ARG1 (gene)

Mammalian protein found in Homo sapiens
ARG1
Available structures
PDBOrtholog 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
AliasesARG1, arginase 1
External IDsOMIM: 608313; MGI: 88070; HomoloGene: 29; GeneCards: ARG1; OMA:ARG1 - orthologs
Gene location (Human)
Chromosome 6 (human)
Chr.Chromosome 6 (human)[1]
Chromosome 6 (human)
Genomic location for ARG1
Genomic location for ARG1
Band6q23.2Start131,470,832 bp[1]
End131,584,332 bp[1]
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)[2]
Chromosome 10 (mouse)
Genomic location for ARG1
Genomic location for ARG1
Band10|10 A4Start24,791,119 bp[2]
End24,803,382 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right lobe of liver

  • human penis

  • skin of arm

  • trabecular bone

  • bone marrow

  • vulva

  • bone marrow cells

  • 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
  • neuronal cell body
  • 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
  • human 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
SpeciesHumanMouse
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 MbChr 10: 24.79 – 24.8 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000118520 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019987 – 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, liver".
  6. ^ [provided by RefSeq, Sep 2011]

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.


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