RTG3_YEAST
ID RTG3_YEAST Reviewed; 486 AA.
AC P38165; D6VPQ0; P89494;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Retrograde regulation protein 3;
GN Name=RTG3; OrderedLocusNames=YBL103C; ORFNames=YBL0810;
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].
RC STRAIN=S288c / GRF88;
RX PubMed=9032238; DOI=10.1128/mcb.17.3.1110;
RA Jia Y., Rothermel B., Thornton J., Butow R.A.;
RT "A basic helix-loop-helix-leucine zipper transcription complex in yeast
RT functions in a signaling pathway from mitochondria to the nucleus.";
RL Mol. Cell. Biol. 17:1110-1117(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7502586; DOI=10.1002/yea.320111112;
RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT cerevisiae chromosome II.";
RL Yeast 11:1103-1112(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
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 [5]
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 [6]
RP DOMAIN.
RX PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
RA Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.;
RT "Nine-amino-acid transactivation domain: establishment and prediction
RT utilities.";
RL Genomics 89:756-768(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123 AND SER-142, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; THR-150; SER-227 AND
RP SER-236, AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-123; SER-142;
RP SER-236; SER-241 AND SER-269, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP IDENTIFICATION BY MASS 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 -!- FUNCTION: Transcription factor that regulates CIT2 gene expression.
CC Binds to two identical sites oriented as inverted repeats 28 bp apart
CC in a regulatory upstream activation sequence element (UASR) in the CIT2
CC promoter. The core binding site is 5'-GGTCAC-3'.
CC -!- SUBUNIT: Binds DNA as a heterodimer with RTG1.
CC -!- INTERACTION:
CC P38165; P32607: RTG1; NbExp=4; IntAct=EBI-16328, EBI-16312;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DOMAIN: the 9aaTAD motifs are transactivation domains present in a
CC large number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:17467953}.
CC -!- MISCELLANEOUS: Present with 1050 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA55992.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U46012; AAA86842.1; -; Genomic_DNA.
DR EMBL; X79489; CAA55992.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z35864; CAA84929.1; -; Genomic_DNA.
DR EMBL; Z35865; CAA84931.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07020.1; -; Genomic_DNA.
DR PIR; S74319; S74319.
DR RefSeq; NP_009447.1; NM_001178343.1.
DR AlphaFoldDB; P38165; -.
DR SMR; P38165; -.
DR BioGRID; 32600; 460.
DR ComplexPortal; CPX-828; RTG transcription factor complex.
DR DIP; DIP-2501N; -.
DR IntAct; P38165; 23.
DR MINT; P38165; -.
DR STRING; 4932.YBL103C; -.
DR iPTMnet; P38165; -.
DR MaxQB; P38165; -.
DR PaxDb; P38165; -.
DR PRIDE; P38165; -.
DR EnsemblFungi; YBL103C_mRNA; YBL103C; YBL103C.
DR GeneID; 852171; -.
DR KEGG; sce:YBL103C; -.
DR SGD; S000000199; RTG3.
DR VEuPathDB; FungiDB:YBL103C; -.
DR eggNOG; KOG1318; Eukaryota.
DR HOGENOM; CLU_043302_0_0_1; -.
DR InParanoid; P38165; -.
DR OMA; DDAMFNY; -.
DR BioCyc; YEAST:G3O-28987-MON; -.
DR Reactome; R-SCE-3232118; SUMOylation of transcription factors.
DR PRO; PR:P38165; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38165; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA: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:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0071400; P:cellular response to oleic acid; IMP:SGD.
DR GO; GO:0031930; P:mitochondria-nucleus signaling pathway; IDA:SGD.
DR GO; GO:0016559; P:peroxisome fission; IDA:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..486
FT /note="Retrograde regulation protein 3"
FT /id="PRO_0000127434"
FT DOMAIN 285..344
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 75..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 27..35
FT /note="9aaTAD 1"
FT MOTIF 189..197
FT /note="9aaTAD 2"
FT COMPBIAS 243..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 150
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 486 AA; 54140 MW; DB635FFDEC740C11 CRC64;
MMNNNESEAE NQRLLDELMN QTKVLQETLD FSLVTPTPHH NDDYKIHGSA YPGGETPAQQ
HEKLSYINTH NSNDNNNLMG SQARSNSQTP TASTIYEEAE SQSSYLDDMF RTSQGGRPVT
QNSISSIGQG PLRSSYSMAY DSPVDRAMNT PLQQQEGLKA ELPHDFLFQH GTDDTMYNLT
DDLSSSLSSS INSDMMTPNT YSSSFSYNPQ SLGPASVSST YSPKVRSPSS SFRAGSFLSS
SFRHGSINTP RTRHTSISSN MTENIGPGSV PKILGGLTSD EKLRRKREFH NAVERRRREL
IKQKIKELGQ LVPPSLLNYD DLGKQIKPNK GIILDRTVEY LQYLAEILEI QARKKKALLA
KIKELEEKKS SVAALSPFTN NHHASSGQNN SENSEERIID IRSVPNALMN EQNSKAELHN
WEPPLYDSVG NHNHAGTMES HPHTNIHEEL KEFLSGDLIE AEDNAKLMFG DDNSNPADYL
LEFGSG
