Reviewed, UniProtKB/Swiss-Prot P00812 (ARGI_YEAST)

Names and origin

Protein names

Recommended name:
    Arginase
    EC=3.5.3.1

Gene names

Name:	CAR1
Ordered Locus Names:	YPL111W
ORF Names:	LPH15W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-arginine + H2O = L-ornithine + urea.
Cofactor	Binds 2 manganese ions per subunit By similarity.
Pathway	Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
Subunit structure	Homotrimer.
Induction	By arginine or homoarginine.
Miscellaneous	Present with 42800 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the arginase family.

Ontologies

Keywords
Biological process	Arginine metabolism
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine catabolic process to ornithine Traceable author statement. Source: SGD
Cellular component	mating projection tip Inferred from direct assay. Source: SGD
Molecular function	arginase activity Traceable author statement. Source: SGD manganese ion binding Ref.4 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Ref.4 Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SRP1	Q02821	1	EBI-2856,EBI-1797
TEM1	P38987	1	EBI-2856,EBI-19113

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 333	333	Arginase		PRO_0000173711
Regions
	Region	148 – 152	5	Substrate binding By similarity
	Region	159 – 161	3	Substrate binding By similarity
Sites
	Metal binding	123	1	Manganese 1 By similarity
	Metal binding	146	1	Manganese 1 By similarity
	Metal binding	146	1	Manganese 2 By similarity
	Metal binding	148	1	Manganese 2 By similarity
	Metal binding	150	1	Manganese 1 By similarity
	Metal binding	256	1	Manganese 1 By similarity
	Metal binding	256	1	Manganese 2 By similarity
	Metal binding	258	1	Manganese 2 By similarity
	Binding site	205	1	Substrate By similarity
	Binding site	301	1	Substrate By similarity
Amino acid modifications
	Modified residue	76	1	Phosphothreonine Ref.6
	Modified residue	77	1	Phosphothreonine Ref.6
	Modified residue	80	1	Phosphoserine Ref.6
	Modified residue	270	1	Phosphothreonine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P00812-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: A5979DC9F1FDFF2E	FASTA	333	35,662
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the Saccharomyces cerevisiae arginase gene (CAR1) and its transcription under various physiological conditions." Sumrada R.A., Cooper T.G. J. Bacteriol. 160:1078-1087(1984) [PubMed: 6094498] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." 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. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Point mutation generates constitutive expression of an inducible eukaryotic gene." Sumrada R.A., Cooper T.G. Proc. Natl. Acad. Sci. U.S.A. 82:643-647(1985) [PubMed: 2983306] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
[4]	"Roles of metal ions in the maintenance of the tertiary and quaternary structure of arginase from Saccharomyces cerevisiae." Green S.M., Ginsburg A., Lewis M.S., Hensley P. J. Biol. Chem. 266:21474-21481(1991) [PubMed: 1939179] [Abstract] Cited for: METAL-BINDING.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-76; THR-77; SER-80 AND THR-270, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M10414 Genomic DNA. Translation: AAA34470.1. U43503 Genomic DNA. Translation: AAB68250.1. M10110 Genomic DNA. Translation: AAA34469.1.
PIR	WZBYR. A01008.
RefSeq	NP_015214.1.
3D structure databases
HSSP	HSSP built from PDB template 1PQ3 based on UniProtKB P78540.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1224N.
IntAct	P00812. 22 interactions.
Proteomic databases
PeptideAtlas	P00812.
PRIDE	P00812.
Genome annotation databases
Ensembl	YPL111W. Saccharomyces cerevisiae. [Contig view]
GeneID	855993.
GenomeReviews	Gene locus YPL111W in contig U00094_GR.
KEGG	sce:YPL111W.
NMPDR	fig|4932.3.peg.6346.
Organism-specific databases
CYGD	YPL111w.
SGD	S000006032. CAR1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P00812.
OMA	P00812. INAVIEM.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-11546.
BRENDA	3.5.3.1. 250.
Gene expression databases
ArrayExpress	P00812.
GermOnline	YPL111W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR005924. Arginase. IPR014033. Arginase_sub. IPR006035. Ureohydrolase. [Graphical view]
Gene3D	G3DSA:3.40.800.10. Ureohydrolase. 1 hit.
PANTHER	PTHR11358:SF2. Arginase_sub. 1 hit. PTHR11358. Ureohydrolase. 1 hit.
Pfam	PF00491. Arginase. 1 hit. [Graphical view]
PRINTS	PR00116. ARGINASE.
TIGRFAMs	TIGR01229. rocF_arginase. 1 hit.
PROSITE	PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	980848.

Entry information

Entry name

ARGI_YEAST

Accession

Primary (citable) accession number: P00812

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)