MRD1_YEAST
ID MRD1_YEAST Reviewed; 887 AA.
AC Q06106; D6W4B1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Multiple RNA-binding domain-containing protein 1;
GN Name=MRD1; OrderedLocusNames=YPR112C;
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 FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NOP1, AND RNA-BINDING.
RX PubMed=11884397; DOI=10.1074/jbc.m112395200;
RA Jin S.-B., Zhao J., Bjoerk P., Schmekel K., Ljungdahl P.O., Wieslander L.;
RT "Mrd1p is required for processing of pre-rRNA and for maintenance of
RT steady-state levels of 40 S ribosomal subunits in yeast.";
RL J. Biol. Chem. 277:18431-18439(2002).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220 AND SER-264, AND
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, 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: Involved in pre-rRNA processing. Required for maintaining
CC steady-state levels of 40S ribosomal subunit. Required for the initial
CC processing of pre-rRNA at the A0 to A2 sites, leading to the processing
CC of the 23S pre-rRNA intermediate to the 18S rRNA.
CC {ECO:0000269|PubMed:11884397}.
CC -!- SUBUNIT: Interacts with NOP1. Binds to the 35S pre-rRNA and the U3
CC snoRNA. {ECO:0000269|PubMed:11884397}.
CC -!- INTERACTION:
CC Q06106; P53254: UTP22; NbExp=3; IntAct=EBI-34383, EBI-1878;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11884397}.
CC -!- MISCELLANEOUS: Present with 2220 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RRM MRD1 family. {ECO:0000305}.
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DR EMBL; U32445; AAB68082.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11527.1; -; Genomic_DNA.
DR PIR; S59777; S59777.
DR RefSeq; NP_015437.1; NM_001184209.1.
DR AlphaFoldDB; Q06106; -.
DR SMR; Q06106; -.
DR BioGRID; 36279; 312.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-6281N; -.
DR IntAct; Q06106; 53.
DR MINT; Q06106; -.
DR STRING; 4932.YPR112C; -.
DR iPTMnet; Q06106; -.
DR MaxQB; Q06106; -.
DR PaxDb; Q06106; -.
DR PRIDE; Q06106; -.
DR EnsemblFungi; YPR112C_mRNA; YPR112C; YPR112C.
DR GeneID; 856228; -.
DR KEGG; sce:YPR112C; -.
DR SGD; S000006316; MRD1.
DR VEuPathDB; FungiDB:YPR112C; -.
DR eggNOG; KOG0110; Eukaryota.
DR GeneTree; ENSGT00840000129953; -.
DR HOGENOM; CLU_008479_0_0_1; -.
DR InParanoid; Q06106; -.
DR OMA; TALIEYC; -.
DR BioCyc; YEAST:G3O-34252-MON; -.
DR PRO; PR:Q06106; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06106; protein.
DR GO; GO:0030686; C:90S preribosome; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0042134; F:rRNA primary transcript binding; IDA:SGD.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:2000815; P:regulation of mRNA stability involved in response to oxidative stress; IBA:GO_Central.
DR GO; GO:0034462; P:small-subunit processome assembly; IMP:SGD.
DR CDD; cd12568; RRM3_MRD1; 1.
DR Gene3D; 3.30.70.330; -; 5.
DR InterPro; IPR034482; Mrd1_RRM3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 5.
DR SMART; SM00360; RRM; 5.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 5.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW RNA-binding; rRNA processing.
FT CHAIN 1..887
FT /note="Multiple RNA-binding domain-containing protein 1"
FT /id="PRO_0000081647"
FT DOMAIN 2..94
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 345..423
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 532..604
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 663..746
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 763..840
FT /note="RRM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 121..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
SQ SEQUENCE 887 AA; 101120 MW; 1E34816BD486DEA8 CRC64;
MSRIIVKGLP VYLTDDNLRE HFTKRLRQKH SHQAVNGSGP DLITDVKILR DRNGESRRFG
FIGYRNEEDA FDAVEYFNGS FINTSKIEVS MAKSFADPRV PQPMKEKRRE ALKRFREKEE
KLLQEENRKK KKVDENKHSN IDDEIRKNKQ LQEFMETMKP SSQVTSWEKV GIDKSIEDEK
LKREEEDSSV QGNSLLAHAL ALKEENNKDE APNLVIENES DDEYSALNRN RDEDQEDAGE
EEKMISISNL KDTDIGLVND DANSDEKENE KRRNLAQDEK VSDLDWFKQR RVRIKESEAE
TREKSSSYAT EQNESLDTKK EEQPERAVPQ KTDEELAIEK INQTGRLFLR NILYTSKEED
FRKLFSPFGE LEEVHVALDT RTGQSKGFAY VLFKDSKNAV NAYVELDKQI FQGRLLHILP
GEEKKSHRLD EFDLKNMPLK KQKELKRKAA ASRQTFSWNS LYMNQDAVLG SVAAKLGLEK
SQLIDAENSS SAVKQALAEA HVIGDVRKYF ESKGVDLTKF SQLKSTNQRD DKVILVKNFP
FGTTREELGE MFLPYGKLER LLMPPAGTIA IVQFRDTTSA RAAFTKLSYK RFKDGIIYLE
RGPKDCFTKP AEADDLINNT SAKEEENPVE VKPSSNDLME ANKDVTEGSS NAHDEDVIDG
PTVSIFIKNL NFSTTNQNLT DRFKVFTGFV VAQVKTKPDP KHQGKTLSMG FGFVEFRTKE
QANAVIAAMD GTVIDGHKIQ LKLSHRQASQ SGNTKTKSNK KSGKIIVKNL PFEATRKDVF
ELFNSFGQLK SVRVPKKFDK SARGFAFVEF LLPKEAENAM DQLHGVHLLG RRLVMQYAEE
DAVDAEEEIA RMTKKVRKQV ATNEMAALRN GGGRKKLDVD DEENEGF
