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Protein

Arginase

Gene

CAR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mn2+PROSITE-ProRule annotationNote: Binds 2 manganese ions per subunit.PROSITE-ProRule annotation

Pathwayi: urea cycle

This protein is involved in step 1 of the subpathway that synthesizes L-ornithine and urea from L-arginine.By similarity
Proteins known to be involved in this subpathway in this organism are:
  1. Arginase (CAR1)
This subpathway is part of the pathway urea cycle, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-ornithine and urea from L-arginine, the pathway urea cycle and in Nitrogen metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi123 – 1231Manganese 1PROSITE-ProRule annotation
Metal bindingi146 – 1461Manganese 1PROSITE-ProRule annotation
Metal bindingi146 – 1461Manganese 2PROSITE-ProRule annotation
Metal bindingi148 – 1481Manganese 2PROSITE-ProRule annotation
Metal bindingi150 – 1501Manganese 1PROSITE-ProRule annotation
Binding sitei205 – 2051SubstrateBy similarity
Metal bindingi256 – 2561Manganese 1PROSITE-ProRule annotation
Metal bindingi256 – 2561Manganese 2PROSITE-ProRule annotation
Metal bindingi258 – 2581Manganese 2PROSITE-ProRule annotation
Binding sitei270 – 2701SubstrateBy similarity
Binding sitei301 – 3011SubstrateBy similarity

GO - Molecular functioni

  • arginase activity Source: SGD
  • manganese ion binding Source: SGD
  • ornithine carbamoyltransferase inhibitor activity Source: SGD
  • zinc ion binding Source: SGD

GO - Biological processi

  • arginine catabolic process to ornithine Source: SGD
  • regulation of ornithine metabolic process Source: SGD
  • urea cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Arginine metabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11546.
YEAST:YPL111W-MONOMER.
ReactomeiR-SCE-351143. Agmatine biosynthesis.
R-SCE-70635. Urea cycle.
SABIO-RKP00812.
UniPathwayiUPA00158; UER00270.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginase (EC:3.5.3.1By similarity)
Gene namesi
Name:CAR1
Ordered Locus Names:YPL111W
ORF Names:LPH15W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL111W.
SGDiS000006032. CAR1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333ArginasePRO_0000173711Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei16 – 161PhosphoserineCombined sources
Modified residuei77 – 771PhosphothreonineCombined sources
Modified residuei270 – 2701PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP00812.
PeptideAtlasiP00812.

2D gel databases

UCD-2DPAGEP00812.

PTM databases

iPTMnetiP00812.

Expressioni

Inductioni

By arginine or homoarginine.

Interactioni

Subunit structurei

Homotrimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
ARG3P051504EBI-2856,EBI-12712

Protein-protein interaction databases

BioGridi36070. 17 interactions.
DIPiDIP-1224N.
IntActiP00812. 14 interactions.
MINTiMINT-409717.

Structurei

3D structure databases

ProteinModelPortaliP00812.
SMRiP00812. Positions 13-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni148 – 1525Substrate bindingBy similarity
Regioni159 – 1613Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the arginase family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204319.
InParanoidiP00812.
KOiK01476.
OMAiIDPLYVP.
OrthoDBiEOG7X0VT2.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00812-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METGPHYNYY KNRELSIVLA PFSGGQGKLG VEKGPKYMLK HGLQTSIEDL
60 70 80 90 100
GWSTELEPSM DEAQFVGKLK MEKDSTTGGS SVMIDGVKAK RADLVGEATK
110 120 130 140 150
LVYNSVSKVV QANRFPLTLG GDHSIAIGTV SAVLDKYPDA GLLWIDAHAD
160 170 180 190 200
INTIESTPSG NLHGCPVSFL MGLNKDVPHC PESLKWVPGN LSPKKIAYIG
210 220 230 240 250
LRDVDAGEKK ILKDLGIAAF SMYHVDKYGI NAVIEMAMKA VHPETNGEGP
260 270 280 290 300
IMCSYDVDGV DPLYIPATGT PVRGGLTLRE GLFLVERLAE SGNLIALDVV
310 320 330
ECNPDLAIHD IHVSNTISAG CAIARCALGE TLL
Length:333
Mass (Da):35,662
Last modified:July 21, 1986 - v1
Checksum:iA5979DC9F1FDFF2E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10414 Genomic DNA. Translation: AAA34470.1.
U43503 Genomic DNA. Translation: AAB68250.1.
M10110 Genomic DNA. Translation: AAA34469.1.
BK006949 Genomic DNA. Translation: DAA11322.1.
PIRiA01008. WZBYR.
RefSeqiNP_015214.1. NM_001183925.1.

Genome annotation databases

EnsemblFungiiYPL111W; YPL111W; YPL111W.
GeneIDi855993.
KEGGisce:YPL111W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10414 Genomic DNA. Translation: AAA34470.1.
U43503 Genomic DNA. Translation: AAB68250.1.
M10110 Genomic DNA. Translation: AAA34469.1.
BK006949 Genomic DNA. Translation: DAA11322.1.
PIRiA01008. WZBYR.
RefSeqiNP_015214.1. NM_001183925.1.

3D structure databases

ProteinModelPortaliP00812.
SMRiP00812. Positions 13-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36070. 17 interactions.
DIPiDIP-1224N.
IntActiP00812. 14 interactions.
MINTiMINT-409717.

PTM databases

iPTMnetiP00812.

2D gel databases

UCD-2DPAGEP00812.

Proteomic databases

MaxQBiP00812.
PeptideAtlasiP00812.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL111W; YPL111W; YPL111W.
GeneIDi855993.
KEGGisce:YPL111W.

Organism-specific databases

EuPathDBiFungiDB:YPL111W.
SGDiS000006032. CAR1.

Phylogenomic databases

GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204319.
InParanoidiP00812.
KOiK01476.
OMAiIDPLYVP.
OrthoDBiEOG7X0VT2.

Enzyme and pathway databases

UniPathwayiUPA00158; UER00270.
BioCyciMetaCyc:MONOMER-11546.
YEAST:YPL111W-MONOMER.
ReactomeiR-SCE-351143. Agmatine biosynthesis.
R-SCE-70635. Urea cycle.
SABIO-RKP00812.

Miscellaneous databases

PROiP00812.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
  5. "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] [Europe PMC] [Abstract]
    Cited for: METAL-BINDING.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND THR-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiARGI_YEAST
AccessioniPrimary (citable) accession number: P00812
Secondary accession number(s): D6W3Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 8, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 42800 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.