UTP18_ARATH
ID UTP18_ARATH Reviewed; 546 AA.
AC Q9FMU5;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=U3 small nucleolar RNA-associated protein 18 homolog;
GN OrderedLocusNames=At5g14050; ORFNames=MUA22.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP DWD MOTIF.
RX PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA He Y.J., Xiong Y., Deng X.W.;
RT "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL Plant Cell 20:152-167(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- DOMAIN: The DWD box is required for interaction with DDB1A.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat UTP18 family. {ECO:0000305}.
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DR EMBL; AB007650; BAB08284.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91981.1; -; Genomic_DNA.
DR EMBL; AY075678; AAL77685.1; -; mRNA.
DR EMBL; AY133634; AAM91464.1; -; mRNA.
DR RefSeq; NP_196909.1; NM_121408.4.
DR AlphaFoldDB; Q9FMU5; -.
DR SMR; Q9FMU5; -.
DR BioGRID; 16532; 1.
DR IntAct; Q9FMU5; 1.
DR STRING; 3702.AT5G14050.1; -.
DR iPTMnet; Q9FMU5; -.
DR PaxDb; Q9FMU5; -.
DR PRIDE; Q9FMU5; -.
DR ProteomicsDB; 228665; -.
DR EnsemblPlants; AT5G14050.1; AT5G14050.1; AT5G14050.
DR GeneID; 831254; -.
DR Gramene; AT5G14050.1; AT5G14050.1; AT5G14050.
DR KEGG; ath:AT5G14050; -.
DR Araport; AT5G14050; -.
DR TAIR; locus:2174698; AT5G14050.
DR eggNOG; KOG2055; Eukaryota.
DR HOGENOM; CLU_011055_3_0_1; -.
DR InParanoid; Q9FMU5; -.
DR OMA; QFHPTST; -.
DR OrthoDB; 462558at2759; -.
DR PhylomeDB; Q9FMU5; -.
DR PRO; PR:Q9FMU5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMU5; baseline and differential.
DR Genevisible; Q9FMU5; AT.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0034388; C:Pwp2p-containing subcomplex of 90S preribosome; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045161; Utp18.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR18359; PTHR18359; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; rRNA processing;
KW WD repeat.
FT CHAIN 1..546
FT /note="U3 small nucleolar RNA-associated protein 18
FT homolog"
FT /id="PRO_0000051407"
FT REPEAT 242..281
FT /note="WD 1"
FT REPEAT 372..411
FT /note="WD 2"
FT REPEAT 413..454
FT /note="WD 3"
FT REPEAT 509..545
FT /note="WD 4"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 389..404
FT /note="DWD box"
FT COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
SQ SEQUENCE 546 AA; 60988 MW; E9EC814182927327 CRC64;
MSLSQNAPKS KGIKREELKK QYEDVEDEEE IGSDDDLTRG KRRKTEKEKQ KLEESELVEM
KKLENLIFGS LYSPVTFGKE EEEDGSALFH VDRSAVRQIP DYEDDGDDDE ELSDEENGQV
VAIRKGEAAW EDEEEKQINV DIASVNRLRK LRKEENEGLI SGSEYIARLR AHHAKLNPGT
DWARPDSQIV DGESSDDDDT QDGGVDDILR TNEDLVVKSR GNKLCAGRLE YSKLVDANAA
DPSNGPINSV HFHQNAQLLL TAGLDRRLRF FQIDGKRNTK IQSIFLEDCP IRKAAFLPNG
SQVIVSGRRK FFYSFDLEKA KFDKIGPLVG REEKSLEYFE VSQDSNTIAF VGNEGYILLV
STKTKELIGT LKMNGSVRSL AFSEDGKHLL SSGGDGQVYV WDLRTMKCLY KGVDEGSTCG
TSLCSSLNGA LFASGTDRGI VNIYKKSEFV GGKRKPIKTV DNLTSKIDFM KFNHDAQILA
IVSTMNKNSV KLVHVPSLTV FSNWPPPNST MHYPRCLDFS PGSGFMAMGN AAGKVLLYKL
HHYQNA
