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O08701

- ARGI2_RAT

UniProt

O08701 - ARGI2_RAT

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Protein
Arginase-2, mitochondrial
Gene
Arg2
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

Cofactori

Binds 2 manganese ions per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi120 – 1201Manganese 1 By similarity
Metal bindingi143 – 1431Manganese 1 By similarity
Metal bindingi143 – 1431Manganese 2 By similarity
Metal bindingi145 – 1451Manganese 2 By similarity
Metal bindingi147 – 1471Manganese 1 By similarity
Binding sitei202 – 2021Substrate By similarity
Metal bindingi251 – 2511Manganese 1 By similarity
Metal bindingi251 – 2511Manganese 2 By similarity
Metal bindingi253 – 2531Manganese 2 By similarity
Binding sitei296 – 2961Substrate By similarity

GO - Molecular functioni

  1. arginase activity Source: MGI
  2. metal ion binding Source: UniProtKB-KW
  3. nitric-oxide synthase binding Source: RGD
  4. protein binding Source: RGD

GO - Biological processi

  1. apoptotic process Source: RGD
  2. arginine catabolic process to ornithine Source: RGD
  3. arginine metabolic process Source: RGD
  4. cellular response to dexamethasone stimulus Source: RGD
  5. cellular response to interferon-gamma Source: RGD
  6. cellular response to interleukin-4 Source: RGD
  7. cellular response to lipopolysaccharide Source: RGD
  8. lung development Source: RGD
  9. maternal process involved in female pregnancy Source: RGD
  10. midgut development Source: RGD
  11. negative regulation of nitric-oxide synthase activity Source: RGD
  12. negative regulation of striated muscle contraction Source: RGD
  13. regulation of L-arginine import Source: RGD
  14. regulation of nitric oxide biosynthetic process Source: RGD
  15. response to amine Source: RGD
  16. response to amino acid Source: RGD
  17. response to axon injury Source: RGD
  18. response to cadmium ion Source: RGD
  19. response to drug Source: RGD
  20. response to glucose Source: RGD
  21. response to herbicide Source: RGD
  22. response to hormone Source: RGD
  23. response to hypoxia Source: RGD
  24. response to mercury ion Source: RGD
  25. response to nutrient Source: RGD
  26. response to selenium ion Source: RGD
  27. response to vitamin E Source: RGD
  28. 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

SABIO-RKO08701.
UniPathwayiUPA00158; UER00270.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginase-2, mitochondrial (EC:3.5.3.1)
Alternative name(s):
Kidney-type arginase
Non-hepatic arginase
Type II arginase
Gene namesi
Name:Arg2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2151. Arg2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2222Mitochondrion Reviewed prediction
Add
BLAST
Chaini23 – 354332Arginase-2, mitochondrial
PRO_0000002086Add
BLAST

Proteomic databases

PaxDbiO08701.
PRIDEiO08701.

Expressioni

Gene expression databases

GenevestigatoriO08701.

Interactioni

Subunit structurei

Homotrimer By similarity.

Structurei

3D structure databases

ProteinModelPortaliO08701.
SMRiO08701. Positions 24-329.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni145 – 1495Substrate binding By similarity
Regioni156 – 1583Substrate binding By similarity

Sequence similaritiesi

Belongs to the arginase family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0010.
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

MFLRSSVSRL LHGQIPCALT RSVHSVAVVG APFSRGQKKK GVEYGPAAIR    50
EAGLLKRLSM LGCHIKDFGD LSFTNVPKDD PYNNLVVYPR SVGIANQELA 100
EVVSRAVSGG YSCVTLGGDH SLAIGTISGH ARHHPDLCVI WVDAHADINT 150
PLTTVSGNIH GQPLSFLIRE LQDKVPQLPG FSWIKPCLSP PNLVYIGLRD 200
VEPAEHFILK SFDIQYFSMR DIDRLGIQKV MEQTFDRLIG KRKRPIHLSF 250
DIDAFDPKLA PATGTPVVGG LTYREGLYIT EEIHSTGLLS ALDLVEVNPH 300
LATSEEEAKA TASLAVDVIA SSFGQTREGG HIAYDHLPTP SSPHESEKEE 350
CVRI 354
Length:354
Mass (Da):38,640
Last modified:July 1, 1997 - v1
Checksum:iBC03E6BC99B29B8C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881Y → N in BAA13183. 1 Publication
Sequence conflicti90 – 901R → P in BAA13183. 1 Publication
Sequence conflicti100 – 1001A → S in BAA13183. 1 Publication
Sequence conflicti116 – 1161L → M in BAA13183. 1 Publication
Sequence conflicti119 – 1191D → Y in BAA13183. 1 Publication
Sequence conflicti128 – 1281S → I in BAA13183. 1 Publication
Sequence conflicti143 – 1431D → Y in BAA13183. 1 Publication
Sequence conflicti164 – 1641L → V in BAA13183. 1 Publication
Sequence conflicti168 – 1681I → L in BAA13183. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U90887 mRNA. Translation: AAC22580.1 .
D86928 mRNA. Translation: BAA13183.1 .
RefSeqi NP_062041.1. NM_019168.1.
UniGenei Rn.11055.

3D structure databases

ProteinModelPortali O08701.
SMRi O08701. Positions 24-329.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi O08701.
PRIDEi O08701.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 29215.
KEGGi rno:29215.
UCSCi RGD:2151. rat.

Organism-specific databases

CTDi 384.
RGDi 2151. Arg2.

Phylogenomic databases

eggNOGi COG0010.
HOGENOMi HOG000204319.
HOVERGENi HBG003030.
InParanoidi O08701.
KOi K01476.
PhylomeDBi O08701.

Enzyme and pathway databases

UniPathwayi UPA00158 ; UER00270 .
SABIO-RK O08701.

Miscellaneous databases

NextBioi 608397.
PROi O08701.

Gene expression databases

Genevestigatori O08701.

Family and domain databases

Gene3Di 3.40.800.10. 1 hit.
InterProi IPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view ]
PANTHERi PTHR11358. PTHR11358. 1 hit.
Pfami PF00491. Arginase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036979. Arginase. 1 hit.
PRINTSi PR00116. ARGINASE.
TIGRFAMsi TIGR01229. rocF_arginase. 1 hit.
PROSITEi PS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

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: June 11, 2014
This is version 107 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

External Data

Dasty 3

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