ARG2

Protein-coding gene in the species Homo sapiens
ARG2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1PQ3, 4HZE, 4I06, 4IE2, 4IE3, 4IXU, 4IXV

Identifiers
AliasesARG2, arginase 2
External IDsOMIM: 107830; MGI: 1330806; HomoloGene: 906; GeneCards: ARG2; OMA:ARG2 - orthologs
Gene location (Human)
Chromosome 14 (human)
Chr.Chromosome 14 (human)[1]
Chromosome 14 (human)
Genomic location for ARG2
Genomic location for ARG2
Band14q24.1Start67,619,920 bp[1]
End67,651,708 bp[1]
Gene location (Mouse)
Chromosome 12 (mouse)
Chr.Chromosome 12 (mouse)[2]
Chromosome 12 (mouse)
Genomic location for ARG2
Genomic location for ARG2
Band12|12 C3Start79,177,551 bp[2]
End79,203,075 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 12: 79.18 – 79.2 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Arginase, type II is an arginase protein that in humans is encoded by the ARG2 gene.[5]

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. ^ a b c GRCh38: Ensembl release 89: ENSG00000081181 – Ensembl, May 2017
  2. ^ a b c 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

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. S2CID 11365908.
  • 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. S2CID 23774473.
  • 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. S2CID 40117905.
  • 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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