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P07824 (ARGI1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-1

EC=3.5.3.1
Alternative name(s):
Liver-type arginase
Type I arginase
Gene names
Name:Arg1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 manganese ions per subunit. Ref.8 Ref.10

Enzyme regulation

Inactivated by diethyl pyrocarbonate (DEPC).

Pathway

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

Subunit structure

Homotrimer.

Subcellular location

Cytoplasm.

Tissue specificity

Detected in liver (at protein level). Ref.10

Induction

By arginine or homoarginine.

Sequence similarities

Belongs to the arginase family.

Biophysicochemical properties

Kinetic parameters:

KM=1.4 mM for arginine Ref.8 Ref.10

Ontologies

Keywords
   Biological processArginine metabolism
Urea cycle
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarginine metabolic process

Inferred from direct assay PubMed 4062872. Source: RGD

cellular response to dexamethasone stimulus

Inferred from expression pattern PubMed 11250887. Source: RGD

cellular response to glucagon stimulus

Inferred from expression pattern PubMed 8460937. Source: RGD

cellular response to hydrogen peroxide

Inferred from expression pattern PubMed 18001708. Source: RGD

cellular response to interleukin-4

Inferred from expression pattern PubMed 14618299. Source: RGD

cellular response to lipopolysaccharide

Inferred from expression pattern PubMed 9013624. Source: RGD

cellular response to transforming growth factor beta stimulus

Inferred from expression pattern PubMed 12069499. Source: RGD

collagen biosynthetic process

Inferred from mutant phenotype PubMed 20107769. Source: RGD

female pregnancy

Inferred from expression pattern PubMed 7649538. Source: RGD

liver development

Inferred from expression pattern PubMed 8690412. Source: RGD

lung development

Inferred from expression pattern PubMed 18192591. Source: RGD

mammary gland involution

Inferred from expression pattern PubMed 20110414. Source: RGD

maternal process involved in female pregnancy

Inferred from expression pattern PubMed 16735458. Source: RGD

positive regulation of endothelial cell proliferation

Inferred from direct assay PubMed 11742824. Source: RGD

protein homotrimerization

Inferred from direct assay PubMed 1569574. Source: RGD

regulation of L-arginine import

Inferred from direct assay PubMed 11120661. Source: RGD

response to amine

Inferred from expression pattern PubMed 16459053. 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 herbicide

Inferred from expression pattern PubMed 20388547. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 10652239PubMed 9686345. Source: RGD

response to manganese ion

Inferred from expression pattern PubMed 15564441. Source: RGD

response to methylmercury

Inferred from expression pattern PubMed 18488197. Source: RGD

response to peptide hormone

Inferred from expression pattern PubMed 19386725. Source: RGD

response to selenium ion

Inferred from expression pattern PubMed 14624471. Source: RGD

response to steroid hormone

Inferred from expression pattern PubMed 9688877. Source: RGD

response to vitamin A

Inferred from expression pattern PubMed 18271400. Source: RGD

response to vitamin E

Inferred from expression pattern PubMed 14624471. Source: RGD

response to wounding

Inferred from expression pattern PubMed 12069499. Source: RGD

response to zinc ion

Inferred from expression pattern PubMed 11686772. Source: RGD

urea cycle

Inferred from direct assay PubMed 4062872. Source: RGD

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11931836. Source: RGD

extracellular space

Inferred from direct assay PubMed 16872590. Source: RGD

neuron projection

Inferred from direct assay PubMed 16914676. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 16914676. Source: RGD

   Molecular_functionarginase activity

Inferred from direct assay PubMed 12069499PubMed 4062872. Source: RGD

manganese ion binding

Inferred from direct assay Ref.8. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323Arginase-1
PRO_0000173697

Regions

Region126 – 1305Substrate binding
Region137 – 1393Substrate binding

Sites

Metal binding1011Manganese 1
Metal binding1241Manganese 1
Metal binding1241Manganese 2
Metal binding1261Manganese 2
Metal binding1281Manganese 1
Metal binding2321Manganese 1
Metal binding2321Manganese 2
Metal binding2341Manganese 2
Binding site1831Substrate

Amino acid modifications

Modified residue171N6-succinyllysine By similarity
Modified residue721Phosphoserine By similarity
Modified residue751N6-succinyllysine By similarity
Modified residue2811Phosphothreonine By similarity

Experimental info

Mutagenesis1011H → E: Reduced catalytic activity. No effect on manganese binding. Ref.8
Mutagenesis1281D → E or N: Reduced manganese binding and strongly reduced catalytic activity. Ref.8
Mutagenesis1411H → A, C or D: Strongly reduced catalytic activity. Minor effect on affinity for arginine. Ref.10
Mutagenesis1411H → N: Reduced affinity for arginine and reduced catalytic activity. Ref.10
Mutagenesis2321D → A: Loss of one manganese ion and strongly reduced catalytic activity. Ref.8
Mutagenesis2321D → C: Reduced manganese binding and strongly reduced catalytic activity. Ref.8
Mutagenesis2341D → A, E or H: Reduced manganese binding and strongly reduced catalytic activity. Ref.8
Mutagenesis2351G → A: 56% of wild-type activity. Ref.4
Mutagenesis2351G → R: Loss of manganese-binding and activity. Ref.4
Sequence conflict2981A → P in AAA40761. Ref.1
Sequence conflict2981A → P in AAA40760. Ref.1

Secondary structure

............................................................... 323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07824 [UniParc].

Last modified April 1, 1990. Version 2.
Checksum: 5A92CB0931F9A053

FASTA32334,973
        10         20         30         40         50         60 
MSSKPKPIEI IGAPFSKGQP RGGVEKGPAA LRKAGLVEKL KETEYNVRDH GDLAFVDVPN 

        70         80         90        100        110        120 
DSPFQIVKNP RSVGKANEQL AAVVAETQKN GTISVVLGGD HSMAIGSISG HARVHPDLCV 

       130        140        150        160        170        180 
IWVDAHTDIN TPLTTSSGNL HGQPVAFLLK ELKGKFPDVP GFSWVTPCIS AKDIVYIGLR 

       190        200        210        220        230        240 
DVDPGEHYII KTLGIKYFSM TEVDKLGIGK VMEETFSYLL GRKKRPIHLS FDVDGLDPVF 

       250        260        270        280        290        300 
TPATGTPVVG GLSYREGLYI TEEIYKTGLL SGLDIMEVNP TLGKTPEEVT RTVNTAVALT 

       310        320 
LSCFGTKREG NHKPETDYLK PPK 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver arginase."
Kawamoto S., Amaya Y., Murakami K., Tokunaga F., Iwanaga S., Kobayashi K., Saheki T., Kimura S., Mori M.
J. Biol. Chem. 262:6280-6283(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Structural organization of the gene for rat liver-type arginase."
Ohtake A., Takiguchi M., Shigeto Y., Amaya Y., Kawamoto S., Mori M.
J. Biol. Chem. 263:2245-2249(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[4]"Functional consequences of the G235R mutation in liver arginase leading to hyperargininemia."
Lavulo L.T., Emig F.A., Ash D.E.
Arch. Biochem. Biophys. 399:49-55(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-235.
[5]"Structure of a unique binuclear manganese cluster in arginase."
Kanyo Z.F., Scolnick L.R., Ash D.E., Christianson D.W.
Nature 383:554-557(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[6]"Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function."
Scolnick L.R., Kanyo Z.F., Cavalli R.C., Ash D.E., Christianson D.W.
Biochemistry 36:10558-10565(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[7]"Arginase-boronic acid complex highlights a physiological role in erectile function."
Cox J.D., Kim N.N., Traish A.M., Christianson D.W.
Nat. Struct. Biol. 6:1043-1047(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[8]"Structural and functional importance of first-shell metal ligands in the binuclear manganese cluster of arginase I."
Cama E., Emig F.A., Ash D.E., Christianson D.W.
Biochemistry 42:7748-7758(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 6-319 OF MUTANTS ASN-101; GLU-101; ASN-128; GLU-128; ALA-232; CYS-232 AND GLU-234 IN COMPLEXES WITH MANGANESE IONS, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-101; ASP-128; ASP-232 AND ASP-234.
[9]"Design of amino acid aldehydes as transition-state analogue inhibitors of arginase."
Shin H., Cama E., Christianson D.W.
J. Am. Chem. Soc. 126:10278-10284(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 6-319 IN COMPLEX WITH MANGANESE IONS AND THE SYNTHETIC INHIBITOR (S)-2-AMINO-7-OXOHEPTANOIC ACID.
[10]"Probing the role of the hyper-reactive histidine residue of arginase."
Colleluori D.M., Reczkowski R.S., Emig F.A., Cama E., Cox J.D., Scolnick L.R., Compher K., Jude K., Han S., Viola R.E., Christianson D.W., Ash D.E.
Arch. Biochem. Biophys. 444:15-26(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 6-319 OF MUTANTS ALA-141; ASN-141; ASP-141 AND CYS-141 IN COMPLEX WITH MANGANESE IONS, COFACTOR, MUTAGENESIS OF HIS-141, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02720 mRNA. Translation: AAA40761.1.
M17931 expand/collapse EMBL AC list , M17924, M17925, M17926, M17927, M17928, M17929, M17930 Genomic DNA. Translation: AAA40760.1.
BC091158 mRNA. Translation: AAH91158.1.
PIRA26702.
RefSeqNP_058830.2. NM_017134.3.
UniGeneRn.9857.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D3VX-ray1.70A/B1-323[»]
1HQ5X-ray2.30A/B1-323[»]
1HQFX-ray2.90A/B/C1-323[»]
1HQGX-ray2.00A/B/C1-323[»]
1HQHX-ray2.80A/B/C1-323[»]
1HQXX-ray3.00A/B/C1-323[»]
1P8MX-ray2.84A/B/C6-319[»]
1P8NX-ray2.90A/B/C6-319[»]
1P8OX-ray2.96A/B/C6-319[»]
1P8PX-ray2.50A/B/C6-319[»]
1P8QX-ray2.95A/B/C6-319[»]
1P8RX-ray2.50A/B6-313[»]
1P8SX-ray3.20A/B/C6-319[»]
1R1OX-ray2.80A/B/C1-323[»]
1RLAX-ray2.10A/B/C1-323[»]
1T4PX-ray2.60A/B/C6-319[»]
1T4RX-ray2.60A/B/C6-319[»]
1T4SX-ray2.80A/B/C6-319[»]
1T4TX-ray2.20A/B/C6-319[»]
1T5FX-ray2.20A/B/C6-319[»]
1T5GX-ray2.40A/B/C6-319[»]
1TA1X-ray2.50A/B/C6-319[»]
1TBHX-ray2.70A/B/C6-319[»]
1TBJX-ray2.80A/B/C6-319[»]
1TBLX-ray3.10A/B/C6-319[»]
1ZPEX-ray1.70A/B/C6-319[»]
1ZPGX-ray1.90A/B/C6-319[»]
2RLAX-ray3.00A/B/C1-323[»]
3E8QX-ray2.90A/B/C1-323[»]
3E8ZX-ray2.00A/B/C1-323[»]
3E9BX-ray2.15A/B/C1-323[»]
3RLAX-ray2.54A/B/C1-323[»]
4RLAX-ray2.94A/B/C1-323[»]
5RLAX-ray2.74A/B/C1-323[»]
ProteinModelPortalP07824.
SMRP07824. Positions 6-319.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247899. 1 interaction.
IntActP07824. 1 interaction.
MINTMINT-4567374.
STRING10116.ENSRNOP00000017911.

PTM databases

PhosphoSiteP07824.

Proteomic databases

PaxDbP07824.
PRIDEP07824.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000017911; ENSRNOP00000017911; ENSRNOG00000013304.
GeneID29221.
KEGGrno:29221.

Organism-specific databases

CTD383.
RGD2150. Arg1.

Phylogenomic databases

eggNOGCOG0010.
GeneTreeENSGT00530000063082.
HOGENOMHOG000204319.
HOVERGENHBG003030.
InParanoidP07824.
KOK01476.
OMAFLIRIEV.
OrthoDBEOG747PJ5.
PhylomeDBP07824.
TreeFamTF300034.

Enzyme and pathway databases

SABIO-RKP07824.
UniPathwayUPA00158; UER00270.

Gene expression databases

GenevestigatorP07824.

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

EvolutionaryTraceP07824.
NextBio608419.
PROP07824.

Entry information

Entry nameARGI1_RAT
AccessionPrimary (citable) accession number: P07824
Secondary accession number(s): Q5BK93
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 1, 1990
Last modified: May 14, 2014
This is version 146 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways