ARGR2_YEAST
ID ARGR2_YEAST Reviewed; 880 AA.
AC P05085; D6W0I6;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Arginine metabolism regulation protein II;
DE AltName: Full=Arginine-requiring protein 81;
GN Name=ARG81; Synonyms=ARGR2; OrderedLocusNames=YML099C;
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=3709534; DOI=10.1111/j.1432-1033.1986.tb09640.x;
RA Messenguy F., Dubois E., Descamps F.;
RT "Nucleotide sequence of the ARGRII regulatory gene and amino acid sequence
RT homologies between ARGRII PPRI and GAL4 regulatory proteins.";
RL Eur. J. Biochem. 157:77-81(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 SUBCELLULAR LOCATION.
RX PubMed=3311884; DOI=10.1016/0378-1119(87)90287-3;
RA Bercy J., Dubois E., Messenguy F.;
RT "Regulation of arginine metabolism in Saccharomyces cerevisiae: expression
RT of the three ARGR regulatory genes and cellular localization of their
RT products.";
RL Gene 55:277-285(1987).
RN [5]
RP FUNCTION.
RX PubMed=3298999; DOI=10.1007/bf00331501;
RA Dubois E., Bercy J., Messenguy F.;
RT "Characterization of two genes, ARGRI and ARGRIII required for specific
RT regulation of arginine metabolism in yeast.";
RL Mol. Gen. Genet. 207:142-148(1987).
RN [6]
RP FUNCTION.
RX PubMed=2274024; DOI=10.1007/bf00633817;
RA Qiu H.F., Dubois E., Broen P., Messenguy F.;
RT "Functional analysis of ARGRI and ARGRIII regulatory proteins involved in
RT the regulation of arginine metabolism in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 222:192-200(1990).
RN [7]
RP DNA-BINDING.
RX PubMed=2005902; DOI=10.1128/mcb.11.4.2162-2168.1991;
RA Dubois E., Messenguy F.;
RT "In vitro studies of the binding of the ARGR proteins to the ARG5,6
RT promoter.";
RL Mol. Cell. Biol. 11:2162-2168(1991).
RN [8]
RP DNA-BINDING.
RX PubMed=2005903; DOI=10.1128/mcb.11.4.2169-2179.1991;
RA Qui H.F., Dubois E., Messenguy F.;
RT "Dissection of the bifunctional ARGRII protein involved in the regulation
RT of arginine anabolic and catabolic pathways.";
RL Mol. Cell. Biol. 11:2169-2179(1991).
RN [9]
RP DNA-BINDING.
RX PubMed=2017180; DOI=10.1128/mcb.11.5.2852-2863.1991;
RA Messenguy F., Dubois E., Boonchird C.;
RT "Determination of the DNA-binding sequences of ARGR proteins to arginine
RT anabolic and catabolic promoters.";
RL Mol. Cell. Biol. 11:2852-2863(1991).
RN [10]
RP INTERACTION WITH ARG80 AND MCM1.
RX PubMed=10632874; DOI=10.1046/j.1365-2958.2000.01665.x;
RA El Bakkoury M., Dubois E., Messenguy F.;
RT "Recruitment of the yeast MADS-box proteins, ArgRI and Mcm1 by the
RT pleiotropic factor ArgRIII is required for their stability.";
RL Mol. Microbiol. 35:15-31(2000).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [12]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: With ARG80, ARG82 and MCM1, coordinates the expression of
CC arginine anabolic and catabolic genes in response to arginine.
CC {ECO:0000269|PubMed:2274024, ECO:0000269|PubMed:3298999}.
CC -!- SUBUNIT: Interacts with ARG80 and MCM1. {ECO:0000269|PubMed:10632874}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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DR EMBL; X03940; CAA27577.1; -; Genomic_DNA.
DR EMBL; Z46660; CAA86638.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09800.1; -; Genomic_DNA.
DR PIR; S49627; S49627.
DR RefSeq; NP_013610.1; NM_001182459.1.
DR AlphaFoldDB; P05085; -.
DR SMR; P05085; -.
DR BioGRID; 35044; 85.
DR ComplexPortal; CPX-1152; ARGR-MCM1 transcription regulation complex.
DR DIP; DIP-1346N; -.
DR IntAct; P05085; 14.
DR MINT; P05085; -.
DR STRING; 4932.YML099C; -.
DR iPTMnet; P05085; -.
DR MaxQB; P05085; -.
DR PaxDb; P05085; -.
DR PRIDE; P05085; -.
DR EnsemblFungi; YML099C_mRNA; YML099C; YML099C.
DR GeneID; 854874; -.
DR KEGG; sce:YML099C; -.
DR SGD; S000004565; ARG81.
DR VEuPathDB; FungiDB:YML099C; -.
DR eggNOG; ENOG502QQBG; Eukaryota.
DR HOGENOM; CLU_009030_1_0_1; -.
DR InParanoid; P05085; -.
DR OMA; AKTFTGC; -.
DR BioCyc; YEAST:G3O-32684-MON; -.
DR PRO; PR:P05085; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P05085; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IC:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0000821; P:regulation of arginine metabolic process; IMP:SGD.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR021858; Fun_TF.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF11951; Fungal_trans_2; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW Activator; Arginine metabolism; Cytoplasm; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..880
FT /note="Arginine metabolism regulation protein II"
FT /id="PRO_0000114937"
FT DNA_BIND 21..48
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT CONFLICT 4
FT /note="S -> F (in Ref. 1; CAA27577)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="Missing (in Ref. 1; CAA27577)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="F -> V (in Ref. 1; CAA27577)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="D -> V (in Ref. 1; CAA27577)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="E -> Q (in Ref. 1; CAA27577)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="T -> A (in Ref. 1; CAA27577)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="T -> S (in Ref. 1; CAA27577)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="K -> N (in Ref. 1; CAA27577)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="V -> I (in Ref. 1; CAA27577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 880 AA; 100282 MW; DA033AB2B373F415 CRC64;
MGISSKNGPK KMGRAKTFTG CWTCRGRKVK CDLRHPHCQR CEKSNLPCGG YDIKLRWSKP
MQFDPYGVPI PQNSPATTTN LSGSVDEPQY QRRNIDFVRY DEEYVYHEDM DDELTMLHTP
PIEKISDNKT WIIKKFGVFK GTDKIDKQYA PRKKRNRKRV AKSLESSASI SLSSLPSSST
ISFPIRHIED KLRNKGHVKT GILSANDGVP PTPNLLDYDW NNLNITGYEW ISSELRDDAL
LSAVTLQGHH LGHTQPQEIS LEENSNVVSG EEHVNAKEHG CAFEADNQGS STLPNKAASA
NDKLYQQNLK LLFQKNSSNS EEPDPQALID DVFVNIEPRS LPASDLNKIT LAPPNEESRM
PKSMLELTSY SSDLPPELVD IIPKTDLTVH GLARFLLNHY FNNVADKMTV VVLEKNPWKT
LYFPRALMAL GDLAGLGQSS NSRNALLNAL LAVSCFHLQS KYPRNYKLQK YFLGLGIELR
NQASNFLRLC LNTKSSIPEK YKDVLTAILS MNSIDVVWGT MADCQDHLAL CEDFVESRMK
LRPNISEKTK TLHRIFSFLK LIQDSTALDK VRAKEIVILP SEEDDNYKPL DTSNATTSSS
EPRVDVVQEG LFREALNEND GKIHIEFVKE PITNVSADST PSSTTPPIFT NIATESYYNK
SDISKLVSKT DENIIGTDSL YGLPNSLILL FSDCVRIVRH NEYYNLTYLP VPRKFNELSL
NFEKRLLKWK SEWNFHQENS EGKSFINSTA EALYHHTMSF YFSLIIYYFT MARSLNCQFL
QNYVAKVLDH LNAMEELVDQ KKVKIVPLIW QGFMAGCACT DENRQQEFRR WAAKLAESGV
GSYWGARQVM LEVWRRRKED EPGDNWYSVY KDWEMNLMLS
