AAL61608.1.
RefSeqiNP_001003035.1. NM_001003035.1.
UniGeneiCfa.6360.

Genome annotation databases

GeneIDi403559.
KEGGicfa:403559.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF346417 mRNA. Translation: AAL61608.1.
RefSeqiNP_001003035.1. NM_001003035.1.
UniGeneiCfa.6360.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ8WNN6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403559.
KEGGicfa:403559.

Organism-specific databases

CTDi6647.

Phylogenomic databases

HOVERGENiHBG000062.
InParanoidiQ8WNN6.
KOiK04565.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSODC_CANLF
AccessioniPrimary (citable) accession number: Q8WNN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: March 1, 2002
Last modified: November 30, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.