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O08701 (ARGI2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginase-2, mitochondrial

EC=3.5.3.1
Alternative name(s):
Kidney-type arginase
Non-hepatic arginase
Type II arginase
Gene names
Name:Arg2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis By similarity.

Catalytic activity

L-arginine + H2O = L-ornithine + urea.

Cofactor

Binds 2 manganese ions per subunit By similarity.

Pathway

Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.

Subunit structure

Homotrimer By similarity.

Subcellular location

Mitochondrion.

Sequence similarities

Belongs to the arginase family.

Ontologies

Keywords
   Biological processArginine metabolism
Urea cycle
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from expression pattern PubMed 17874066. Source: RGD

arginine catabolic process to ornithine

Traceable author statement PubMed 14871882. Source: RGD

arginine metabolic process

Inferred from mutant phenotype PubMed 16537391. Source: RGD

cellular response to dexamethasone stimulus

Inferred from expression pattern PubMed 11250887. Source: RGD

cellular response to interferon-gamma

Inferred from expression pattern PubMed 11250887. Source: RGD

cellular response to interleukin-4

Inferred from expression pattern PubMed 14618299. Source: RGD

cellular response to lipopolysaccharide

Inferred from expression pattern PubMed 11250887. Source: RGD

lung development

Inferred from expression pattern PubMed 18192591. Source: RGD

maternal process involved in female pregnancy

Inferred from expression pattern PubMed 16735458. Source: RGD

midgut development

Inferred from expression pattern PubMed 10050048. Source: RGD

negative regulation of nitric-oxide synthase activity

Inferred from mutant phenotype PubMed 16537391. Source: RGD

negative regulation of striated muscle contraction

Inferred from mutant phenotype PubMed 16537391. Source: RGD

regulation of L-arginine import

Inferred from direct assay PubMed 11120661. Source: RGD

regulation of nitric oxide biosynthetic process

Inferred from expression pattern PubMed 11829529. Source: RGD

response to amine

Inferred from expression pattern PubMed 16168957. Source: RGD

response to amino acid

Inferred from expression pattern PubMed 15458774. Source: RGD

response to axon injury

Inferred from expression pattern PubMed 15735325. Source: RGD

response to cadmium ion

Inferred from expression pattern PubMed 16570515. Source: RGD

response to drug

Inferred from expression pattern PubMed 15888029. Source: RGD

response to glucose

Inferred from expression pattern PubMed 15254879. Source: RGD

response to herbicide

Inferred from expression pattern PubMed 20388547. Source: RGD

response to hormone

Inferred from expression pattern PubMed 14532164. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 20039818. Source: RGD

response to mercury ion

Inferred from expression pattern PubMed 17874066. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 18348861. Source: RGD

response to selenium ion

Inferred from expression pattern PubMed 14624471. Source: RGD

response to vitamin E

Inferred from expression pattern PubMed 14624471. Source: RGD

urea cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrion

Inferred from direct assay PubMed 16537391. Source: MGI

   Molecular_functionarginase activity

Inferred from direct assay PubMed 16537391. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nitric-oxide synthase binding

Inferred from physical interaction PubMed 16537391. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2222Mitochondrion Potential
Chain23 – 354332Arginase-2, mitochondrial
PRO_0000002086

Regions

Region145 – 1495Substrate binding By similarity
Region156 – 1583Substrate binding By similarity

Sites

Metal binding1201Manganese 1 By similarity
Metal binding1431Manganese 1 By similarity
Metal binding1431Manganese 2 By similarity
Metal binding1451Manganese 2 By similarity
Metal binding1471Manganese 1 By similarity
Metal binding2511Manganese 1 By similarity
Metal binding2511Manganese 2 By similarity
Metal binding2531Manganese 2 By similarity
Binding site2021Substrate By similarity
Binding site2961Substrate By similarity

Experimental info

Sequence conflict881Y → N in BAA13183. Ref.2
Sequence conflict901R → P in BAA13183. Ref.2
Sequence conflict1001A → S in BAA13183. Ref.2
Sequence conflict1161L → M in BAA13183. Ref.2
Sequence conflict1191D → Y in BAA13183. Ref.2
Sequence conflict1281S → I in BAA13183. Ref.2
Sequence conflict1431D → Y in BAA13183. Ref.2
Sequence conflict1641L → V in BAA13183. Ref.2
Sequence conflict1681I → L in BAA13183. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O08701 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: BC03E6BC99B29B8C

FASTA35438,640
        10         20         30         40         50         60 
MFLRSSVSRL LHGQIPCALT RSVHSVAVVG APFSRGQKKK GVEYGPAAIR EAGLLKRLSM 

        70         80         90        100        110        120 
LGCHIKDFGD LSFTNVPKDD PYNNLVVYPR SVGIANQELA EVVSRAVSGG YSCVTLGGDH 

       130        140        150        160        170        180 
SLAIGTISGH ARHHPDLCVI WVDAHADINT PLTTVSGNIH GQPLSFLIRE LQDKVPQLPG 

       190        200        210        220        230        240 
FSWIKPCLSP PNLVYIGLRD VEPAEHFILK SFDIQYFSMR DIDRLGIQKV MEQTFDRLIG 

       250        260        270        280        290        300 
KRKRPIHLSF DIDAFDPKLA PATGTPVVGG LTYREGLYIT EEIHSTGLLS ALDLVEVNPH 

       310        320        330        340        350 
LATSEEEAKA TASLAVDVIA SSFGQTREGG HIAYDHLPTP SSPHESEKEE CVRI 

« Hide

References

[1]"Cloning and characterization of the mouse and rat type II arginase genes."
Iyer R.K., Bando J.M., Jenkinson C.P., Vockley J.G., Kim P.S., Kern R.M., Cederbaum S.D., Grody W.W.
Mol. Genet. Metab. 63:168-175(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Kidney.
[2]"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."
Gotoh T., Sonoki T., Nagasaki A., Terada K., Takiguchi M., Mori M.
FEBS Lett. 395:119-122(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-168.
Strain: Wistar.
Tissue: Small intestine.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U90887 mRNA. Translation: AAC22580.1.
D86928 mRNA. Translation: BAA13183.1.
RefSeqNP_062041.1. NM_019168.1.
UniGeneRn.11055.

3D structure databases

ProteinModelPortalO08701.
SMRO08701. Positions 24-329.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbO08701.
PRIDEO08701.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29215.
KEGGrno:29215.
UCSCRGD:2151. rat.

Organism-specific databases

CTD384.
RGD2151. Arg2.

Phylogenomic databases

eggNOGCOG0010.
HOGENOMHOG000204319.
HOVERGENHBG003030.
InParanoidO08701.
KOK01476.
PhylomeDBO08701.

Enzyme and pathway databases

SABIO-RKO08701.
UniPathwayUPA00158; UER00270.

Gene expression databases

GenevestigatorO08701.

Family and domain databases

Gene3D3.40.800.10. 1 hit.
InterProIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERPTHR11358. PTHR11358. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFPIRSF036979. Arginase. 1 hit.
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01229. rocF_arginase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio608397.
PROO08701.

Entry information

Entry nameARGI2_RAT
AccessionPrimary (citable) accession number: O08701
Secondary accession number(s): P97539
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways