Superoxide dismutase 3, extracellular

mammalian protein found in Mus musculus
Protein protein Q21989524
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Superoxide dismutase 3, extracellular

Summary

Superoxide dismutase 3, extracellular is a protein[1].

Key Facts

  • Superoxide dismutase 3, extracellular's instance of is recorded as protein[2].
  • Superoxide dismutase 3, extracellular's subclass of is recorded as protein[3].
  • Superoxide dismutase 3, extracellular's UniProt protein ID is recorded as O09164[4].
  • Superoxide dismutase 3, extracellular's part of is recorded as Superoxide dismutase (Cu/Zn) / superoxide dismutase copper chaperone[5].
  • Superoxide dismutase 3, extracellular's part of is recorded as Superoxide dismutase-like, copper/zinc binding domain superfamily[6].
  • Superoxide dismutase 3, extracellular's part of is recorded as Superoxide dismutase, copper/zinc binding domain, protein family[7].
  • Superoxide dismutase 3, extracellular's part of is recorded as Superoxide dismutase, copper/zinc, binding site, protein family[8].
  • Superoxide dismutase 3, extracellular's has part is recorded as Superoxide dismutase, copper/zinc binding domain[9].
  • Superoxide dismutase 3, extracellular's has part is recorded as Superoxide dismutase, copper/zinc, binding site[10].
  • Superoxide dismutase 3, extracellular's RefSeq protein ID is recorded as NP_035565[11].
  • Superoxide dismutase 3, extracellular's PDB structure ID is recorded as 2DZ2[12].
  • Superoxide dismutase 3, extracellular's PDB structure ID is recorded as 2DZ3[13].
  • Superoxide dismutase 3, extracellular's molecular function is recorded as zinc ion binding[14].
  • Superoxide dismutase 3, extracellular's molecular function is recorded as metal ion binding[15].
  • Superoxide dismutase 3, extracellular's molecular function is recorded as antioxidant activity[16].
  • Superoxide dismutase 3, extracellular's molecular function is recorded as protein binding[17].
  • Superoxide dismutase 3, extracellular's molecular function is recorded as oxidoreductase activity[18].
  • Superoxide dismutase 3, extracellular's molecular function is recorded as copper ion binding[19].
  • Superoxide dismutase 3, extracellular's molecular function is recorded as superoxide dismutase activity[20].
  • Superoxide dismutase 3, extracellular's molecular function is recorded as superoxide dismutase activity[21].
  • Superoxide dismutase 3, extracellular's molecular function is recorded as superoxide dismutase copper chaperone activity[22].
  • Superoxide dismutase 3, extracellular's cell component is recorded as extracellular matrix[23].
  • Superoxide dismutase 3, extracellular's cell component is recorded as Golgi lumen[24].
  • Superoxide dismutase 3, extracellular's cell component is recorded as extracellular space[25].
  • Superoxide dismutase 3, extracellular's cell component is recorded as extracellular region[26].

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [2] ↑ . Q905695. Retrieved . wikidata.org.
  2. [3] ↑ . Q905695. Retrieved . wikidata.org.
  3. [4] ↑ . Q905695. Retrieved . wikidata.org.
  4. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [7] ↑ . wikidata.org.
  7. [8] ↑ . wikidata.org.
  8. [9] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . Q20641742. Retrieved . wikidata.org.
  11. [12] ↑ . Swiss-Prot. Retrieved . uniprot.org. Provenance: wikidata.org.
  12. [13] ↑ . Swiss-Prot. Retrieved . uniprot.org. Provenance: wikidata.org.
  13. [14] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . Essential role for the Menkes ATPase in activation of extracellular superoxide dismutase: implication for vascular oxidative stress. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

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Use these citations when quoting this entity in research, articles, AI prompts, or wherever provenance matters. We aggregate Wikidata + Wikipedia + authoritative open-data sources; the stitched, scored, cross-referenced view is what 4ort.xyz contributes.

APA 4ort.xyz Knowledge Graph. (2026). Superoxide dismutase 3, extracellular. Retrieved May 3, 2026, from https://4ort.xyz/entity/superoxide-dismutase-3-extracellular
MLA “Superoxide dismutase 3, extracellular.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/superoxide-dismutase-3-extracellular.
BibTeX @misc{4ortxyz_superoxide-dismutase-3-extracellular_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Superoxide dismutase 3, extracellular}}, year = {2026}, url = {https://4ort.xyz/entity/superoxide-dismutase-3-extracellular}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Superoxide dismutase 3, extracellular — https://4ort.xyz/entity/superoxide-dismutase-3-extracellular (retrieved 2026-05-03)

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