O08701 (ARGI2_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	354 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Arginine metabolism Urea cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from expression pattern PubMed 17874066. Source: RGD arginine catabolic process to ornithine Traceable author statement PubMed 14871882. 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 stimulus Inferred from expression pattern PubMed 16168957. Source: RGD response to amino acid stimulus 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 stimulus Inferred from expression pattern PubMed 15254879. Source: RGD response to herbicide Inferred from expression pattern PubMed 20388547. 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 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_component	mitochondrion Inferred from direct assay PubMed 16537391. Source: MGI
Molecular_function	arginase activity Inferred from direct assay PubMed 16537391. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 22	22	Mitochondrion Potential
	Chain	23 – 354	332	Arginase-2, mitochondrial		PRO_0000002086
Regions
	Region	145 – 149	5	Substrate binding By similarity
	Region	156 – 158	3	Substrate binding By similarity
Sites
	Metal binding	120	1	Manganese 1 By similarity
	Metal binding	143	1	Manganese 1 By similarity
	Metal binding	143	1	Manganese 2 By similarity
	Metal binding	145	1	Manganese 2 By similarity
	Metal binding	147	1	Manganese 1 By similarity
	Metal binding	251	1	Manganese 1 By similarity
	Metal binding	251	1	Manganese 2 By similarity
	Metal binding	253	1	Manganese 2 By similarity
	Binding site	202	1	Substrate By similarity
	Binding site	296	1	Substrate By similarity
Experimental info
	Sequence conflict	88	1	Y → N in BAA13183. Ref.2
	Sequence conflict	90	1	R → P in BAA13183. Ref.2
	Sequence conflict	100	1	A → S in BAA13183. Ref.2
	Sequence conflict	116	1	L → M in BAA13183. Ref.2
	Sequence conflict	119	1	D → Y in BAA13183. Ref.2
	Sequence conflict	128	1	S → I in BAA13183. Ref.2
	Sequence conflict	143	1	D → Y in BAA13183. Ref.2
	Sequence conflict	164	1	L → V in BAA13183. Ref.2
	Sequence conflict	168	1	I → L in BAA13183. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O08701 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: BC03E6BC99B29B8C	FASTA	354	38,640
	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

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.
IPI	IPI00231829.
RefSeq	NP_062041.1. NM_019168.1.
UniGene	Rn.11055.
3D structure databases
ProteinModelPortal	O08701.
SMR	O08701. Positions 24-329.
ModBase	Search...
Proteomic databases
PaxDb	O08701.
PRIDE	O08701.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	29215.
KEGG	rno:29215.
UCSC	RGD:2151. rat.
Organism-specific databases
CTD	384.
RGD	2151. Arg2.
Phylogenomic databases
eggNOG	COG0010.
HOGENOM	HOG000204319.
HOVERGEN	HBG003030.
InParanoid	O08701.
KO	K01476.
OrthoDB	EOG4FR0S2.
Enzyme and pathway databases
SABIO-RK	O08701.
UniPathway	UPA00158; UER00270.
Gene expression databases
Genevestigator	O08701.
GermOnline	ENSRNOG00000011139. Rattus norvegicus.
Family and domain databases
Gene3D	3.40.800.10. 1 hit.
InterPro	IPR014033. Arginase. IPR006035. Ureohydrolase. IPR023696. Ureohydrolase_domain. IPR020855. Ureohydrolase_Mn_BS. [Graphical view]
PANTHER	PTHR11358. PTHR11358. 1 hit.
Pfam	PF00491. Arginase. 1 hit. [Graphical view]
PIRSF	PIRSF036979. Arginase. 1 hit.
PRINTS	PR00116. ARGINASE.
TIGRFAMs	TIGR01229. rocF_arginase. 1 hit.
PROSITE	PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	608397.

Entry information

Entry name

ARGI2_RAT

Accession

Primary (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 3, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program