ARGI_YEAST
ID ARGI_YEAST Reviewed; 333 AA.
AC P00812; D6W3Q6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Arginase;
DE EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089};
GN Name=CAR1; OrderedLocusNames=YPL111W; ORFNames=LPH15W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6094498; DOI=10.1128/jb.160.3.1078-1087.1984;
RA Sumrada R.A., Cooper T.G.;
RT "Nucleotide sequence of the Saccharomyces cerevisiae arginase gene (CAR1)
RT and its transcription under various physiological conditions.";
RL J. Bacteriol. 160:1078-1087(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RX PubMed=2983306; DOI=10.1073/pnas.82.3.643;
RA Sumrada R.A., Cooper T.G.;
RT "Point mutation generates constitutive expression of an inducible
RT eukaryotic gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:643-647(1985).
RN [5]
RP METAL-BINDING.
RX PubMed=1939179; DOI=10.1016/s0021-9258(18)54663-9;
RA Green S.M., Ginsburg A., Lewis M.S., Hensley P.;
RT "Roles of metal ions in the maintenance of the tertiary and quaternary
RT structure of arginase from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 266:21474-21481(1991).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-270, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND THR-77, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:46911; EC=3.5.3.1;
CC Evidence={ECO:0000250|UniProtKB:P05089};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00742};
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-
CC arginine: step 1/1. {ECO:0000250|UniProtKB:P05089}.
CC -!- SUBUNIT: Homotrimer.
CC -!- INTERACTION:
CC P00812; P05150: ARG3; NbExp=4; IntAct=EBI-2856, EBI-12712;
CC -!- INDUCTION: By arginine or homoarginine.
CC -!- MISCELLANEOUS: Present with 42800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; M10414; AAA34470.1; -; Genomic_DNA.
DR EMBL; U43503; AAB68250.1; -; Genomic_DNA.
DR EMBL; M10110; AAA34469.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11322.1; -; Genomic_DNA.
DR PIR; A01008; WZBYR.
DR RefSeq; NP_015214.1; NM_001183925.1.
DR AlphaFoldDB; P00812; -.
DR SMR; P00812; -.
DR BioGRID; 36070; 59.
DR ComplexPortal; CPX-1707; Ornithine carbamoyltransferase arginase complex.
DR DIP; DIP-1224N; -.
DR IntAct; P00812; 19.
DR MINT; P00812; -.
DR STRING; 4932.YPL111W; -.
DR MoonProt; P00812; -.
DR iPTMnet; P00812; -.
DR UCD-2DPAGE; P00812; -.
DR MaxQB; P00812; -.
DR PaxDb; P00812; -.
DR PRIDE; P00812; -.
DR EnsemblFungi; YPL111W_mRNA; YPL111W; YPL111W.
DR GeneID; 855993; -.
DR KEGG; sce:YPL111W; -.
DR SGD; S000006032; CAR1.
DR VEuPathDB; FungiDB:YPL111W; -.
DR eggNOG; KOG2965; Eukaryota.
DR GeneTree; ENSGT00950000183195; -.
DR HOGENOM; CLU_039478_6_1_1; -.
DR InParanoid; P00812; -.
DR OMA; IATCFGQ; -.
DR BioCyc; MetaCyc:YPL111W-MON; -.
DR BioCyc; YEAST:YPL111W-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-70635; Urea cycle.
DR SABIO-RK; P00812; -.
DR UniPathway; UPA00158; UER00270.
DR PRO; PR:P00812; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P00812; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:1903269; C:ornithine carbamoyltransferase inhibitor complex; IPI:ComplexPortal.
DR GO; GO:0004053; F:arginase activity; IDA:SGD.
DR GO; GO:0030145; F:manganese ion binding; IDA:SGD.
DR GO; GO:0090369; F:ornithine carbamoyltransferase inhibitor activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IDA:SGD.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IDA:SGD.
DR GO; GO:0090368; P:regulation of ornithine metabolic process; IDA:SGD.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd09989; Arginase; 1.
DR InterPro; IPR014033; Arginase.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR PANTHER; PTHR43782; PTHR43782; 1.
DR Pfam; PF00491; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01229; rocF_arginase; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Arginine metabolism; Hydrolase; Manganese; Metal-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..333
FT /note="Arginase"
FT /id="PRO_0000173711"
FT BINDING 123
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 146
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 146
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 148..152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 148
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 150
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 159..161
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 256
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 256
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 77
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 270
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 333 AA; 35662 MW; A5979DC9F1FDFF2E CRC64;
METGPHYNYY KNRELSIVLA PFSGGQGKLG VEKGPKYMLK HGLQTSIEDL GWSTELEPSM
DEAQFVGKLK MEKDSTTGGS SVMIDGVKAK RADLVGEATK LVYNSVSKVV QANRFPLTLG
GDHSIAIGTV SAVLDKYPDA GLLWIDAHAD INTIESTPSG NLHGCPVSFL MGLNKDVPHC
PESLKWVPGN LSPKKIAYIG LRDVDAGEKK ILKDLGIAAF SMYHVDKYGI NAVIEMAMKA
VHPETNGEGP IMCSYDVDGV DPLYIPATGT PVRGGLTLRE GLFLVERLAE SGNLIALDVV
ECNPDLAIHD IHVSNTISAG CAIARCALGE TLL
