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UniProtKB/Swiss-Prot entry P05089


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

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Entry information
Entry name ARGI1_HUMAN
Primary accession number P05089
Secondary accession numbers A6NEA0 Q5JWT5 Q5JWT6 Q8TE72 Q9BS50
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on January 11, 2001 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 112)
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
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=3540966 [NCBI, ExPASy, EBI, Israel, Japan]
Haraguchi Y., Takiguchi M., Amaya Y., Kawamoto S., Matsuda I., Mori M.;
"Molecular cloning and nucleotide sequence of cDNA for human liver arginase.";
Proc. Natl. Acad. Sci. U.S.A. 84:412-415(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
DOI=10.1093/nar/16.18.8789; PubMed=3174433 [NCBI, ExPASy, EBI, Israel, Japan]
Takiguchi M., Haraguchi Y., Mori M.;
"Human liver-type arginase gene: structure of the gene and analysis of the promoter region.";
Nucleic Acids Res. 16:8789-8802(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Erythroblast;
Lee Y.T., Miller J.L.;
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Liver, and Skeletal muscle;
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).
[7]
NUCLEOTIDE SEQUENCE OF 1-13, AND CHARACTERIZATION.
TISSUE=Liver;
PubMed=2241902 [NCBI, ExPASy, EBI, Israel, Japan]
Ikemoto M., Tabata M., Miyake T., Kono T., Mori M., Totani M., Murachi T.;
"Expression of human liver arginase in Escherichia coli. Purification and properties of the product.";
Biochem. J. 270:697-703(1990).
[8]
VARIANT ARGININEMIA ARG-235.
PubMed=1463019 [NCBI, ExPASy, EBI, Israel, Japan]
Uchino T., Haraguchi Y., Aparicio J.M., Mizutani N., Higashikawa M., Naitoh H., Mori M., Matsuda I.;
"Three novel mutations in the liver-type arginase gene in three unrelated Japanese patients with argininemia.";
Am. J. Hum. Genet. 51:1406-1412(1992).
[9]
VARIANT SER-290.
PubMed=1598908 [NCBI, ExPASy, EBI, Israel, Japan]
Grody W.W., Klein D., Dodson A.E., Kern R.M., Wissmann P.B., Goodman B.K., Bassand P., Marescau B., Kang S.-S., Leonard J.V., Cederbaum S.D.;
"Molecular genetic study of human arginase deficiency.";
Am. J. Hum. Genet. 50:1281-1290(1992).
[10]
VARIANTS ARGININEMIA THR-11 AND VAL-138.
DOI=10.1007/BF00210403; PubMed=7649538 [NCBI, ExPASy, EBI, Israel, Japan]
Uchino T., Snyderman S.E., Lambert M., Qureshi I.A., Shapira S.K., Sansaricq C., Smit L.M.E., Jakobs C., Matsuda I.;
"Molecular basis of phenotypic variation in patients with argininemia.";
Hum. Genet. 96:255-260(1995).
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
M14502; AAA51776.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X12662; CAA31188.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X12663; CAA31188.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X12664; CAA31188.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X12665; CAA31188.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X12666; CAA31188.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X12667; CAA31188.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X12668; CAA31188.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X12669; CAA31188.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY074488; AAL71547.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006741; AAP35387.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121575; CAB92071.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121575; CAI23317.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121575; CAI23318.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005321; AAH05321.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020653; AAH20653.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S02132; A26370.
RefSeq NP_000036.2; -.
UniGene Hs.440934
3D structure databases
PDB
1WVA; X-ray; 1.94 A; A/B=1-322.[ExPASy / RCSB / EBI]
1WVB; X-ray; 2.30 A; A/B=1-322.[ExPASy / RCSB / EBI]
2AEB; X-ray; 1.29 A; A/B=1-322.[ExPASy / RCSB / EBI]
2PHA; X-ray; 1.90 A; A/B=1-322.[ExPASy / RCSB / EBI]
2PHO; X-ray; 1.95 A; A/B=1-322.[ExPASy / RCSB / EBI]
2PLL; X-ray; 1.90 A; A/B=1-322.[ExPASy / RCSB / EBI]
2ZAV; X-ray; 1.70 A; A/B=1-322.[ExPASy / RCSB / EBI]
3DJ8; X-ray; 1.51 A; A/B=1-322.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1WVA; -.
1WVB; -.
2AEB; -.
2PHA; -.
2PHO; -.
2PLL; -.
2ZAV; -.
3DJ8; -.
ModBase P05089.
PTM databases
PhosphoSite P05089; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-11284; -.
Reactome REACT_13; Metabolism of amino acids.
Organism-specific databases
H-InvDB HIX0006220; -.
HGNC HGNC:663; ARG1.
GenAtlas ARG1.
HPA CAB009434; -.
HPA003595; -.
MIM 207800; phenotype. [NCBI / EBI]
608313; gene. [NCBI / EBI]
Orphanet 90; Argininemia.
PharmGKB PA24947; -.
GeneCards P05089.
Gene expression databases
ArrayExpress P05089; -.
CleanEx HS_ARG1; -.
GermOnline ENSG00000118520; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from ProtInc).
GO:0004053; Molecular function: arginase activity (traceable author statement from ProtInc).
GO:0006527; Biological process: arginine catabolic process (traceable author statement from ProtInc).
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 P05089.
ProtoNet P05089.
Genome annotation databases
Ensembl ENSG00000118520; Homo sapiens. [Contig view]
GeneID 383; -.
KEGG hsa:383; -.
Phylogenomic databases
HOVERGEN P05089; -.
Other
DrugBank DB00129; L-Ornithine.
NextBio 1603; -.
SOURCE ARG1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Arginine metabolism; Cytoplasm; Disease mutation; Hydrolase; Manganese; Metal-binding; Phosphoprotein; Polymorphism; Urea cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   322  322     Arginase-1. PRO_0000173693
METAL   101   101        Manganese 1 (By similarity). 
METAL   124   124        Manganese 1 (By similarity). 
METAL   124   124        Manganese 2 (By similarity). 
METAL   126   126        Manganese 2 (By similarity). 
METAL   128   128        Manganese 1 (By similarity). 
METAL   232   232        Manganese 1 (By similarity). 
METAL   232   232        Manganese 2 (By similarity). 
METAL   234   234        Manganese 2 (By similarity). 
MOD_RES   230   230        Phosphoserine (By similarity). 
VAR_SEQ   43    43        Q -> QVTQNFLIL (in isoform 2). VSP_009330
VAR_SEQ   204   289        Missing (in isoform 3). VSP_009331
VARIANT   11    11  1     I -> T (in argininemia; 12% of wild-type activity). VAR_015594 [3D]
VARIANT   138   138  1     G -> V (in argininemia). VAR_015595 [3D]
VARIANT   235   235  1     G -> R (in argininemia). VAR_000674 [3D]
VARIANT   290   290  1     T -> S (could be a polymorphism). VAR_000675 [3D]
CONFLICT   48    48        K -> E (in Ref. 3; AAL71547). 
CONFLICT   86    86        E -> Q (in Ref. 1; AAA51776). 
CONFLICT   202   202        E -> K (in Ref. 3; AAL71547). 
STRAND   7    13  7      
HELIX   22    26  5      
HELIX   27    33  7      
HELIX   36    42  7      
STRAND   46    52  7      
HELIX   70    89  20      
STRAND   93    99  7      
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      
TURN   153   155  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   221   223  3      
STRAND   227   232  6      
HELIX   233   235  3      
TURN   238   240  3      
STRAND   243   246  4      
HELIX   254   267  14      
STRAND   270   276  7      
HELIX   280   282  3      
HELIX   286   303  18      
Sequence information
Length: 322 AA [This is the length of the unprocessed precursor] Molecular weight: 34735 Da [This is the MW of the unprocessed precursor] CRC64: 8F3BE2652243F622 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSAKSRTIGI IGAPFSKGQP RGGVEEGPTV LRKAGLLEKL KEQECDVKDY GDLPFADIPN 

        70         80         90        100        110        120 
DSPFQIVKNP RSVGKASEQL AGKVAEVKKN GRISLVLGGD HSLAIGSISG HARVHPDLGV 

       130        140        150        160        170        180 
IWVDAHTDIN TPLTTTSGNL HGQPVSFLLK ELKGKIPDVP GFSWVTPCIS AKDIVYIGLR 

       190        200        210        220        230        240 
DVDPGEHYIL KTLGIKYFSM TEVDRLGIGK VMEETLSYLL GRKKRPIHLS FDVDGLDPSF 

       250        260        270        280        290        300 
TPATGTPVVG GLTYREGLYI TEEIYKTGLL SGLDIMEVNP SLGKTPEEVT RTVNTAVAIT 

       310        320 
LACFGLAREG NHKPIDYLNP PK 

P05089 in FASTA format

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