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O08691 (ARGI2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2222Mitochondrion Potential
Chain23 – 354332Arginase-2, mitochondrial
PRO_0000002085

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

Sequences

Sequence LengthMass (Da)Tools
O08691 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: B372DF68A19473F2

FASTA35438,878
        10         20         30         40         50         60 
MFLRSSASRL LHGQIPCVLT RSVHSVAIVG APFSRGQKKL GVEYGPAAIR EAGLLKRLSR 

        70         80         90        100        110        120 
LGCHLKDFGD LSFTNVPQDD PYNNLVVYPR SVGLANQELA EVVSRAVSGG YSCVTMGGDH 

       130        140        150        160        170        180 
SLAIGTIIGH ARHRPDLCVI WVDAHADINT PLTTVSGNIH GQPLSFLIKE LQDKVPQLPG 

       190        200        210        220        230        240 
FSWIKPCLSP PNIVYIGLRD VEPPEHFILK NYDIQYFSMR EIDRLGIQKV MEQTFDRLIG 

       250        260        270        280        290        300 
KRQRPIHLSF DIDAFDPKLA PATGTPVVGG LTYREGVYIT EEIHNTGLLS ALDLVEVNPH 

       310        320        330        340        350 
LATSEEEAKA TARLAVDVIA SSFGQTREGG HIVYDHLPTP SSPHESENEE 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: 9608538] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Kidney.
[2]"Differential regulation of arginases and inducible nitric oxide synthase in murine macrophage cells."
Morris S.M. Jr., Kepka-Lenhart D., Chen L.C.
Am. J. Physiol. 275:E740-E747(1998) [PubMed: 9814991] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[3]"Structure of the murine arginase II gene."
Shi O.U., Kepka-Lenhart D., Morris S.M. Jr., O'Brien W.E.
Mamm. Genome 9:822-824(1998) [PubMed: 9745037] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[4]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 51-57, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U90886 mRNA. Translation: AAC22548.1.
AF032466 mRNA. Translation: AAB86959.1.
AF045965 expand/collapse EMBL AC list , AF044680, AF045959, AF045960, AF045961, AF045962, AF045963, AF045964 Genomic DNA. Translation: AAC78460.1.
IPIIPI00114974.
RefSeqNP_033835.1. NM_009705.3.
UniGeneMm.3506.

3D structure databases

ProteinModelPortalO08691.
SMRO08691. Positions 24-329.
ModBaseSearch...

Protein-protein interaction databases

STRINGO08691.

PTM databases

PhosphoSiteO08691.

2D gel databases

REPRODUCTION-2DPAGEO08691.

Proteomic databases

PRIDEO08691.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021550; ENSMUSP00000021550; ENSMUSG00000021125.
GeneID11847.
KEGGmmu:11847.
UCSCuc007nzv.2. mouse.

Organism-specific databases

CTD384.
MGIMGI:1330806. Arg2.

Phylogenomic databases

eggNOGroNOG04538.
HOGENOMHBG391953.
HOVERGENHBG003030.
InParanoidO08691.
OMADYNTPAT.
OrthoDBEOG4FR0S2.
PhylomeDBO08691.

Gene expression databases

ArrayExpressO08691.
BgeeO08691.
CleanExMM_ARG2.
GenevestigatorO08691.
GermOnlineENSMUSG00000021125. Mus musculus.

Family and domain databases

InterProIPR014033. Arginase_subgr.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
Gene3DG3DSA:3.40.800.10. Ureohydrolase. 1 hit.
KOK01476.
PANTHERPTHR11358:SF2. Arginase_sub. 1 hit.
PTHR11358. Ureohydrolase. 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

NextBio279811.
SOURCESearch...

Entry information

Entry nameARGI2_MOUSE
AccessionPrimary (citable) accession number: O08691
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: November 16, 2011
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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