Reviewed,
UniProtKB/Swiss-Prot O46412 (SODC_CEREL)
Last modified
October 13, 2009.
Version 62.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Superoxide dismutase [Cu-Zn] EC=1.15.1.1 | ||
| Gene names |
| ||
| Organism | Cervus elaphus (Red deer) | ||
| Taxonomic identifier | 9860 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Cervidae › Cervinae › Cervus |
Protein attributes
| Sequence length | 152 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 | |
| Sequence similarities | Belongs to the Cu-Zn superoxide dismutase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Coding sequence diversity | Polymorphism |
| Ligand | Copper Metal-binding Zinc |
| Molecular function | Antioxidant Oxidoreductase |
| PTM | Acetylation Disulfide bond |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW superoxide metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | antioxidant activity Inferred from electronic annotation. Source: UniProtKB-KW copper ion bindingInferred from electronic annotation. Source: UniProtKB-KW superoxide dismutase activityInferred from electronic annotation. Source: EC zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||||
| Chain | 2 – 152 | 151 | Superoxide dismutase [Cu-Zn] | PRO_0000164055 | |||||||
Sites | |||||||||||
| Metal binding | 45 | 1 | Copper; catalytic By similarity | ||||||||
| Metal binding | 47 | 1 | Copper; catalytic By similarity | ||||||||
| Metal binding | 62 | 1 | Copper; catalytic By similarity | ||||||||
| Metal binding | 62 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 70 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 79 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 82 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 119 | 1 | Copper; catalytic By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||||
| Modified residue | 69 | 1 | N6-acetyllysine By similarity | ||||||||
| Modified residue | 121 | 1 | N6-acetyllysine By similarity | ||||||||
| Disulfide bond | 56 ↔ 145 | By similarity | |||||||||
Natural variations | |||||||||||
| Natural variant | 9 | 1 | L → M in European red deer. | ||||||||
| Natural variant | 26 | 1 | H → N in European red deer. | ||||||||
Sequences
| ||||||||||||||||||
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 | |
| HSSP | HSSP built from PDB template 1CBJ based on UniProtKB P00442. |
| SMR | O46412. Positions 2-152. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | O46412. |
Enzyme and pathway databases | |
| BRENDA | 1.15.1.1. 289563. |
Family and domain databases | |
| InterPro | IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn. [Graphical view] |
| Gene3D | G3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit. |
| PANTHER | PTHR10003. SOD_Cu_Zn. 1 hit. |
| Pfam | PF00080. Sod_Cu. 1 hit. [Graphical view] |
| PRINTS | PR00068. CUZNDISMTASE. |
| ProDom | PD000469. SOD_CU_ZN. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00087. SOD_CU_ZN_1. 1 hit. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SODC_CEREL | ||||||||
| Accession | Primary (citable) accession number: O46412 Secondary accession number(s): O46413 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


