MRB1_YEAST
ID MRB1_YEAST Reviewed; 306 AA.
AC Q06390; D6VT05;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Methylated RNA-binding protein 1;
DE AltName: Full=PHOsphate metabolism protein 92 {ECO:0000303|PubMed:24206186};
DE AltName: Full=YTH domain-containing protein PHO92;
GN Name=PHO92 {ECO:0000303|PubMed:24206186}; Synonyms=MRB1;
GN OrderedLocusNames=YDR374C;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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, AND RNA-BINDING.
RX PubMed=24206186; DOI=10.1042/bj20130862;
RA Kang H.J., Jeong S.J., Kim K.N., Baek I.J., Chang M., Kang C.M., Park Y.S.,
RA Yun C.W.;
RT "A novel protein, Pho92, has a conserved YTH domain and regulates phosphate
RT metabolism by decreasing the mRNA stability of PHO4 in Saccharomyces
RT cerevisiae.";
RL Biochem. J. 457:391-400(2014).
RN [4]
RP FUNCTION, RNA-BINDING, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=24269006; DOI=10.1016/j.cell.2013.10.047;
RA Schwartz S., Agarwala S.D., Mumbach M.R., Jovanovic M., Mertins P.,
RA Shishkin A., Tabach Y., Mikkelsen T.S., Satija R., Ruvkun G., Carr S.A.,
RA Lander E.S., Fink G.R., Regev A.;
RT "High-resolution mapping reveals a conserved, widespread, dynamic mRNA
RT methylation program in yeast meiosis.";
RL Cell 155:1409-1421(2013).
RN [5] {ECO:0007744|PDB:4RCM}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 141-306 IN COMPLEX WITH
RP N6-METHYLADENOSINE (M6A)-CONTAINING RNA, FUNCTION, RNA-BINDING, AND
RP MUTAGENESIS OF TRP-177; TRP-231 AND ARG-273.
RX PubMed=26318451; DOI=10.1074/jbc.m115.680389;
RA Xu C., Liu K., Ahmed H., Loppnau P., Schapira M., Min J.;
RT "structural basis for the discriminative recognition of N6-methyladenosine
RT RNA by the human YT521-B homology domain family of proteins.";
RL J. Biol. Chem. 290:24902-24913(2015).
CC -!- FUNCTION: RNA-binding protein that acts as a post-transcriptional
CC regulator of phosphate metabolism by binding to the 3'-UTR region of
CC PHO4 mRNA, decreasing its stability (PubMed:24206186). Acts by
CC recognizing and binding N6-methyladenosine (m6A)-containing RNAs, a
CC modification present at internal sites of mRNAs and some non-coding
CC RNAs (PubMed:24269006, PubMed:26318451). {ECO:0000269|PubMed:24206186,
CC ECO:0000269|PubMed:24269006, ECO:0000269|PubMed:26318451}.
CC -!- DEVELOPMENTAL STAGE: Expressed in a meiosis-specific manner.
CC {ECO:0000269|PubMed:24269006}.
CC -!- DISRUPTION PHENOTYPE: Defects in meiotic progression.
CC {ECO:0000269|PubMed:24269006}.
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DR EMBL; U28373; AAB64810.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12215.1; -; Genomic_DNA.
DR PIR; S61169; S61169.
DR RefSeq; NP_010662.3; NM_001180682.3.
DR PDB; 4RCM; X-ray; 1.80 A; A/B=141-306.
DR PDBsum; 4RCM; -.
DR AlphaFoldDB; Q06390; -.
DR SMR; Q06390; -.
DR BioGRID; 32433; 79.
DR DIP; DIP-5677N; -.
DR IntAct; Q06390; 3.
DR MINT; Q06390; -.
DR STRING; 4932.YDR374C; -.
DR PaxDb; Q06390; -.
DR PRIDE; Q06390; -.
DR EnsemblFungi; YDR374C_mRNA; YDR374C; YDR374C.
DR GeneID; 851980; -.
DR KEGG; sce:YDR374C; -.
DR SGD; S000002782; PHO92.
DR VEuPathDB; FungiDB:YDR374C; -.
DR eggNOG; KOG1901; Eukaryota.
DR GeneTree; ENSGT00940000170935; -.
DR HOGENOM; CLU_064798_1_0_1; -.
DR InParanoid; Q06390; -.
DR OMA; ERTHIEV; -.
DR BioCyc; YEAST:G3O-29924-MON; -.
DR PRO; PR:Q06390; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06390; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; IDA:UniProtKB.
DR GO; GO:0061157; P:mRNA destabilization; IBA:GO_Central.
DR GO; GO:0043488; P:regulation of mRNA stability; IMP:SGD.
DR GO; GO:0019220; P:regulation of phosphate metabolic process; IMP:SGD.
DR InterPro; IPR007275; YTH_domain.
DR InterPro; IPR045168; YTH_prot.
DR PANTHER; PTHR12357; PTHR12357; 1.
DR Pfam; PF04146; YTH; 1.
DR PROSITE; PS50882; YTH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; RNA-binding.
FT CHAIN 1..306
FT /note="Methylated RNA-binding protein 1"
FT /id="PRO_0000253821"
FT DOMAIN 155..290
FT /note="YTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00225"
FT BINDING 161..163
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000269|PubMed:26318451,
FT ECO:0007744|PDB:4RCM"
FT BINDING 207
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT BINDING 231
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000250|UniProtKB:Q9BYJ9"
FT MUTAGEN 177
FT /note="W->A: Abolishes binding to N6-methyladenosine (m6A)-
FT containing RNAs."
FT /evidence="ECO:0000269|PubMed:26318451"
FT MUTAGEN 231
FT /note="W->A: Abolishes binding to N6-methyladenosine (m6A)-
FT containing RNAs."
FT /evidence="ECO:0000269|PubMed:26318451"
FT MUTAGEN 273
FT /note="R->A: Abolishes binding to N6-methyladenosine (m6A)-
FT containing RNAs."
FT /evidence="ECO:0000269|PubMed:26318451"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:4RCM"
FT HELIX 165..174
FT /evidence="ECO:0007829|PDB:4RCM"
FT HELIX 181..192
FT /evidence="ECO:0007829|PDB:4RCM"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:4RCM"
FT TURN 207..210
FT /evidence="ECO:0007829|PDB:4RCM"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:4RCM"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:4RCM"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:4RCM"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:4RCM"
FT STRAND 240..251
FT /evidence="ECO:0007829|PDB:4RCM"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:4RCM"
FT TURN 262..266
FT /evidence="ECO:0007829|PDB:4RCM"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:4RCM"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:4RCM"
SQ SEQUENCE 306 AA; 36052 MW; DA06874B5D36B6FF CRC64;
MNQIWSTGPP NFYFNSEWKE NKRNDRTIED SLRELDGLIH SLERTHIEVQ TNPKLKNDVT
ALNDINKKEN KEEITHENYT HQINSIPLTS SNLNRHFSFS RDYNQSDNSN NNYYREYLSK
PRYLQQSTKE QTFNEINKRK SAAIIPPWLN IPENSRFFVI KSSSLKHVKR SFYNGIWSST
HFGNKRLSEA YKKLNSGAKV FLFFSINTSG RFCGVAEMVS DLKMDLDTSI WEDEQKYGKA
FKVRWVIVRD INNRSLKRFL IPSNEMKPIT HSRDTQEIPY SIGISIINLF KTQDSDIFSF
LDETYE
