ROG3_YEAST
ID ROG3_YEAST Reviewed; 733 AA.
AC P43602; D6VTQ2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein ROG3;
DE AltName: Full=Revertant of glycogen synthase kinase mutation protein 3;
GN Name=ROG3; OrderedLocusNames=YFR022W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
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 [3]
RP FUNCTION, DOMAIN, INTERACTION WITH RSP5, AND MUTAGENESIS OF 460-PRO-PRO-461
RP AND 625-PRO-PRO-626.
RX PubMed=12163175; DOI=10.1016/s0014-5793(02)03104-6;
RA Andoh T., Hirata Y., Kikuchi A.;
RT "PY motifs of Rod1 are required for binding to Rsp5 and for drug
RT resistance.";
RL FEBS Lett. 525:131-134(2002).
RN [4]
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).
RN [5]
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).
CC -!- FUNCTION: Involved in resistance to GST substrate o-dinitrobenzene (o-
CC DNB). {ECO:0000269|PubMed:12163175}.
CC -!- SUBUNIT: Interacts with RSP5 via its 2 PY-motifs.
CC {ECO:0000269|PubMed:12163175}.
CC -!- INTERACTION:
CC P43602; P39940: RSP5; NbExp=3; IntAct=EBI-22976, EBI-16219;
CC -!- DOMAIN: The PY-motifs are required for the interaction with RSP5
CC ubiquitin-ligase. {ECO:0000269|PubMed:12163175}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; D50617; BAA09261.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12462.1; -; Genomic_DNA.
DR PIR; S56277; S56277.
DR RefSeq; NP_116677.3; NM_001179987.3.
DR AlphaFoldDB; P43602; -.
DR BioGRID; 31175; 48.
DR DIP; DIP-4111N; -.
DR IntAct; P43602; 2.
DR MINT; P43602; -.
DR STRING; 4932.YFR022W; -.
DR iPTMnet; P43602; -.
DR MaxQB; P43602; -.
DR PaxDb; P43602; -.
DR PRIDE; P43602; -.
DR EnsemblFungi; YFR022W_mRNA; YFR022W; YFR022W.
DR GeneID; 850578; -.
DR KEGG; sce:YFR022W; -.
DR SGD; S000001918; ROG3.
DR VEuPathDB; FungiDB:YFR022W; -.
DR eggNOG; KOG3780; Eukaryota.
DR GeneTree; ENSGT00940000176571; -.
DR HOGENOM; CLU_018982_1_0_1; -.
DR InParanoid; P43602; -.
DR OMA; GMATPFH; -.
DR BioCyc; YEAST:G3O-30473-MON; -.
DR PRO; PR:P43602; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43602; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:SGD.
DR GO; GO:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IGI:SGD.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0070086; P:ubiquitin-dependent endocytosis; IBA:GO_Central.
DR Gene3D; 2.60.40.640; -; 1.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR011021; Arrestin-like_N.
DR InterPro; IPR011022; Arrestin_C-like.
DR Pfam; PF02752; Arrestin_C; 1.
DR Pfam; PF00339; Arrestin_N; 1.
DR SMART; SM01017; Arrestin_C; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..733
FT /note="Protein ROG3"
FT /id="PRO_0000202690"
FT REGION 518..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 460..463
FT /note="PY-motif"
FT MOTIF 625..628
FT /note="PY-motif"
FT COMPBIAS 519..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 460..461
FT /note="PP->QA: Reduced binding to RSP5."
FT /evidence="ECO:0000269|PubMed:12163175"
FT MUTAGEN 625..626
FT /note="PP->QA: Reduced binding to RSP5."
FT /evidence="ECO:0000269|PubMed:12163175"
SQ SEQUENCE 733 AA; 79709 MW; 2BC6F7F24B9806A5 CRC64;
MGFSSGKSTK KKPLLFDIRL KNVDNDVILL KGPPNEAPSV LLSGCIVLSI NEPMQIKSIS
LRLYGKIQID VPLERPQDAS SSSLSSSPPK IRKYNKVFYN YAWDNVNLKE YLSGLRGQSG
LAGSSSSSNI LGTRQRAQST SSLKSLKGSS SPSSCTLDKG NYDFPFSAIL PGSLPESVES
LPNCFVTYSM ESVIERSKNY SDLICRKNIR VLRTISPAAV ELSETVCVDN SWPDKVDYSI
SVPNKAVAIG SATPINISIV PLSKGLKLGS IKVVLFENYQ YCDPFPPVIS ENRQVTELNL
EDPLNESSGE FNGNGCFVNN PFFQPDHSFQ DKWEIDTILQ IPNSLSNCVQ DCDVRSNIKV
RHKLKFFIIL INPDGHKSEL RASLPIQLFI SPFVALSIKP LSSSNLYSLF STTNQKDENS
SQEEEEEYLF SRSASVTGLE LLADMRSGGS VPTISDLMTP PNYEMHVYDR LYSGSFTRTA
VETSGTCTPL GSECSTVEDQ QQDLEDLRIR LTKIRNQRDN LGLPPSASSA AASRSLSPLL
NVPAPEDGTE RILPQSALGP NSGSVPGVHS NVSPVLLSRS PAPSVSAHEV LPVPSGLNYP
ETQNLNKVPS YGKAMKYDII GEDLPPSYPC AIQNVQPRKP SRVHSRNSST TLSSSIPTSF
HSSSFMSSTA SPISIINGSR SSSSGVSLNT LNELTSKTSN NPSSNSMKRS PTRRRATSLA
GFMGGFLSKG NKR
