P27082 (SODC_NICPL) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 85.
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 | ||
| Gene names |
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| Organism | Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco) | ||
| Taxonomic identifier | 4092 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Nicotianoideae › Nicotianeae › Nicotiana![]() |
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. |
| Subcellular location | |
| Induction | By sulfhydryl-containing molecules such as glutathione, DDT, and cysteine. |
| Sequence similarities | Belongs to the Cu-Zn superoxide dismutase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Copper Metal-binding Zinc |
| Molecular function | Antioxidant Oxidoreductase |
| PTM | Disulfide bond |
| 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 By similarity | ||||||||
| Chain | 2 – 152 | 151 | Superoxide dismutase [Cu-Zn] | PRO_0000164146 | |||||||
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 | |||||||||||
| Disulfide bond | 56 ↔ 145 | By similarity | |||||||||
Sequences
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References
| [1] | "Differential regulation of superoxide dismutases in plants exposed to environmental stress." Tsang E.W.T., Bowler C., Herouart D., van Camp W., Villarroel R., Genetello C., van Montagu M., Inze D. Plant Cell 3:783-792(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Redox-activated expression of the cytosolic copper/zinc superoxide dismutase gene in Nicotiana." Herouart D.M., van Montagu M.M., Inze D.M. Proc. Natl. Acad. Sci. U.S.A. 90:3108-3112(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X55974 mRNA. Translation: CAA39444.1. L08253 Genomic DNA. Translation: AAA34058.1. |
| PIR | JQ1334. |
3D structure databases | |
| ProteinModelPortal | P27082. |
| SMR | P27082. Positions 1-152. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
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_NICPL | ||||||||
| Accession | Primary (citable) accession number: P27082 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
