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UniProtKB/Swiss-Prot entry P00812


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

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Entry information
Entry name ARGI_YEAST
Primary accession number P00812
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 83)
Name and origin of the protein
Protein name Arginase
Synonym EC 3.5.3.1
Gene name
Name: CAR1
OrderedLocusNames: YPL111W
ORFNames: LPH15W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6094498 [NCBI, ExPASy, EBI, Israel, Japan]
Sumrada R.A., Cooper T.G.;
"Nucleotide sequence of the Saccharomyces cerevisiae arginase gene (CAR1) and its transcription under various physiological conditions.";
J. Bacteriol. 160:1078-1087(1984).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169875 [NCBI, ExPASy, EBI, Israel, Japan]
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
PubMed=2983306 [NCBI, ExPASy, EBI, Israel, Japan]
Sumrada R.A., Cooper T.G.;
"Point mutation generates constitutive expression of an inducible eukaryotic gene.";
Proc. Natl. Acad. Sci. U.S.A. 82:643-647(1985).
[4]
METAL-BINDING.
PubMed=1939179 [NCBI, ExPASy, EBI, Israel, Japan]
Green S.M., Ginsburg A., Lewis M.S., Hensley P.;
"Roles of metal ions in the maintenance of the tertiary and quaternary structure of arginase from Saccharomyces cerevisiae.";
J. Biol. Chem. 266:21474-21481(1991).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-76; THR-77; SER-80 AND THR-270, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
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
M10414; AAA34470.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U43503; AAB68250.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M10110; AAA34469.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A01008; WZBYR.
RefSeq NP_015214.1; -.
3D structure databases
HSSP P78540; 1PQ3. [HSSP ENTRY / PDB]
ModBase P00812.
Protein-protein interaction databases
DIP DIP:1224N; -.
IntAct P00812; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-11546; -.
Organism-specific databases
CYGD YPL111w; -.
SGD S000006032; CAR1.
Yeast-GFP YPL111W.
Gene expression databases
ArrayExpress P00812; -.
GermOnline YPL111W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0004053; Molecular function: arginase activity (traceable author statement from SGD).
GO:0030145; Molecular function: manganese ion binding (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008270; Molecular function: zinc ion binding (inferred from direct assay from SGD).
GO:0019547; Biological process: arginine catabolic process to ornithine (traceable author statement from SGD).
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 P00812.
ProtoNet P00812.
Proteomic databases
PeptideAtlas P00812; -.
Genome annotation databases
Ensembl YPL111W; Saccharomyces cerevisiae. [Contig view]
GeneID 855993; -.
GenomeReviews U00094_GR; YPL111W.
KEGG sce:YPL111W; -.
NMPDR fig|4932.3.peg.6346; -.
Phylogenomic databases
HOGENOM P00812; -.
Other
LinkHub P00812; -.
NextBio 980848; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Arginine metabolism; Complete proteome; Hydrolase; Manganese; Metal-binding; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   333  333     Arginase. PRO_0000173711
METAL   123   123        Manganese 1 (By similarity). 
METAL   146   146        Manganese 1 (By similarity). 
METAL   146   146        Manganese 2 (By similarity). 
METAL   148   148        Manganese 2 (By similarity). 
METAL   150   150        Manganese 1 (By similarity). 
METAL   256   256        Manganese 1 (By similarity). 
METAL   256   256        Manganese 2 (By similarity). 
METAL   258   258        Manganese 2 (By similarity). 
MOD_RES   76    76        Phosphothreonine. 
MOD_RES   77    77        Phosphothreonine. 
MOD_RES   80    80        Phosphoserine. 
MOD_RES   270   270        Phosphothreonine. 
Sequence information
Length: 333 AA [This is the length of the unprocessed precursor] Molecular weight: 35662 Da [This is the MW of the unprocessed precursor] CRC64: A5979DC9F1FDFF2E [This is a checksum on the sequence]
        10         20         30         40         50         60 
METGPHYNYY KNRELSIVLA PFSGGQGKLG VEKGPKYMLK HGLQTSIEDL GWSTELEPSM 

        70         80         90        100        110        120 
DEAQFVGKLK MEKDSTTGGS SVMIDGVKAK RADLVGEATK LVYNSVSKVV QANRFPLTLG 

       130        140        150        160        170        180 
GDHSIAIGTV SAVLDKYPDA GLLWIDAHAD INTIESTPSG NLHGCPVSFL MGLNKDVPHC 

       190        200        210        220        230        240 
PESLKWVPGN LSPKKIAYIG LRDVDAGEKK ILKDLGIAAF SMYHVDKYGI NAVIEMAMKA 

       250        260        270        280        290        300 
VHPETNGEGP IMCSYDVDGV DPLYIPATGT PVRGGLTLRE GLFLVERLAE SGNLIALDVV 

       310        320        330 
ECNPDLAIHD IHVSNTISAG CAIARCALGE TLL 

P00812 in FASTA format

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