P80174 · SODC_CARCR
- ProteinSuperoxide dismutase [Cu-Zn]
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids167 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic activity
- 2 H+ + 2 superoxide = H2O2 + O2
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 copper ion per subunit.
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 59 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 61 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 76 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 76 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 84 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 93 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 96 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: D | ||||||
Binding site | 133 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Cellular Component | peroxisome | |
Molecular Function | copper ion binding | |
Molecular Function | superoxide dismutase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSuperoxide dismutase [Cu-Zn]
- EC number
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Testudinata > Testudines > Cryptodira > Durocryptodira > Americhelydia > Chelonioidea > Cheloniidae > Caretta
Accessions
- Primary accessionP80174
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, lipidation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | Blocked amino end (Ala) | ||||
Sequence: A | ||||||
Chain | PRO_0000164070 | 2-167 | Superoxide dismutase [Cu-Zn] | |||
Sequence: ATVKAVCVLKGEDPVKEPVKGPVKEPVKGIIYFEQQGNGPVTLSGSITGLTEGKHGFHVHEFGDNTNGCTSAGAHFNPPGKNHGGPQDNERHVGDLGNVIANKEGVAEVCIKDSLISLTGSQSIIGRTMVVHEKEDDLGKGGNDESLKTGNAGSRLACGVVGIAKL | ||||||
Lipidation | 8 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Disulfide bond | 70↔159 | |||||
Sequence: CTSAGAHFNPPGKNHGGPQDNERHVGDLGNVIANKEGVAEVCIKDSLISLTGSQSIIGRTMVVHEKEDDLGKGGNDESLKTGNAGSRLAC |
Keywords
- PTM
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 15-18 | |||||
Sequence: PVKE | ||||||
Repeat | 19-22 | |||||
Sequence: PVKG | ||||||
Repeat | 23-26 | |||||
Sequence: PVKE | ||||||
Repeat | 27-30 | |||||
Sequence: PVKG |
Sequence similarities
Belongs to the Cu-Zn superoxide dismutase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length167
- Mass (Da)17,277
- Last updated2007-01-23 v2
- ChecksumF4F46538FAE69E8F
Keywords
- Technical term