RLM1_YEAST
ID RLM1_YEAST Reviewed; 676 AA.
AC Q12224; D6W3S8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Transcription factor RLM1;
GN Name=RLM1; OrderedLocusNames=YPL089C; ORFNames=LPG19C;
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=ATCC 204508 / S288c;
RX PubMed=7565726; DOI=10.1128/mcb.15.10.5740;
RA Watanabe Y., Irie K., Matsumoto K.;
RT "Yeast RLM1 encodes a serum response factor-like protein that may function
RT downstream of the Mpk1 (Slt2) mitogen-activated protein kinase pathway.";
RL Mol. Cell. Biol. 15:5740-5749(1995).
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 CHARACTERIZATION.
RX PubMed=9121433; DOI=10.1128/mcb.17.4.1848;
RA Dodou E., Treisman R.;
RT "The Saccharomyces cerevisiae MADS-box transcription factor Rlm1 is a
RT target for the Mpk1 mitogen-activated protein kinase pathway.";
RL Mol. Cell. Biol. 17:1848-1859(1997).
RN [5]
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH KDX1 AND SLT2.
RX PubMed=9111331; DOI=10.1128/mcb.17.5.2615;
RA Watanabe Y., Takaesu G., Hagiwara M., Irie K., Matsumoto K.;
RT "Characterization of a serum response factor-like protein in Saccharomyces
RT cerevisiae, Rlm1, which has transcriptional activity regulated by the Mpk1
RT (Slt2) mitogen-activated protein kinase pathway.";
RL Mol. Cell. Biol. 17:2615-2623(1997).
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 SER-164; SER-374 AND SER-377, 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-374, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-374 AND SER-377, 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).
CC -!- FUNCTION: May function as a transcription factor downstream of MPK1
CC that is subject to activation by the MPK1 mitogen-activated protein
CC kinase pathway. Binds to the DNA sequence 5'-CTA[TA](4)TAG-3'. At least
CC some RML1 target genes are involved in cell wall biosynthesis.
CC {ECO:0000269|PubMed:9111331}.
CC -!- SUBUNIT: Can heterodimerize with SPM1. Interacts with KDX1 and SLT2.
CC {ECO:0000269|PubMed:9111331}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
CC -!- PTM: Phosphorylated by SLT2. {ECO:0000269|PubMed:9111331}.
CC -!- MISCELLANEOUS: Present with 736 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MEF2 family. {ECO:0000305}.
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DR EMBL; U43281; AAB68210.1; -; Genomic_DNA.
DR EMBL; D63340; BAA09658.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11344.1; -; Genomic_DNA.
DR PIR; S61977; S61977.
DR RefSeq; NP_015236.1; NM_001183903.1.
DR AlphaFoldDB; Q12224; -.
DR SMR; Q12224; -.
DR BioGRID; 36092; 125.
DR DIP; DIP-2480N; -.
DR ELM; Q12224; -.
DR IntAct; Q12224; 12.
DR MINT; Q12224; -.
DR STRING; 4932.YPL089C; -.
DR iPTMnet; Q12224; -.
DR MaxQB; Q12224; -.
DR PaxDb; Q12224; -.
DR PRIDE; Q12224; -.
DR EnsemblFungi; YPL089C_mRNA; YPL089C; YPL089C.
DR GeneID; 856016; -.
DR KEGG; sce:YPL089C; -.
DR SGD; S000006010; RLM1.
DR VEuPathDB; FungiDB:YPL089C; -.
DR eggNOG; KOG0014; Eukaryota.
DR GeneTree; ENSGT00940000169350; -.
DR HOGENOM; CLU_022725_0_0_1; -.
DR InParanoid; Q12224; -.
DR OMA; MFQEWPF; -.
DR BioCyc; YEAST:G3O-33994-MON; -.
DR Reactome; R-SCE-525793; Myogenesis.
DR PRO; PR:Q12224; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12224; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0008301; F:DNA binding, bending; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:UniProtKB.
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:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IDA:SGD.
DR GO; GO:0060256; P:regulation of flocculation; IMP:SGD.
DR GO; GO:1903450; P:regulation of G1 to G0 transition; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IMP:SGD.
DR CDD; cd00265; MADS_MEF2_like; 1.
DR Gene3D; 3.40.1810.10; -; 1.
DR InterPro; IPR033896; MADS_MEF2-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 DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..676
FT /note="Transcription factor RLM1"
FT /id="PRO_0000199440"
FT DOMAIN 3..57
FT /note="MADS-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT DNA_BIND 58..87
FT /note="Mef2-type"
FT /evidence="ECO:0000255"
FT REGION 103..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 676 AA; 73484 MW; 9CE6B3DE47632747 CRC64;
MGRRKIEIQR ISDDRNRAVT FIKRKAGLFK KAHELSVLCQ VDIAVIILGS NNTFYEFSSV
DTNDLIYHYQ NDKNLLHEVK DPSDYGDFHK SASVNINQDL LRSSMSNKPS KSNVKGMNQS
ENDDDENNDE DDDDHGNFER NSNMHSNKKA SDKNIPSAHM KLLSPTALIS KMDGSEQNKR
HPENALPPLQ HLKRLKPDPL QISRTPQQQQ QQNISRPYHS SMYNLNQPSS SSSSPSTMDF
PKLPSFQNSS FNGRPPPISI SPNKFSKPFT NASSRTPKQE HKINNSGSNN NDNSNYTQSP
SNSLEDSIQQ TVKARRKLSA RPVLRVRIPN NNFSSNSAIP SEPSSASSTS ANGNSMGSSQ
IMKENKTSRS SKISPLSASA SGPLTLQKGN NGRMVIKLPN ANAPNGSNNG NGSNNNNHPY
PFGSGSSPLF SATQPYIATP LQPSNIPGGP FQQNTSFLAQ RQTQQYQQMS FKKQSQTVPL
TTTLTGRPPS TFSGPETSNG PPTGSLPSKF VHDLMSNSPN VSSISMFPDW SMGPNSAKPG
NTNNPGTFPP VQTAVNNGNS SNISSTNNTN NNNNNNNNNS SNNNSNNGND NNSNNSNNSY
YSNNEDAPVN GAAISEHTTD GDSNNQSNSS TYDAAATAYN GNTGLTPYIN TAQTPLGTKF
FNFSTDISGE KNSSKI
