RIM4_YEAST
ID RIM4_YEAST Reviewed; 713 AA.
AC P38741; D3DKU4; E9P8V3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Meiotic activator RIM4;
DE AltName: Full=Regulator of IME2 protein 4;
GN Name=RIM4; OrderedLocusNames=YHL024W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 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 [4]
RP FUNCTION.
RX PubMed=8417990; DOI=10.1093/genetics/133.1.67;
RA Su S.S., Mitchell A.P.;
RT "Identification of functionally related genes that stimulate early meiotic
RT gene expression in yeast.";
RL Genetics 133:67-77(1993).
RN [5]
RP FUNCTION, INDUCTION, AND MUTAGENESIS OF PHE-96; PHE-139; PHE-349 AND
RP PHE-385.
RX PubMed=10806425;
RX DOI=10.1002/(sici)1097-0061(200005)16:7<631::aid-yea559>3.0.co;2-u;
RA Soushko M., Mitchell A.P.;
RT "An RNA-binding protein homologue that promotes sporulation-specific gene
RT expression in Saccharomyces cerevisiae.";
RL Yeast 16:631-639(2000).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=11713679; DOI=10.1007/s004380100571;
RA Deng C., Saunders W.S.;
RT "RIM4 encodes a meiotic activator required for early events of meiosis in
RT Saccharomyces cerevisiae.";
RL Mol. Genet. Genomics 266:497-504(2001).
RN [7]
RP UBIQUITINATION BY RSP5.
RX PubMed=15955809; DOI=10.1074/jbc.m502197200;
RA Kus B., Gajadhar A., Stanger K., Cho R., Sun W., Rouleau N., Lee T.,
RA Chan D., Wolting C., Edwards A., Bosse R., Rotin D.;
RT "A high throughput screen to identify substrates for the ubiquitin ligase
RT Rsp5.";
RL J. Biol. Chem. 280:29470-29478(2005).
RN [8]
RP UBIQUITINATION BY RSP5.
RX PubMed=17551511; DOI=10.1038/msb4100159;
RA Gupta R., Kus B., Fladd C., Wasmuth J., Tonikian R., Sidhu S., Krogan N.J.,
RA Parkinson J., Rotin D.;
RT "Ubiquitination screen using protein microarrays for comprehensive
RT identification of Rsp5 substrates in yeast.";
RL Mol. Syst. Biol. 3:116-116(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525, AND IDENTIFICATION BY
RP 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: Positive regulator of sporulation-specific genes and of
CC sporulation. Required for premeiotic DNA synthesis and meiotic
CC chromosomal segregation. May act in a nutritional signaling pathway.
CC {ECO:0000269|PubMed:10806425, ECO:0000269|PubMed:11713679,
CC ECO:0000269|PubMed:8417990}.
CC -!- INDUCTION: Expressed at elevated levels early in meiosis. Expression
CC depends on IME1. {ECO:0000269|PubMed:10806425,
CC ECO:0000269|PubMed:11713679}.
CC -!- PTM: Polyubiquitinated by RSP5. {ECO:0000269|PubMed:15955809,
CC ECO:0000269|PubMed:17551511}.
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DR EMBL; U11582; AAB65077.1; -; Genomic_DNA.
DR EMBL; AY558114; AAS56440.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06661.1; -; Genomic_DNA.
DR PIR; S46838; S46838.
DR RefSeq; NP_011839.1; NM_001179104.1.
DR AlphaFoldDB; P38741; -.
DR BioGRID; 36398; 130.
DR DIP; DIP-5673N; -.
DR IntAct; P38741; 3.
DR MINT; P38741; -.
DR STRING; 4932.YHL024W; -.
DR iPTMnet; P38741; -.
DR PaxDb; P38741; -.
DR PRIDE; P38741; -.
DR EnsemblFungi; YHL024W_mRNA; YHL024W; YHL024W.
DR GeneID; 856361; -.
DR KEGG; sce:YHL024W; -.
DR SGD; S000001016; RIM4.
DR VEuPathDB; FungiDB:YHL024W; -.
DR eggNOG; ENOG502QUGB; Eukaryota.
DR HOGENOM; CLU_016668_0_0_1; -.
DR InParanoid; P38741; -.
DR OMA; LNKTMHV; -.
DR BioCyc; YEAST:G3O-31044-MON; -.
DR PRO; PR:P38741; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38741; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IMP:SGD.
DR GO; GO:0017069; F:snRNA binding; IBA:GO_Central.
DR GO; GO:0030619; F:U1 snRNA binding; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0006279; P:premeiotic DNA replication; IMP:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:SGD.
DR CDD; cd12453; RRM1_RIM4_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034352; Rim4_RRM1.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00361; RRM_1; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Meiosis; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Sporulation; Ubl conjugation.
FT CHAIN 1..713
FT /note="Meiotic activator RIM4"
FT /id="PRO_0000082031"
FT DOMAIN 93..172
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 346..420
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..70
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 96
FT /note="F->L: Leads to absolute sporulation defect."
FT /evidence="ECO:0000269|PubMed:10806425"
FT MUTAGEN 139
FT /note="F->L: Leads to absolute sporulation defect."
FT /evidence="ECO:0000269|PubMed:10806425"
FT MUTAGEN 349
FT /note="F->L: Leads to mild sporulation defect."
FT /evidence="ECO:0000269|PubMed:10806425"
FT MUTAGEN 385
FT /note="F->L: Leads to absolute sporulation defect."
FT /evidence="ECO:0000269|PubMed:10806425"
FT CONFLICT 385
FT /note="F -> V (in Ref. 3; AAS56440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 713 AA; 80109 MW; AEB3C53530677837 CRC64;
MKTEISTADS LRDPPSNGLK ADSELVIRED IDQFLPSEVS SLGSDHQNDG EDSDTDSDNF
LQDPEDDVDE ESTGRGTVTT TSTSTESRGR PSSCIFVASL AAALSDDELC LSVTENFKKY
GDLARVKVLR DNANRPYAFV QYNNDHDAKH ALIRAQGTLL NGRRLRCEPA KVNRTLYLKN
QQSIDFNEIS QICEKFGGLE QIVPDRTDNQ YTRRYTYPIS SANSWFVQFV YRDDAIRAYA
NLRTDPNWII EWAQNINVPK NYNLLHKSKF KSSKYHQNNG IINNDGSNNN DNNNSNNNNR
EDSRRNGDVI EEECGHVHGS DSEEKLTSDG IYDDEDKDSE ITIDKRSIFV GQLDKETTRE
ELNRRFSTHG KIQDINLIFK PTNIFAFIKY ETEEAAAAAL ESENHAIFLN KTMHVQYKEV
GGRHNRKFSG KNGGSNFNHH QFFSTRSGKT FTGPELNLAP PPINMYRKMS GGSQQESETM
MPYMPMGPMP MGPPPPNAAS LSDFDMFPPS YSTFMKGMMP LRRKSMPNSW SSPSSKSVNS
ENESVNGGDE NSELPSEIPE SSGRYNAANS FTTYNNSSAG NSNNNNNNNN SNSNKSQYKK
RYARRSSYGY NEVPPKPYYF QPYYYHPMQY HMGPMGPLHP SQGSAGNHHP YMMVYPMSPP
PPSGLDGSMI PPPINVSQSH AANHGSTHVH ANEFISNDTG DINEDNKAYS LDY
