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Reviewed, UniProtKB/Swiss-Prot O46412 (SODC_CEREL)

Last modified October 13, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Superoxide dismutase [Cu-Zn]
    EC=1.15.1.1
Gene names
Name: SOD1
OrganismCervus elaphus (Red deer)
Taxonomic identifier9860 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraCervidaeCervinaeCervus

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

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

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Cofactor

Binds 1 copper ion per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMAcetylation
Disulfide bond
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionantioxidant activity

Inferred from electronic annotation. Source: UniProtKB-KW

copper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide dismutase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 152151Superoxide dismutase [Cu-Zn]
PRO_0000164055

Sites

Metal binding451Copper; catalytic By similarity
Metal binding471Copper; catalytic By similarity
Metal binding621Copper; catalytic By similarity
Metal binding621Zinc; structural By similarity
Metal binding701Zinc; structural By similarity
Metal binding791Zinc; structural By similarity
Metal binding821Zinc; structural By similarity
Metal binding1191Copper; catalytic By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue691N6-acetyllysine By similarity
Modified residue1211N6-acetyllysine By similarity
Disulfide bond56 ↔ 145 By similarity

Natural variations

Natural variant91L → M in European red deer.
Natural variant261H → N in European red deer.

Sequences

Sequence LengthMass (Da)Tools
O46412-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BAC5F0E9D3EBFFFD

FASTA15215,829
        10         20         30         40         50         60 
MATKAVCVLK GDGPVQGTIR FEAKGHTVVV TGSITGLTEG DHGFHVHQFG DNTQGCTSAG 

        70         80         90        100        110        120 
PHFNPLSKKH GGPKDEERHV GDLGNVTADK NGVAKVDIVD SLISLSGEHS IIGRTMVVHE 

       130        140        150 
KPDDLGRGGN EESTKTGNAR NRLACGVIGI AQ 

« Hide

References

[1]"Characterization of the erythrocyte superoxide dismutase allozymes in the deer Cervus elaphus."
He K., Wilton S.D., Tate M.L., Murphy M.P.
Anim. Genet. 28:299-301(1997) [PubMed: 9345726] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: European red deer and North American wapiti.

Cross-references

Sequence databases

U93268 mRNA. Translation: AAB88115.1.
U93269 mRNA. Translation: AAB88116.1.

3D structure databases

HSSPHSSP built from PDB template 1CBJ based on UniProtKB P00442.
SMRO46412. Positions 2-152.
ModBaseSearch...

Phylogenomic databases

HOVERGENO46412.

Enzyme and pathway databases

BRENDA1.15.1.1. 289563.

Family and domain databases

InterProIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn.
[Graphical view]
Gene3DG3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
PANTHERPTHR10003. SOD_Cu_Zn. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
ProDomPD000469. SOD_CU_ZN. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODC_CEREL
AccessionPrimary (citable) accession number: O46412
Secondary accession number(s): O46413
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: October 13, 2009
This is version 62 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents