Arginase-1

ARG1
Identifiers
Aliases	ARG1, arginase 1
External IDs	OMIM: 608313; MGI: 88070; HomoloGene: 29; GeneCards: ARG1; OMA:ARG1 - orthologs
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
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 3.5.3.1 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 6 (human) Band 6q23.2 Start 131,470,832 bp End 131,584,332 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10|10 A4 Start 24,791,119 bp End 24,803,382 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver human penis skin of arm trabecular bone bone marrow vulva bone marrow cell skin of leg skin of hip skin of abdomen Top expressed in left lobe of liver gallbladder cervix parotid gland superior surface of tongue esophagus primitive streak somite corneal stroma lacrimal gland More reference expression data BioGPS n/a
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 protein binding Cellular component cytoplasm cytosol mitochondrial outer membrane soma neuron projection extracellular exosome 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 ageing 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 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 Species Human Mouse Entrez 383 11846 Ensembl ENSG00000118520 ENSMUSG00000019987 UniProt P05089 Q61176 RefSeq (mRNA) NM_000045 NM_001244438 NM_001369020 NM_007482 RefSeq (protein) NP_000036 NP_001231367 NP_001355949 NP_031508 Location (UCSC) Chr 6: 131.47 – 131.58 Mb Chr 10: 24.79 – 24.8 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Arginase-1 is a protein which in humans is encoded by the ARG1 gene.

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.

External links

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

Further reading

• 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. S2CID 20180459.
• 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. S2CID 25335372.
• 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. S2CID 205937936.
• 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. Bibcode:2010PLoSO...512107G. 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.