Reviewed,
UniProtKB/Swiss-Prot Q54RQ1 (SODC3_DICDI)
Last modified
October 13, 2009.
Version 38.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Extracellular superoxide dismutase [Cu-Zn] 3 Short name=EC-SOD 3 EC=1.15.1.1 | ||||
| Gene names |
| ||||
| Organism | Dictyostelium discoideum (Slime mold) [Complete proteome] | ||||
| Taxonomic identifier | 44689 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium |
Protein attributes
| Sequence length | 407 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 | Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxyde radicals into hydrogen peroxyde and oxygen By similarity. |
| 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. |
| Subcellular location | Cell membrane; Single-pass type I membrane protein; Extracellular side Potential. |
| Sequence similarities | Belongs to the Cu-Zn superoxide dismutase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Membrane |
| Domain | Signal Transmembrane |
| Ligand | Copper Metal-binding Zinc |
| Molecular function | Antioxidant Oxidoreductase |
| PTM | Glutathionylation Glycoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW superoxide metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | external side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Potential | ||||||
| Chain | 20 – 407 | 388 | Extracellular superoxide dismutase [Cu-Zn] 3 | PRO_0000327853 | |||||
Regions | |||||||||
| Topological domain | 20 – 386 | 367 | Extracellular Potential | ||||||
| Transmembrane | 387 – 406 | 20 | Potential | ||||||
| Topological domain | 407 | 1 | Cytoplasmic Potential | ||||||
Sites | |||||||||
| Metal binding | 245 | 1 | Copper; catalytic By similarity | ||||||
| Metal binding | 247 | 1 | Copper; catalytic By similarity | ||||||
| Metal binding | 263 | 1 | Copper; catalytic By similarity | ||||||
| Metal binding | 263 | 1 | Zinc; structural By similarity | ||||||
| Metal binding | 271 | 1 | Zinc; structural By similarity | ||||||
| Metal binding | 280 | 1 | Zinc; structural By similarity | ||||||
| Metal binding | 283 | 1 | Zinc; structural By similarity | ||||||
| Metal binding | 320 | 1 | Copper; catalytic By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 51 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 205 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 224 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 256 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 321 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 364 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 68 | 1 | A → V in FAA00020. Ref.1 | ||||||
| Sequence conflict | 352 – 353 | 2 | LP → HT in FAA00020. Ref.1 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. Kuspa A.Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4. |
| [2] | "Multinucleation of the sodC-deficient Dictyostelium discoideum." Tsuji A., Akaza Y., Nakamura S., Kodaira K., Yasukawa H. Biol. Pharm. Bull. 26:1174-1177(2003) [PubMed: 12913271] [Abstract] Cited for: IDENTIFICATION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AAFI02000049 Genomic DNA. Translation: EAL65940.1. BR000218 mRNA. Translation: FAA00020.1. | |
| RefSeq | XP_639300.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3390890. |
| GenomeReviews | Gene locus sodC in contig CM000153_GR. |
| KEGG | ddi:DDB_0232186. |
Organism-specific databases | |
| dictyBase | DDB_G0282993. sodC. |
Enzyme and pathway databases | |
| BRENDA | 1.15.1.1. 424. |
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. 2 hits. |
| PANTHER | PTHR10003. SOD_Cu_Zn. 1 hit. |
| Pfam | PF00080. Sod_Cu. 2 hits. [Graphical view] |
| PROSITE | PS00087. SOD_CU_ZN_1. 1 hit. PS00332. SOD_CU_ZN_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SODC3_DICDI | ||||||||
| Accession | Primary (citable) accession number: Q54RQ1 Secondary accession number(s): Q52KB2 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Dictyostelium discoideum Dictyostelium discoideum: entries, gene names and cross-references to dictyBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with


