ARGR1_YEAST
ID ARGR1_YEAST Reviewed; 177 AA.
AC P07249; D6VZL7;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Arginine metabolism regulation protein I;
DE AltName: Full=Arginine-requiring protein 80;
GN Name=ARG80; Synonyms=ARGR1; OrderedLocusNames=YMR042W; ORFNames=YM9532.07;
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], AND 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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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 [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=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 [9]
RP INTERACTION WITH ARG81 AND ARG82, FUNCTION, AND MUTAGENESIS OF ARG-94;
RP HIS-95; ALA-109; LEU-115 AND GLY-148.
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 [10]
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).
CC -!- FUNCTION: With ARG81, ARG82 and MCM1, coordinates the expression of
CC arginine anabolic and catabolic genes in response to arginine.
CC {ECO:0000269|PubMed:10632874, ECO:0000269|PubMed:2274024,
CC ECO:0000269|PubMed:3298999}.
CC -!- SUBUNIT: Interacts with ARG81 and ARG82. {ECO:0000269|PubMed:10632874}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:3311884}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X05327; CAA28944.1; -; Genomic_DNA.
DR EMBL; Z48502; CAA88408.1; -; Genomic_DNA.
DR EMBL; AY692845; AAT92864.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09941.1; -; Genomic_DNA.
DR PIR; S05822; RGBYGI.
DR RefSeq; NP_013756.1; NM_001182539.1.
DR AlphaFoldDB; P07249; -.
DR SMR; P07249; -.
DR BioGRID; 35215; 87.
DR ComplexPortal; CPX-1152; ARGR-MCM1 transcription regulation complex.
DR DIP; DIP-2404N; -.
DR IntAct; P07249; 1.
DR STRING; 4932.YMR042W; -.
DR iPTMnet; P07249; -.
DR MaxQB; P07249; -.
DR PaxDb; P07249; -.
DR PRIDE; P07249; -.
DR EnsemblFungi; YMR042W_mRNA; YMR042W; YMR042W.
DR GeneID; 855059; -.
DR KEGG; sce:YMR042W; -.
DR SGD; S000004645; ARG80.
DR VEuPathDB; FungiDB:YMR042W; -.
DR eggNOG; KOG0015; Eukaryota.
DR GeneTree; ENSGT00400000022158; -.
DR HOGENOM; CLU_130026_0_0_1; -.
DR InParanoid; P07249; -.
DR OMA; ANSGLVX; -.
DR BioCyc; YEAST:G3O-32747-MON; -.
DR PRO; PR:P07249; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P07249; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IC:ComplexPortal.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:SGD.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:1900079; P:regulation of arginine biosynthetic process; IMP:SGD.
DR GO; GO:1900081; P:regulation of arginine catabolic process; IMP:SGD.
DR GO; GO:0000821; P:regulation of arginine metabolic process; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00266; MADS_SRF_like; 1.
DR Gene3D; 3.40.1810.10; -; 1.
DR InterPro; IPR033897; MADS_SRF-like.
DR InterPro; IPR002100; TF_MADSbox.
DR InterPro; IPR036879; TF_MADSbox_sf.
DR Pfam; PF00319; SRF-TF; 1.
DR PRINTS; PR00404; MADSDOMAIN.
DR SMART; SM00432; MADS; 1.
DR SUPFAM; SSF55455; SSF55455; 1.
DR PROSITE; PS00350; MADS_BOX_1; 1.
DR PROSITE; PS50066; MADS_BOX_2; 1.
PE 1: Evidence at protein level;
KW Arginine metabolism; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..177
FT /note="Arginine metabolism regulation protein I"
FT /id="PRO_0000199438"
FT DOMAIN 80..134
FT /note="MADS-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 94
FT /note="R->G: Decreases the physical interaction with ARG82.
FT Abolishes the physical interaction with ARG82 and impairs
FT function; when associated with D-95 and R-103."
FT /evidence="ECO:0000269|PubMed:10632874"
FT MUTAGEN 95
FT /note="H->G: Decreases the physical interaction with ARG82.
FT Abolishes the physical interaction with ARG82 and impairs
FT function; when associated with G-94 and R-103."
FT /evidence="ECO:0000269|PubMed:10632874"
FT MUTAGEN 103
FT /note="H->R: Abolishes the physical interaction with ARG82
FT and impairs function; when associated with G-94 and D-95."
FT MUTAGEN 109
FT /note="A->T: Decreases the physical interaction with
FT ARG82."
FT /evidence="ECO:0000269|PubMed:10632874"
FT MUTAGEN 115
FT /note="L->H: Decreases the physical interaction with
FT ARG82."
FT /evidence="ECO:0000269|PubMed:10632874"
FT MUTAGEN 148
FT /note="G->D: Decreases the physical interaction with
FT ARG82."
FT /evidence="ECO:0000269|PubMed:10632874"
SQ SEQUENCE 177 AA; 19488 MW; 1F46C5C53ED88EE6 CRC64;
MTSNSDGSST SPVEKPITGD VETNEPTKPI RRLSTPSPEQ DQEGDFDEED DDDKFSVSTS
TPTPTITKTK DSSDTSTVTR RKQPIRYIEN KTRRHVTFSK RRHGIMKKAY ELSVLTGANI
LLLILANSGL VYTFTTPKLE PVVREDEGKS LIRACINASD TPDATDTSPA QEQSPAN
