Arginase type II

mammalian protein found in Mus musculus
Protein protein Q21984970
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Arginase type II

Summary

Arginase type II is a protein[1].

Key Facts

  • Arginase type II's instance of is recorded as protein[2].
  • Arginase type II's subclass of is recorded as protein[3].
  • Arginase type II's UniProt protein ID is recorded as O08691[4].
  • Arginase type II's part of is recorded as Ureohydrolase domain superfamily[5].
  • Arginase type II's part of is recorded as arginase[6].
  • Arginase type II's part of is recorded as Ureohydrolase, manganese-binding site, protein family[7].
  • Arginase type II's has part is recorded as Ureohydrolase, manganese-binding site[8].
  • Arginase type II's RefSeq protein ID is recorded as NP_033835[9].
  • Arginase type II's molecular function is recorded as hydrolase activity[10].
  • Arginase type II's molecular function is recorded as hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines[11].
  • Arginase type II's molecular function is recorded as metal ion binding[12].
  • Arginase type II's molecular function is recorded as arginase activity[13].
  • Arginase type II's molecular function is recorded as arginase activity[14].
  • Arginase type II's molecular function is recorded as manganese ion binding[15].
  • Arginase type II's molecular function is recorded as nitric-oxide synthase binding[16].
  • Arginase type II's cell component is recorded as mitochondrion[17].
  • Arginase type II's cell component is recorded as cytoplasm[18].
  • Arginase type II's cell component is recorded as mitochondrion[19].
  • Arginase type II's biological process is recorded as striated muscle contraction[20].
  • Arginase type II's biological process is recorded as ureteric bud development[21].
  • Arginase type II's biological process is recorded as urea cycle[22].
  • Arginase type II's biological process is recorded as arginine metabolic process[23].
  • Arginase type II's biological process is recorded as negative regulation of type 2 immune response[24].
  • Arginase type II's biological process is recorded as negative regulation of macrophage inflammatory protein 1 alpha production[25].
  • Arginase type II's biological process is recorded as negative regulation of chemokine (C-C motif) ligand 4 production[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] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [9] . Q20641742. Retrieved . wikidata.org.
  9. [10] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . Arginase modulates myocardial contractility by a nitric oxide synthase 1-dependent mechanism. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . Arginase modulates myocardial contractility by a nitric oxide synthase 1-dependent mechanism. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . Arginase modulates myocardial contractility by a nitric oxide synthase 1-dependent mechanism. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . Arginase modulates myocardial contractility by a nitric oxide synthase 1-dependent mechanism. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . Arginase modulates myocardial contractility by a nitric oxide synthase 1-dependent mechanism. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . Spatial gene expression in the T-stage mouse metanephros. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . Increased mitochondrial arginine metabolism supports bioenergetics in asthma. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . Arginase 2 deletion leads to enhanced M1 macrophage activation and upregulated polyamine metabolism in response to Helicobacter pylori infection.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . Arginase 2 deletion leads to enhanced M1 macrophage activation and upregulated polyamine metabolism in response to Helicobacter pylori infection.. 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). Arginase type II. Retrieved May 3, 2026, from https://4ort.xyz/entity/arginase-type-ii
MLA “Arginase type II.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/arginase-type-ii.
BibTeX @misc{4ortxyz_arginase-type-ii_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Arginase type II}}, year = {2026}, url = {https://4ort.xyz/entity/arginase-type-ii}, note = {Accessed: 2026-05-03}}
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