ARG1 (gene)

ARG1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1WVA, 1WVB, 2AEB, 2PHA, 2PHO, 2PLL, 2ZAV, 3DJ8, 3E6K, 3E6V, 3F80, 3GMZ, 3GN0, 3KV2, 3LP4, 3LP7, 3MFV, 3MFW, 3MJL, 3SJT, 3SKK, 3TF3, 3TH7, 3THE, 3THH, 3THJ, 4FCI, 4FCK, 4GSM, 4GSV, 4GSZ, 4GWC, 4GWD, 4HWW, 4HXQ, 4IE1
Identifiers
Aliases	ARG1, arginase 1
External IDs	MGI: 88070 HomoloGene: 29 GeneCards: ARG1
Gene location (Human)
Chr.	Chromosome 6 (human)[1]
End	131,584,332 bp[1]
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)[2]
End	24,927,484 bp[2]
Gene ontology
Molecular function	• arginase activity; • manganese ion binding; • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; • metal ion binding; • hydrolase activity;
Cellular component	• cytoplasm; • cytosol; • mitochondrial outer membrane; • neuronal cell body; • neuron projection; • extracellular exosome; • cell nucleus; • extracellular region; • azurophil granule lumen; • specific granule lumen; • extracellular space;
Biological process	• cellular response to interleukin-4; • cellular response to transforming growth factor beta stimulus; • response to selenium ion; • response to amino acid; • response to cadmium ion; • positive regulation of endothelial cell proliferation; • maternal process involved in female pregnancy; • lung development; • urea cycle; • female pregnancy; • response to steroid hormone; • cellular response to glucagon stimulus; • aging; • response to peptide hormone; • response to zinc ion; • arginine catabolic process; • arginine metabolic process; • response to vitamin E; • protein homotrimerization; • cellular response to dexamethasone stimulus; • response to vitamin A; • arginine catabolic process to ornithine; • response to lipopolysaccharide; • response to manganese ion; • response to wounding; • response to axon injury; • collagen biosynthetic process; • response to amine; • liver development; • response to methylmercury; • cellular response to lipopolysaccharide; • response to herbicide; • response to drug; • regulation of L-arginine import; • cellular response to hydrogen peroxide; • mammary gland involution; • neutrophil degranulation; • negative regulation of T cell proliferation; • defense response to protozoan; • negative regulation of activated T cell proliferation; • negative regulation of interferon-gamma-mediated signaling pathway; • positive regulation of neutrophil mediated killing of fungus; • negative regulation of T-helper 2 cell cytokine production; • adaptive immune response; • immune system process; • innate immune response;
	Sources:Amigo / QuickGO
Orthologs
	383
	11846
	ENSG00000118520
	ENSMUSG00000019987
	P05089
	Q61176
	NM_000045; NM_001244438
	NM_007482
	NP_000036; NP_001231367
	NP_031508
	Wikidata
View/Edit Human	View/Edit Mouse

The human ARG1 gene encodes the protein arginase.^[5]

Function

Arginase catalyzes the hydrolysis of arginine to ornithine and urea. At least two isoforms of mammalian arginase exist (types I and II) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic function. The type I isoform encoded by this gene, is a cytosolic enzyme and expressed predominantly in the liver as a component of the urea cycle. Inherited deficiency of this enzyme results in argininemia, an autosomal recessive disorder characterized by hyperammonemia. Two transcript variants encoding different isoforms have been found for this gene.^[6]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000118520 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000019987 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ "Entrez Gene: Arginase, liver".
↑ [provided by RefSeq, Sep 2011]

External links

Human ARG1 genome location and ARG1 gene details page in the UCSC Genome Browser.

Morris CR, Kato GJ, Poljakovic M, Wang X, Blackwelder WC, Sachdev V, Hazen SL, Vichinsky EP, Morris SM, Gladwin MT (July 2005). "Dysregulated arginine metabolism, hemolysis-associated pulmonary hypertension, and mortality in sickle cell disease". JAMA. 294 (1): 81–90. doi:10.1001/jama.294.1.81. PMC 2065861. PMID 15998894.
Jiang M, Ding Y, Su Y, Hu X, Li J, Zhang Z (December 2006). "Arginase-flotillin interaction brings arginase to red blood cell membrane". FEBS Letters. 580 (28–29): 6561–4. doi:10.1016/j.febslet.2006.11.003. PMID 17113085.
Morris SM (July 2009). "Recent advances in arginine metabolism: roles and regulation of the arginases". British Journal of Pharmacology. 157 (6): 922–30. doi:10.1111/j.1476-5381.2009.00278.x. PMC 2737650. PMID 19508396.
Rotondo R, Bertolotto M, Barisione G, Astigiano S, Mandruzzato S, Ottonello L, Dallegri F, Bronte V, Ferrini S, Barbieri O (May 2011). "Exocytosis of azurophil and arginase 1-containing granules by activated polymorphonuclear neutrophils is required to inhibit T lymphocyte proliferation". Journal of Leukocyte Biology. 89 (5): 721–7. doi:10.1189/jlb.1109737. PMID 21330347.
Shapiro MB, Senapathy P (September 1987). "RNA splice junctions of different classes of eukaryotes: sequence statistics and functional implications in gene expression". Nucleic Acids Research. 15 (17): 7155–74. doi:10.1093/nar/15.17.7155. PMC 306199. PMID 3658675.
Rotondo R, Barisione G, Mastracci L, Grossi F, Orengo AM, Costa R, Truini M, Fabbi M, Ferrini S, Barbieri O (August 2009). "IL-8 induces exocytosis of arginase 1 by neutrophil polymorphonuclears in nonsmall cell lung cancer". International Journal of Cancer. 125 (4): 887–93. doi:10.1002/ijc.24448. PMID 19431148.
Salam MT, Bastain TM, Rappaport EB, Islam T, Berhane K, Gauderman WJ, Gilliland FD (March 2011). "Genetic variations in nitric oxide synthase and arginase influence exhaled nitric oxide levels in children". Allergy. 66 (3): 412–9. doi:10.1111/j.1398-9995.2010.02492.x. PMC 3058253. PMID 21039601.
Gannon PO, Godin-Ethier J, Hassler M, Delvoye N, Aversa M, Poisson AO, Péant B, Alam Fahmy M, Saad F, Lapointe R, Mes-Masson AM (August 2010). Creighton C, ed. "Androgen-regulated expression of arginase 1, arginase 2 and interleukin-8 in human prostate cancer". PLOS One. 5 (8): e12107. doi:10.1371/journal.pone.0012107. PMC 2920336. PMID 20711410.
Ishikawa T, Harada T, Koi H, Kubota T, Azuma H, Aso T (2007). "Identification of arginase in human placental villi". Placenta. 28 (2–3): 133–8. doi:10.1016/j.placenta.2006.03.015. PMID 16720041.

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

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000118520 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000019987 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[entrez-5] "Entrez Gene: Arginase, liver".

[6] [provided by RefSeq, Sep 2011]

ARG1 (gene)

Function

References

External links

Further reading