P80174 (SODC_CARCR) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 80.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Superoxide dismutase [Cu-Zn] EC=1.15.1.1 |
| Organism | Caretta caretta (Loggerhead sea turtle) |
| Taxonomic identifier | 8467 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Testudines › Cryptodira › Chelonioidea › Cheloniidae › Caretta![]() |
Protein attributes
| Sequence length | 167 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein 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. |
| Subcellular location | |
| Sequence similarities | Belongs to the Cu-Zn superoxide dismutase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Domain | Repeat |
| Ligand | Copper Metal-binding Zinc |
| Molecular function | Antioxidant Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | superoxide metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW superoxide dismutase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.1 | ||||||||
| Chain | 2 – 167 | 166 | Superoxide dismutase [Cu-Zn] | PRO_0000164070 | |||||||
Regions | |||||||||||
| Repeat | 15 – 18 | 4 | |||||||||
| Repeat | 19 – 22 | 4 | |||||||||
| Repeat | 23 – 26 | 4 | |||||||||
| Repeat | 27 – 30 | 4 | |||||||||
Sites | |||||||||||
| Metal binding | 59 | 1 | Copper; catalytic By similarity | ||||||||
| Metal binding | 61 | 1 | Copper; catalytic By similarity | ||||||||
| Metal binding | 76 | 1 | Copper; catalytic By similarity | ||||||||
| Metal binding | 76 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 84 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 93 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 96 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 133 | 1 | Copper; catalytic By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 2 | 1 | Blocked amino end (Ala) | ||||||||
| Disulfide bond | 70 ↔ 159 | By similarity | |||||||||
Sequences
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References
| [1] | "The primary structure of turtle Cu,Zn superoxide dismutase. Structural and functional irrelevance of an insert conferring proteolytic susceptibility." Schinina M.E., Bossa F., Lania A., Capo C.R., Carlini P., Calabrese L. Eur. J. Biochem. 211:843-849(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-167. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| PIR | S29782. |
3D structure databases | |
| ProteinModelPortal | P80174. |
| SMR | P80174. Positions 5-166. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P80174. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG000062. |
Family and domain databases | |
| Gene3D | 2.60.40.200. 1 hit. |
| InterPro | IPR024134. SOD_Cu/Zn_/chaperones. IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn_dom. [Graphical view] |
| PANTHER | PTHR10003. PTHR10003. 1 hit. |
| Pfam | PF00080. Sod_Cu. 1 hit. [Graphical view] |
| PRINTS | PR00068. CUZNDISMTASE. |
| SUPFAM | SSF49329. SOD_Cu_Zn. 1 hit. |
| PROSITE | PS00087. SOD_CU_ZN_1. 1 hit. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SODC_CARCR | ||||||||
| Accession | Primary (citable) accession number: P80174 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
