CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010432
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Arginase-2, mitochondrial 
Protein Synonyms/Alias
 Kidney-type arginase; Non-hepatic arginase; Type II arginase 
Gene Name
 ARG2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
56IREAGLMKRLSSLGCacetylation[1]
78LSFTPVPKDDLYNNLubiquitination[2]
241TFDLLIGKRQRPIHLubiquitination[2]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
 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. 
Sequence Annotation
 REGION 145 149 Substrate binding (By similarity).
 REGION 156 158 Substrate binding (By similarity).
 METAL 120 120 Manganese 1.
 METAL 143 143 Manganese 1.
 METAL 143 143 Manganese 2.
 METAL 145 145 Manganese 2.
 METAL 147 147 Manganese 1.
 METAL 251 251 Manganese 1.
 METAL 251 251 Manganese 2.
 METAL 253 253 Manganese 2.
 BINDING 202 202 Substrate (By similarity).
 BINDING 296 296 Substrate (By similarity).  
Keyword
 3D-structure; Arginine metabolism; Complete proteome; Hydrolase; Manganese; Metal-binding; Mitochondrion; Polymorphism; Reference proteome; Transit peptide; Urea cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 354 AA 
Protein Sequence
MSLRGSLSRL LQTRVHSILK KSVHSVAVIG APFSQGQKRK GVEHGPAAIR EAGLMKRLSS 60
LGCHLKDFGD LSFTPVPKDD LYNNLIVNPR SVGLANQELA EVVSRAVSDG YSCVTLGGDH 120
SLAIGTISGH ARHCPDLCVV WVDAHADINT PLTTSSGNLH GQPVSFLLRE LQDKVPQLPG 180
FSWIKPCISS ASIVYIGLRD VDPPEHFILK NYDIQYFSMR DIDRLGIQKV MERTFDLLIG 240
KRQRPIHLSF DIDAFDPTLA PATGTPVVGG LTYREGMYIA EEIHNTGLLS ALDLVEVNPQ 300
LATSEEEAKT TANLAVDVIA SSFGQTREGG HIVYDQLPTP SSPDESENQA RVRI 354 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0004053; F:arginase activity; EXP:Reactome.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
 GO:0006809; P:nitric oxide biosynthetic process; TAS:ProtInc.
 GO:0006941; P:striated muscle contraction; IEA:Compara.
 GO:0000050; P:urea cycle; TAS:Reactome.
 GO:0001657; P:ureteric bud development; IEA:Compara. 
Interpro
 IPR014033; Arginase.
 IPR006035; Ureohydrolase.
 IPR023696; Ureohydrolase_domain.
 IPR020855; Ureohydrolase_Mn_BS. 
Pfam
 PF00491; Arginase 
SMART
  
PROSITE
 PS01053; ARGINASE_1
 PS51409; ARGINASE_2 
PRINTS
 PR00116; ARGINASE.