Arginase-2, mitochondrial

NameArginase-2, mitochondrial
Synonyms
  • 3.5.3.1
  • Kidney-type arginase
  • Non-hepatic arginase
  • Type II arginase
Gene NameARG2
OrganismHuman
Amino acid sequence
>lcl|BSEQ0010535|Arginase-2, mitochondrial
MSLRGSLSRLLQTRVHSILKKSVHSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSS
LGCHLKDFGDLSFTPVPKDDLYNNLIVNPRSVGLANQELAEVVSRAVSDGYSCVTLGGDH
SLAIGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVSFLLRELQDKVPQLPG
FSWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDIDRLGIQKVMERTFDLLIG
KRQRPIHLSFDIDAFDPTLAPATGTPVVGGLTYREGMYIAEEIHNTGLLSALDLVEVNPQ
LATSEEEAKTTANLAVDVIASSFGQTREGGHIVYDQLPTPSSPDESENQARVRI
Number of residues354
Molecular Weight38577.515
Theoretical pI6.45
GO Classification
Functions
  • arginase activity
  • metal ion binding
Processes
  • polyamine metabolic process
  • urea cycle
  • nitric oxide biosynthetic process
  • ureteric bud development
  • arginine metabolic process
  • striated muscle contraction
  • cellular nitrogen compound metabolic process
  • small molecule metabolic process
Components
  • mitochondrion
  • mitochondrial matrix
General FunctionMetal ion binding
Specific FunctionMay 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.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID1694633
UniProtKB IDP78540
UniProtKB Entry NameARGI2_HUMAN
Cellular LocationMitochondrion
Gene sequence
>lcl|BSEQ0010536|Arginase-2, mitochondrial (ARG2)
ATGTCCCTAAGGGGCAGCCTCTCGCGTCTCCTCCAGACGCGAGTGCATTCCATCCTGAAG
AAATCCGTCCACTCCGTGGCTGTGATAGGAGCCCCGTTCTCACAAGGGCAGAAAAGAAAA
GGAGTGGAGCATGGTCCCGCTGCCATAAGAGAAGCTGGCTTGATGAAAAGGCTCTCCAGT
TTGGGCTGCCACCTAAAAGACTTTGGAGATTTGAGTTTTACTCCAGTCCCCAAAGATGAT
CTCTACAACAACCTGATAGTGAATCCACGCTCAGTGGGTCTTGCCAACCAGGAACTGGCT
GAGGTGGTTAGCAGAGCTGTGTCAGATGGCTACAGCTGTGTCACACTGGGAGGAGACCAC
AGCCTGGCAATCGGTACCATTAGTGGCCATGCCCGACACTGCCCAGACCTTTGTGTTGTC
TGGGTTGATGCCCATGCTGACATCAACACACCCCTTACCACTTCATCAGGAAATCTCCAT
GGACAGCCAGTTTCATTTCTCCTCAGAGAACTACAGGATAAGGTACCACAACTCCCAGGA
TTTTCCTGGATCAAACCTTGTATCTCTTCTGCAAGTATTGTGTATATTGGTCTGAGAGAC
GTGGACCCTCCTGAACATTTTATTTTAAAGAACTATGATATCCAGTATTTTTCCATGAGA
GATATTGATCGACTTGGTATCCAGAAGGTCATGGAACGAACATTTGATCTGCTGATTGGC
AAGAGACAAAGACCAATCCATTTGAGTTTTGATATTGATGCATTTGACCCTACACTGGCT
CCAGCCACAGGAACTCCTGTTGTCGGGGGACTAACCTATCGAGAAGGCATGTATATTGCT
GAGGAAATACACAATACAGGGTTGCTATCAGCACTGGATCTTGTTGAAGTCAATCCTCAG
TTGGCCACCTCAGAGGAAGAGGCGAAGACTACAGCTAACCTGGCAGTAGATGTGATTGCT
TCAAGCTTTGGTCAGACAAGAGAAGGAGGGCATATTGTCTATGACCAACTTCCTACTCCC
AGTTCACCAGATGAATCAGAAAATCAAGCACGTGTGAGAATTTAG
GenBank Gene IDD86724
GeneCard IDNot Available
GenAtlas IDARG2
HGNC IDHGNC:664
Chromosome Location14
Locus14q24.1-q24.3
References
  1. 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. 8898077
  2. 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. 8954792
  3. 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. 9256072
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