P31161 (SODM1_CAEEL) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 101.
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 [Mn] 1, mitochondrial EC=1.15.1.1 | ||||||
| Gene names |
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| Organism | Caenorhabditis elegans [Reference proteome] | ||||||
| Taxonomic identifier | 6239 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis![]() |
Protein attributes
| Sequence length | 221 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 superoxide anion 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 manganese ion per subunit By similarity. |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Sequence similarities | Belongs to the iron/manganese superoxide dismutase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Manganese Metal-binding |
| Molecular function | Oxidoreductase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | superoxide metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular_component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrionInferred from direct assay PubMed 20188671. Source: WormBase |
| 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 | ||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 24 | 24 | Mitochondrion By similarity | |||||||||||||||||||||||||||||||||||||
| Chain | 25 – 221 | 197 | Superoxide dismutase [Mn] 1, mitochondrial | PRO_0000032876 | ||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||
| Metal binding | 50 | 1 | Manganese By similarity | |||||||||||||||||||||||||||||||||||||
| Metal binding | 98 | 1 | Manganese By similarity | |||||||||||||||||||||||||||||||||||||
| Metal binding | 182 | 1 | Manganese By similarity | |||||||||||||||||||||||||||||||||||||
| Metal binding | 186 | 1 | Manganese By similarity | |||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||
| Turn | 35 – 41 | 7 | ||||||||||||||||||||||||||||||||||||||
| Helix | 44 – 52 | 9 | ||||||||||||||||||||||||||||||||||||||
| Helix | 54 – 74 | 21 | ||||||||||||||||||||||||||||||||||||||
| Helix | 78 – 83 | 6 | ||||||||||||||||||||||||||||||||||||||
| Helix | 85 – 103 | 19 | ||||||||||||||||||||||||||||||||||||||
| Helix | 114 – 124 | 11 | ||||||||||||||||||||||||||||||||||||||
| Helix | 127 – 139 | 13 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 143 – 152 | 10 | ||||||||||||||||||||||||||||||||||||||
| Turn | 153 – 156 | 4 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 157 – 164 | 8 | ||||||||||||||||||||||||||||||||||||||
| Helix | 169 – 173 | 5 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 176 – 182 | 7 | ||||||||||||||||||||||||||||||||||||||
| Helix | 185 – 187 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 189 – 192 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 196 – 202 | 7 | ||||||||||||||||||||||||||||||||||||||
| Helix | 203 – 206 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 209 – 219 | 11 | ||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and characterization of manganese superoxide dismutase gene in C.elegans." Suzuki N., Ishii N., Suzuki K. Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Cloning, sequencing and mapping of a manganese superoxide dismutase gene of the nematode Caenorhabditis elegans." Suzuki N., Inokuma K., Yasuda K., Ishii N. DNA Res. 3:171-174(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | D12984 mRNA. Translation: BAA02363.1. D85499 Genomic DNA. Translation: BAA12821.1. Z81057 Genomic DNA. Translation: CAB02913.1. | ||||||||||||
| PIR | JC5122. | ||||||||||||
| RefSeq | NP_492290.1. NM_059889.4. | ||||||||||||
| UniGene | Cel.112. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P31161. | ||||||||||||
| SMR | P31161. Positions 25-221. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | 6239.F10D11.1.1. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | P31161. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblMetazoa | F10D11.1.1; F10D11.1.1; F10D11.1. F10D11.1.2; F10D11.1.2; F10D11.1. | ||||||||||||
| GeneID | 172632. | ||||||||||||
| KEGG | cel:CELE_F10D11.1. | ||||||||||||
| UCSC | F10D11.1.1. c. elegans. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 172632. | ||||||||||||
| WormBase | F10D11.1; CE09323; WBGene00004931; sod-2. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0605. | ||||||||||||
| GeneTree | ENSGT00390000011877. | ||||||||||||
| HOGENOM | HOG000013583. | ||||||||||||
| InParanoid | P31161. | ||||||||||||
| KO | K04564. | ||||||||||||
| OMA | MAPPGKG. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR001189. Mn/Fe_SOD. IPR019833. Mn/Fe_SOD_BS. IPR019832. Mn/Fe_SOD_C. IPR019831. Mn/Fe_SOD_N. [Graphical view] | ||||||||||||
| PANTHER | PTHR11404. PTHR11404. 1 hit. | ||||||||||||
| Pfam | PF02777. Sod_Fe_C. 1 hit. PF00081. Sod_Fe_N. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF000349. SODismutase. 1 hit. | ||||||||||||
| PRINTS | PR01703. MNSODISMTASE. | ||||||||||||
| SUPFAM | SSF46609. SODismutase. 1 hit. SSF54719. SODismutase. 1 hit. | ||||||||||||
| PROSITE | PS00088. SOD_MN. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P31161. | ||||||||||||
| NextBio | 876347. | ||||||||||||
Entry information
| Entry name | SODM1_CAEEL | ||||||||
| Accession | Primary (citable) accession number: P31161 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Caenorhabditis annotation project | ||||||||
Relevant documents
| Caenorhabditis elegans Caenorhabditis elegans: entries, gene names and cross-references to WormBase |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
