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Identification
HMDB Protein ID HMDBP01035
Secondary Accession Numbers
  • 6323
  • HMDBP03499
Name Arginase-2, mitochondrial
Synonyms
  1. Kidney-type arginase
  2. Non-hepatic arginase
  3. Type II arginase
Gene Name ARG2
Protein Type Unknown
Biological Properties
General Function Involved in arginase activity
Specific Function May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to NO synthase. Since NO synthase is found in the penile corpus cavernosum smooth muscle, the clitoral corpus cavernosum and the vagina, arginase II plays a role in both male and female sexual arousal. It is therefore a potential target for the treatment of male and female sexual arousal disorders.
Pathways
  • Amoebiasis
  • Arginine and proline metabolism
  • urea cycle
Reactions
L-Arginine + Water → Ornithine + Urea details
GO Classification
Biological Process
response to cadmium ion
striated muscle contraction
response to amino acid stimulus
apoptotic process
response to drug
negative regulation of nitric-oxide synthase activity
cellular response to lipopolysaccharide
response to glucose stimulus
lung development
response to selenium ion
midgut development
cellular response to dexamethasone stimulus
maternal process involved in female pregnancy
regulation of L-arginine import
response to amine stimulus
response to axon injury
response to hypoxia
response to herbicide
response to vitamin E
urea cycle
arginine metabolic process
cellular response to interferon-gamma
negative regulation of striated muscle contraction
nitric oxide biosynthetic process
regulation of nitric oxide biosynthetic process
response to mercury ion
ureteric bud development
Cellular Component
mitochondrial matrix
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
arginase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Molecular Function
metal ion binding
arginase activity
Process
metabolic process
arginine metabolic process
cellular metabolic process
glutamine family amino acid metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
Cellular Location
  1. Mitochondrion
Gene Properties
Chromosome Location 14
Locus 14q24.1
SNPs ARG2
Gene Sequence
>1065 bp
ATGTCCCTAAGGGGCAGCCTCTCGCGTCTCCTCCAGACGCGAGTGCATTCCATCCTGAAG
AAATCCGTCCACTCCGTGGCTGTGATAGGAGCCCCGTTCTCACAAGGGCAGAAAAGAAAA
GGAGTGGAGCATGGTCCCGCTGCCATAAGAGAAGCTGGCTTGATGAAAAGGCTCTCCAGT
TTGGGCTGCCACCTAAAAGACTTTGGAGATTTGAGTTTTACTCCAGTCCCCAAAGATGAT
CTCTACAACAACCTGATAGTGAATCCACGCTCAGTGGGTCTTGCCAACCAGGAACTGGCT
GAGGTGGTTAGCAGAGCTGTGTCAGATGGCTACAGCTGTGTCACACTGGGAGGAGACCAC
AGCCTGGCAATCGGTACCATTAGTGGCCATGCCCGACACTGCCCAGACCTTTGTGTTGTC
TGGGTTGATGCCCATGCTGACATCAACACACCCCTTACCACTTCATCAGGAAATCTCCAT
GGACAGCCAGTTTCATTTCTCCTCAGAGAACTACAGGATAAGGTACCACAACTCCCAGGA
TTTTCCTGGATCAAACCTTGTATCTCTTCTGCAAGTATTGTGTATATTGGTCTGAGAGAC
GTGGACCCTCCTGAACATTTTATTTTAAAGAACTATGATATCCAGTATTTTTCCATGAGA
GATATTGATCGACTTGGTATCCAGAAGGTCATGGAACGAACATTTGATCTGCTGATTGGC
AAGAGACAAAGACCAATCCATTTGAGTTTTGATATTGATGCATTTGACCCTACACTGGCT
CCAGCCACAGGAACTCCTGTTGTCGGGGGACTAACCTATCGAGAAGGCATGTATATTGCT
GAGGAAATACACAATACAGGGTTGCTATCAGCACTGGATCTTGTTGAAGTCAATCCTCAG
TTGGCCACCTCAGAGGAAGAGGCGAAGACTACAGCTAACCTGGCAGTAGATGTGATTGCT
TCAAGCTTTGGTCAGACAAGAGAAGGAGGGCATATTGTCTATGACCAACTTCCTACTCCC
AGTTCACCAGATGAATCAGAAAATCAAGCACGTGTGAGAATTTAG
Protein Properties
Number of Residues 354
Molecular Weight 38577.515
Theoretical pI 6.468
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Arginase-2, mitochondrial
MSLRGSLSRLLQTRVHSILKKSVHSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSS
LGCHLKDFGDLSFTPVPKDDLYNNLIVNPRSVGLANQELAEVVSRAVSDGYSCVTLGGDH
SLAIGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVSFLLRELQDKVPQLPG
FSWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDIDRLGIQKVMERTFDLLIG
KRQRPIHLSFDIDAFDPTLAPATGTPVVGGLTYREGMYIAEEIHNTGLLSALDLVEVNPQ
LATSEEEAKTTANLAVDVIASSFGQTREGGHIVYDQLPTPSSPDESENQARVRI
GenBank ID Protein 189065548
UniProtKB/Swiss-Prot ID P78540
UniProtKB/Swiss-Prot Entry Name ARGI2_HUMAN
PDB IDs
GenBank Gene ID AK312484
GeneCard ID ARG2
GenAtlas ID ARG2
HGNC ID HGNC:664
References
General References
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  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Gotoh T, Sonoki T, Nagasaki A, Terada K, Takiguchi M, Mori M: 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 Lett. 1996 Oct 21;395(2-3):119-22. [PubMed:8898077 ]
  4. Vockley JG, Jenkinson CP, Shukla H, Kern RM, Grody WW, Cederbaum SD: Cloning and characterization of the human type II arginase gene. Genomics. 1996 Dec 1;38(2):118-23. [PubMed:8954792 ]
  5. Morris SM Jr, Bhamidipati D, Kepka-Lenhart D: Human type II arginase: sequence analysis and tissue-specific expression. Gene. 1997 Jul 9;193(2):157-61. [PubMed:9256072 ]
  6. Cama E, Colleluori DM, Emig FA, Shin H, Kim SW, Kim NN, Traish AM, Ash DE, Christianson DW: Human arginase II: crystal structure and physiological role in male and female sexual arousal. Biochemistry. 2003 Jul 22;42(28):8445-51. [PubMed:12859189 ]