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UniProtKB/Swiss-Prot entry P07824


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ARGI1_RAT
Primary accession number P07824
Secondary accession number Q5BK93
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on April 1, 1990 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 98)
Name and origin of the protein
Protein name Arginase-1
Synonyms EC 3.5.3.1
Type I arginase
Liver-type arginase
Gene name
Name: Arg1
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=3571256 [NCBI, ExPASy, EBI, Israel, Japan]
Kawamoto S., Amaya Y., Murakami K., Tokunaga F., Iwanaga S., Kobayashi K., Saheki T., Kimura S., Mori M.;
"Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver arginase.";
J. Biol. Chem. 262:6280-6283(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=2892837 [NCBI, ExPASy, EBI, Israel, Japan]
Ohtake A., Takiguchi M., Shigeto Y., Amaya Y., Kawamoto S., Mori M.;
"Structural organization of the gene for rat liver-type arginase.";
J. Biol. Chem. 263:2245-2249(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
MUTAGENESIS OF GLY-235.
DOI=10.1006/abbi.2001.2720; PubMed=11883902 [NCBI, ExPASy, EBI, Israel, Japan]
Lavulo L.T., Emig F.A., Ash D.E.;
"Functional consequences of the G235R mutation in liver arginase leading to hyperargininemia.";
Arch. Biochem. Biophys. 399:49-55(2002).
[5]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1038/383554a0; PubMed=8849731 [NCBI, ExPASy, EBI, Israel, Japan]
Kanyo Z.F., Scolnick L.R., Ash D.E., Christianson D.W.;
"Structure of a unique binuclear manganese cluster in arginase.";
Nature 383:554-557(1996).
[6]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
DOI=10.1021/bi970800v; PubMed=9265637 [NCBI, ExPASy, EBI, Israel, Japan]
Scolnick L.R., Kanyo Z.F., Cavalli R.C., Ash D.E., Christianson D.W.;
"Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function.";
Biochemistry 36:10558-10565(1997).
[7]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
DOI=10.1038/14929; PubMed=10542097 [NCBI, ExPASy, EBI, Israel, Japan]
Cox J.D., Kim N.N., Traish A.M., Christianson D.W.;
"Arginase-boronic acid complex highlights a physiological role in erectile function.";
Nat. Struct. Biol. 6:1043-1047(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J02720; AAA40761.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17931; AAA40760.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17924; AAA40760.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17925; AAA40760.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17926; AAA40760.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17927; AAA40760.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17928; AAA40760.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17929; AAA40760.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17930; AAA40760.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC091158; AAH91158.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A26702; A26702.
RefSeq NP_058830.2; -.
UniGene Rn.9857
3D structure databases
PDB
1D3V; X-ray; 1.70 A; A/B=1-323.[ExPASy / RCSB / EBI]
1HQ5; X-ray; 2.30 A; A/B=1-323.[ExPASy / RCSB / EBI]
1HQF; X-ray; 2.90 A; A/B/C=1-323.[ExPASy / RCSB / EBI]
1HQG; X-ray; 2.00 A; A/B/C=1-323.[ExPASy / RCSB / EBI]
1HQH; X-ray; 2.80 A; A/B/C=1-323.[ExPASy / RCSB / EBI]
1HQX; X-ray; 3.00 A; A/B/C=1-323.[ExPASy / RCSB / EBI]
1P8M; X-ray; 2.84 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1P8N; X-ray; 2.90 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1P8O; X-ray; 2.96 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1P8P; X-ray; 2.50 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1P8Q; X-ray; 2.95 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1P8R; X-ray; 2.50 A; A/B=6-313.[ExPASy / RCSB / EBI]
1P8S; X-ray; 3.20 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1R1O; X-ray; 2.80 A; A/B/C=1-323.[ExPASy / RCSB / EBI]
1RLA; X-ray; 2.10 A; A/B/C=1-323.[ExPASy / RCSB / EBI]
1T4P; X-ray; 2.60 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1T4R; X-ray; 2.60 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1T4S; X-ray; 2.80 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1T4T; X-ray; 2.20 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1T5F; X-ray; 2.20 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1T5G; X-ray; 2.40 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1TA1; X-ray; 2.50 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1TBH; X-ray; 2.70 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1TBJ; X-ray; 2.80 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1TBL; X-ray; 3.10 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1ZPE; X-ray; 1.70 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
1ZPG; X-ray; 1.90 A; A/B/C=6-319.[ExPASy / RCSB / EBI]
2RLA; X-ray; 3.00 A; A/B/C=1-323.[ExPASy / RCSB / EBI]
3RLA; X-ray; 2.54 A; A/B/C=1-323.[ExPASy / RCSB / EBI]
4RLA; X-ray; 2.94 A; A/B/C=1-323.[ExPASy / RCSB / EBI]
5RLA; X-ray; 2.74 A; A/B/C=1-323.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1D3V; -.
1HQ5; -.
1HQF; -.
1HQG; -.
1HQH; -.
1HQX; -.
1P8M; -.
1P8N; -.
1P8O; -.
1P8P; -.
1P8Q; -.
1P8R; -.
1P8S; -.
1R1O; -.
1RLA; -.
1T4P; -.
1T4R; -.
1T4S; -.
1T4T; -.
1T5F; -.
1T5G; -.
1TA1; -.
1TBH; -.
1TBJ; -.
1TBL; -.
1ZPE; -.
1ZPG; -.
2RLA; -.
3RLA; -.
4RLA; -.
5RLA; -.
ModBase P07824.
Organism-specific databases
RGD 2150; Arg1.
Gene expression databases
ArrayExpress P07824; -.
GermOnline ENSRNOG00000013304; Rattus norvegicus.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006525; Biological process: arginine metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0000050; Biological process: urea cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR005924; Arginase.
IPR014033; Arginase_sub.
IPR006035; Ureohydrolase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.800.10; Ureohydrolase; 1.
PANTHER PTHR11358:SF2; Arginase_sub; 1.
PTHR11358; Ureohydrolase; 1.
Pfam PF00491; Arginase; 1.
Pfam graphical view of domain structure.
PRINTS PR00116; ARGINASE.
TIGRFAMs TIGR01229; rocF_arginase; 1.
PROSITE PS00147; ARGINASE_1; 1.
PS00148; ARGINASE_2; 1.
PS01053; ARGINASE_3; 1.
BLOCKS P07824.
ProtoNet P07824.
Genome annotation databases
Ensembl ENSRNOG00000013304; Rattus norvegicus. [Contig view]
GeneID 29221; -.
KEGG rno:29221; -.
NMPDR fig|10116.3.peg.244; -.
Phylogenomic databases
HOVERGEN P07824; -.
Other
LinkHub P07824; -.
NextBio 608419; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Arginine metabolism; Cytoplasm; Hydrolase; Manganese; Metal-binding; Phosphoprotein; Urea cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   323  323     Arginase-1. PRO_0000173697
METAL   101   101        Manganese 1. 
METAL   124   124        Manganese 1. 
METAL   124   124        Manganese 2. 
METAL   126   126        Manganese 2. 
METAL   128   128        Manganese 1. 
METAL   232   232        Manganese 1. 
METAL   232   232        Manganese 2. 
METAL   234   234        Manganese 2. 
MOD_RES   3     3        Phosphoserine (By similarity). 
MOD_RES   230   230        Phosphoserine (By similarity). 
MUTAGEN   235   235        G->A: 56% of wild-type activity. 
MUTAGEN   235   235        G->R: Loss of manganese-binding and activity. 
CONFLICT   298   298        A -> P (in Ref. 1; AAA40761/AAA40760). 
STRAND   8    12  5      
HELIX   22    26  5      
HELIX   27    33  7      
HELIX   36    40  5      
STRAND   43    45  3      
STRAND   47    52  6      
HELIX   70    89  20      
STRAND   93    97  5      
HELIX   101   103  3      
HELIX   104   114  11      
STRAND   119   126  8      
TURN   132   134  3      
HELIX   140   142  3      
HELIX   144   148  5      
HELIX   150   152  3      
HELIX   171   173  3      
STRAND   174   179  6      
HELIX   184   193  10      
STRAND   196   199  4      
HELIX   200   206  7      
HELIX   208   220  13      
STRAND   227   232  6      
HELIX   233   235  3      
TURN   238   240  3      
STRAND   244   246  3      
HELIX   254   267  14      
STRAND   270   276  7      
HELIX   286   303  18      
Sequence information
Length: 323 AA [This is the length of the unprocessed precursor] Molecular weight: 34973 Da [This is the MW of the unprocessed precursor] CRC64: 5A92CB0931F9A053 [This is a checksum on the sequence]
        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 

P07824 in FASTA format

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