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ARG2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1PQ3, 4HZE, 4I06, 4IE2, 4IE3, 4IXU, 4IXV
Identifiers
Aliases	ARG2, arginase 2
External IDs	OMIM: 107830; MGI: 1330806; HomoloGene: 906; GeneCards: ARG2; OMA:ARG2 - orthologs
Gene location (Human) Chr. Chromosome 14 (human) Band 14q24.1 Start 67,619,920 bp End 67,651,708 bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12|12 C3 Start 79,177,551 bp End 79,203,075 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tendon of biceps brachii oocyte renal medulla human kidney secondary oocyte islet of Langerhans Pituitary Gland beta cell mucosa of paranasal sinus anterior pituitary Top expressed in duodenum granulocyte primary oocyte lobe of prostate jejunum zygote transitional epithelium of urinary bladder hair follicle secondary oocyte intestinal villus More reference expression data BioGPS n/a
Gene ontology Molecular function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines arginase activity hydrolase activity metal ion binding manganese ion binding Cellular component mitochondrial matrix mitochondrion cytoplasm Biological process urea cycle ureteric bud development nitric oxide biosynthetic process striated muscle contraction arginine metabolic process negative regulation of type 2 immune response negative regulation of tumor necrosis factor production negative regulation of macrophage inflammatory protein 1 alpha production negative regulation of chemokine (C-C motif) ligand 4 production negative regulation of chemokine (C-C motif) ligand 5 production negative regulation of defense response to bacterium regulation of reactive oxygen species biosynthetic process negative regulation of activated CD8-positive, alpha-beta T cell apoptotic process negative regulation of CD4-positive, alpha-beta T cell proliferation positive regulation of cellular senescence adaptive immune response immune system process innate immune response arginine catabolic process to ornithine Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 384 11847 Ensembl ENSG00000081181 ENSMUSG00000021125 UniProt P78540 O08691 RefSeq (mRNA) NM_001172 NM_009705 RefSeq (protein) NP_001163 NP_033835 Location (UCSC) Chr 14: 67.62 – 67.65 Mb Chr 12: 79.18 – 79.2 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Arginase, type II is an arginase protein that in humans is encoded by the ARG2 gene.

Function

Arginase catalyzes the hydrolysis of arginine to ornithine and urea. At least two isoforms of mammalian arginase exists (types I and II, this enzyme) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic function. The type II isoform encoded by this gene, is located in the mitochondria and expressed in extra-hepatic tissues, especially kidney. The physiologic role of this isoform is poorly understood; it is thought to play a role in nitric oxide and polyamine metabolism. Transcript variants of the type II gene resulting from the use of alternative polyadenylation sites have been described.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000081181 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000021125 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: Arginase, type II".

External links

• Human ARG2 genome location and ARG2 gene details page in the UCSC Genome Browser.

Further reading

• Sankaralingam S, Xu H, Davidge ST (January 2010). "Arginase contributes to endothelial cell oxidative stress in response to plasma from women with preeclampsia". Cardiovascular Research. 85 (1): 194–203. doi:10.1093/cvr/cvp277. PMID 19684035.
• Krause BJ, Prieto CP, Muñoz-Urrutia E, San Martín S, Sobrevia L, Casanello P (May 2012). "Role of arginase-2 and eNOS in the differential vascular reactivity and hypoxia-induced endothelial response in umbilical arteries and veins". Placenta. 33 (5): 360–6. doi:10.1016/j.placenta.2012.02.006. hdl:10533/131155. PMID 22391327.
• Sousa MS, Latini FR, Monteiro HP, Cerutti JM (September 2010). "Arginase 2 and nitric oxide synthase: Pathways associated with the pathogenesis of thyroid tumors". Free Radical Biology & Medicine. 49 (6): 997–1007. doi:10.1016/j.freeradbiomed.2010.06.006. PMID 20542107.
• Gotoh T, Sonoki T, Nagasaki A, Terada K, Takiguchi M, Mori M (October 1996). "Molecular cloning of cDNA for nonhepatic mitochondrial arginase (arginase II) and comparison of its induction with nitric oxide synthase in a murine macrophage-like cell line". FEBS Letters. 395 (2–3): 119–22. doi:10.1016/0014-5793(96)01015-0. PMID 8898077.
• Rotondo R, Mastracci L, Piazza T, Barisione G, Fabbi M, Cassanello M, Costa R, Morandi B, Astigiano S, Cesario A, Sormani MP, Ferlazzo G, Grossi F, Ratto GB, Ferrini S, Frumento G (September 2008). "Arginase 2 is expressed by human lung cancer, but it neither induces immune suppression, nor affects disease progression". International Journal of Cancer. 123 (5): 1108–16. doi:10.1002/ijc.23437. PMID 18528866.
• Warnken M, Haag S, Matthiesen S, Juergens UR, Racké K (April 2010). "Species differences in expression pattern of arginase isoenzymes and differential effects of arginase inhibition on collagen synthesis in human and rat pulmonary fibroblasts". Naunyn-Schmiedeberg's Archives of Pharmacology. 381 (4): 297–304. doi:10.1007/s00210-009-0489-6. PMID 20107769.
• Rodrigues Pereira N, Bandeira Moss M, Assumpção CR, Cardoso CB, Mann GE, Brunini TM, Mendes-Ribeiro AC (March 2010). "Oxidative stress, l-arginine-nitric oxide and arginase pathways in platelets from adolescents with anorexia nervosa". Blood Cells, Molecules & Diseases. 44 (3): 164–8. doi:10.1016/j.bcmd.2009.12.003. PMID 20071203.
• Bron L, Jandus C, Andrejevic-Blant S, Speiser DE, Monnier P, Romero P, Rivals JP (February 2013). "Prognostic value of arginase-II expression and regulatory T-cell infiltration in head and neck squamous cell carcinoma". International Journal of Cancer. 132 (3): E85-93. doi:10.1002/ijc.27728. PMID 22815199.
• Fiori LM, Gross JA, Turecki G (September 2012). "Effects of histone modifications on increased expression of polyamine biosynthetic genes in suicide". The International Journal of Neuropsychopharmacology. 15 (8): 1161–6. doi:10.1017/S1461145711001520. PMID 22008221.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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