MRN1_YEAST
ID MRN1_YEAST Reviewed; 612 AA.
AC Q08925; D6W3I4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=RNA-binding protein MRN1;
DE AltName: Full=Multicopy suppressor of RSC-NHP6 synthetic lethality protein 1;
DE AltName: Full=Post-transcriptional regulator of 69 kDa;
GN Name=MRN1; Synonyms=PTR69; OrderedLocusNames=YPL184C;
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=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 [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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
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 [5]
RP RNA-BINDING, AND FUNCTION.
RX PubMed=18959479; DOI=10.1371/journal.pbio.0060255;
RA Hogan D.J., Riordan D.P., Gerber A.P., Herschlag D., Brown P.O.;
RT "Diverse RNA-binding proteins interact with functionally related sets of
RT RNAs, suggesting an extensive regulatory system.";
RL PLoS Biol. 6:E255-E255(2008).
RN [6]
RP RNA-BINDING.
RX PubMed=20959291; DOI=10.1093/nar/gkq920;
RA Riordan D.P., Herschlag D., Brown P.O.;
RT "Identification of RNA recognition elements in the Saccharomyces cerevisiae
RT transcriptome.";
RL Nucleic Acids Res. 39:1501-1509(2011).
CC -!- FUNCTION: RNA-binding protein that binds specific categories of mRNAs,
CC including those that contain upstream open reading frames (uORFs) and
CC internal ribosome entry sites (IRES). Probably involved in
CC translational regulation. {ECO:0000269|PubMed:18959479}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 7950 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z73540; CAA97894.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11250.1; -; Genomic_DNA.
DR PIR; S65196; S65196.
DR RefSeq; NP_015140.1; NM_001183998.1.
DR AlphaFoldDB; Q08925; -.
DR BioGRID; 35998; 223.
DR IntAct; Q08925; 8.
DR MINT; Q08925; -.
DR STRING; 4932.YPL184C; -.
DR iPTMnet; Q08925; -.
DR MaxQB; Q08925; -.
DR PaxDb; Q08925; -.
DR PRIDE; Q08925; -.
DR EnsemblFungi; YPL184C_mRNA; YPL184C; YPL184C.
DR GeneID; 855917; -.
DR KEGG; sce:YPL184C; -.
DR SGD; S000006105; MRN1.
DR VEuPathDB; FungiDB:YPL184C; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_017390_1_0_1; -.
DR InParanoid; Q08925; -.
DR OMA; RWSPTSF; -.
DR BioCyc; YEAST:G3O-34078-MON; -.
DR PRO; PR:Q08925; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08925; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IGI:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IGI:SGD.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd12520; RRM1_MRN1; 1.
DR CDD; cd12262; RRM2_4_MRN1; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR039171; Cwc2/Slt11.
DR InterPro; IPR034195; Mrn1_RRM1.
DR InterPro; IPR034194; Mrn1_RRM2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR14089; PTHR14089; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Repeat; RNA-binding; Translation regulation.
FT CHAIN 1..612
FT /note="RNA-binding protein MRN1"
FT /id="PRO_0000082038"
FT DOMAIN 201..274
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 292..379
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 431..504
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 522..602
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 68664 MW; A1B2EB381C0BBC8E CRC64;
MVVSYNNNNN NNNNNNNNNI SNNNNNNNMF PPFPSSDDFA MYQQSSSSGP YQETYASGPQ
NFGDAVYPMN GNFTLLPSDF TREPNDSFFY ENDGIFDYQR IQQQPTQFQT KQRNDSQQQR
FSQEQNFEID NEVVHNNNRY YEYERSSNEV SPFDDENPNV LSDGMSPTIM ATATAVTNAN
APLPVNAQAN NPLNFTSAPS RTVYLGNVPP NLSVKELLDH VRSGVVEDVK IIPEKMCAFV
SFIDESAALL FHSDAILKRL NIGDRDIKIG WGKPTRIDPI VAARISTDGA TRNVYIGRMT
IEGEESHLSE EQLRVDLEEY GEIDCIKIIK EKGIAFIHFA SILNAIKVVT NLPIRNPYYQ
NKRIFYGKDR CAFITKTQQH NAAQFLGVQP GMEHMIEFSD REFISNALLQ QSAAAAAIAT
SAGGPNNLGN RTVYLGSLPK DVKIEEICNA VRGGLLQSIK LLNDRYVCFV TFIDPTAAAQ
FYAMSSLYGF TVQKKRCKVG WGKHSGPLPN ALALAVSNGA SRNVYVGNID FVGDSLRDER
VFTESNLRHI FQQYGEVEQI NFLPEKNCCF INYTNISNAI LALDKIKSNP YFKDLKINFG
KDRCGNVPHQ SR
