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Protein

Arginase-2, mitochondrial

Gene

Arg2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

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

Cofactori

Mn2+PROSITE-ProRule annotationNote: Binds 2 manganese ions per subunit.PROSITE-ProRule annotation

Pathwayi: urea cycle

This protein is involved in step 1 of the subpathway that synthesizes L-ornithine and urea from L-arginine.By similarity
Proteins known to be involved in this subpathway in this organism are:
  1. Arginase-1 (Arg1), Arginase (Arg2), Arginase-2, mitochondrial (Arg2), Arginase (Arg2)
This subpathway is part of the pathway urea cycle, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-ornithine and urea from L-arginine, the pathway urea cycle and in Nitrogen metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi120Manganese 1PROSITE-ProRule annotation1
Metal bindingi143Manganese 1PROSITE-ProRule annotation1
Metal bindingi143Manganese 2PROSITE-ProRule annotation1
Metal bindingi145Manganese 2PROSITE-ProRule annotation1
Metal bindingi147Manganese 1PROSITE-ProRule annotation1
Binding sitei202SubstrateBy similarity1
Metal bindingi251Manganese 1PROSITE-ProRule annotation1
Metal bindingi251Manganese 2PROSITE-ProRule annotation1
Metal bindingi253Manganese 2PROSITE-ProRule annotation1
Binding sitei265SubstrateBy similarity1
Binding sitei296SubstrateBy similarity1

GO - Molecular functioni

  • arginase activity Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • nitric-oxide synthase binding Source: RGD

GO - Biological processi

  • apoptotic process Source: RGD
  • arginine catabolic process to ornithine Source: RGD
  • arginine metabolic process Source: RGD
  • cellular response to dexamethasone stimulus Source: RGD
  • cellular response to interferon-gamma Source: RGD
  • cellular response to interleukin-4 Source: RGD
  • cellular response to lipopolysaccharide Source: RGD
  • lung development Source: RGD
  • maternal process involved in female pregnancy Source: RGD
  • midgut development Source: RGD
  • negative regulation of nitric-oxide synthase activity Source: RGD
  • negative regulation of striated muscle contraction Source: RGD
  • regulation of L-arginine import Source: RGD
  • regulation of nitric oxide biosynthetic process Source: RGD
  • response to amine Source: RGD
  • response to amino acid Source: RGD
  • response to axon injury Source: RGD
  • response to cadmium ion Source: RGD
  • response to drug Source: RGD
  • response to glucose Source: RGD
  • response to herbicide Source: RGD
  • response to hormone Source: RGD
  • response to hypoxia Source: RGD
  • response to mercury ion Source: RGD
  • response to nutrient Source: RGD
  • response to selenium ion Source: RGD
  • response to vitamin E Source: RGD
  • urea cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Arginine metabolism, Urea cycle

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi3.5.3.1. 5301.
SABIO-RKO08701.
UniPathwayiUPA00158; UER00270.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginase-2, mitochondrial (EC:3.5.3.1By similarity)
Alternative name(s):
Kidney-type arginase
Non-hepatic arginase
Type II arginase
Gene namesi
Name:Arg2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2151. Arg2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 22MitochondrionSequence analysisAdd BLAST22
ChainiPRO_000000208623 – 354Arginase-2, mitochondrialAdd BLAST332

Proteomic databases

PaxDbiO08701.
PRIDEiO08701.

Interactioni

Subunit structurei

Homotrimer.By similarity

GO - Molecular functioni

  • nitric-oxide synthase binding Source: RGD

Protein-protein interaction databases

DIPiDIP-61133N.
STRINGi10116.ENSRNOP00000015083.

Structurei

3D structure databases

ProteinModelPortaliO08701.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni145 – 149Substrate bindingBy similarity5
Regioni156 – 158Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the arginase family.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2965. Eukaryota.
COG0010. LUCA.
HOGENOMiHOG000204319.
HOVERGENiHBG003030.
InParanoidiO08701.
KOiK01476.
PhylomeDBiO08701.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O08701-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLRSSVSRL LHGQIPCALT RSVHSVAVVG APFSRGQKKK GVEYGPAAIR
60 70 80 90 100
EAGLLKRLSM LGCHIKDFGD LSFTNVPKDD PYNNLVVYPR SVGIANQELA
110 120 130 140 150
EVVSRAVSGG YSCVTLGGDH SLAIGTISGH ARHHPDLCVI WVDAHADINT
160 170 180 190 200
PLTTVSGNIH GQPLSFLIRE LQDKVPQLPG FSWIKPCLSP PNLVYIGLRD
210 220 230 240 250
VEPAEHFILK SFDIQYFSMR DIDRLGIQKV MEQTFDRLIG KRKRPIHLSF
260 270 280 290 300
DIDAFDPKLA PATGTPVVGG LTYREGLYIT EEIHSTGLLS ALDLVEVNPH
310 320 330 340 350
LATSEEEAKA TASLAVDVIA SSFGQTREGG HIAYDHLPTP SSPHESEKEE

CVRI
Length:354
Mass (Da):38,640
Last modified:July 1, 1997 - v1
Checksum:iBC03E6BC99B29B8C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti88Y → N in BAA13183 (PubMed:8898077).Curated1
Sequence conflicti90R → P in BAA13183 (PubMed:8898077).Curated1
Sequence conflicti100A → S in BAA13183 (PubMed:8898077).Curated1
Sequence conflicti116L → M in BAA13183 (PubMed:8898077).Curated1
Sequence conflicti119D → Y in BAA13183 (PubMed:8898077).Curated1
Sequence conflicti128S → I in BAA13183 (PubMed:8898077).Curated1
Sequence conflicti143D → Y in BAA13183 (PubMed:8898077).Curated1
Sequence conflicti164L → V in BAA13183 (PubMed:8898077).Curated1
Sequence conflicti168I → L in BAA13183 (PubMed:8898077).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90887 mRNA. Translation: AAC22580.1.
D86928 mRNA. Translation: BAA13183.1.
RefSeqiNP_062041.1. NM_019168.1.
UniGeneiRn.11055.

Genome annotation databases

GeneIDi29215.
KEGGirno:29215.
UCSCiRGD:2151. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90887 mRNA. Translation: AAC22580.1.
D86928 mRNA. Translation: BAA13183.1.
RefSeqiNP_062041.1. NM_019168.1.
UniGeneiRn.11055.

3D structure databases

ProteinModelPortaliO08701.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61133N.
STRINGi10116.ENSRNOP00000015083.

Proteomic databases

PaxDbiO08701.
PRIDEiO08701.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29215.
KEGGirno:29215.
UCSCiRGD:2151. rat.

Organism-specific databases

CTDi384.
RGDi2151. Arg2.

Phylogenomic databases

eggNOGiKOG2965. Eukaryota.
COG0010. LUCA.
HOGENOMiHOG000204319.
HOVERGENiHBG003030.
InParanoidiO08701.
KOiK01476.
PhylomeDBiO08701.

Enzyme and pathway databases

UniPathwayiUPA00158; UER00270.
BRENDAi3.5.3.1. 5301.
SABIO-RKO08701.

Miscellaneous databases

PROiO08701.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiARGI2_RAT
AccessioniPrimary (citable) accession number: O08701
Secondary accession number(s): P97539
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: October 5, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.