UTP18_DROME
ID UTP18_DROME Reviewed; 506 AA.
AC Q9V7P1;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=U3 small nucleolar RNA-associated protein 18 homolog;
DE AltName: Full=Protein wicked;
DE AltName: Full=WD repeat protein l(2)k07824;
GN Name=wcd; Synonyms=l(2)k07824; ORFNames=CG7989;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-104; SER-164 AND
RP SER-165, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19430468; DOI=10.1038/ncb1874;
RA Fichelson P., Moch C., Ivanovitch K., Martin C., Sidor C.M., Lepesant J.A.,
RA Bellaiche Y., Huynh J.R.;
RT "Live-imaging of single stem cells within their niche reveals that a
RT U3snoRNP component segregates asymmetrically and is required for self-
RT renewal in Drosophila.";
RL Nat. Cell Biol. 11:685-693(2009).
CC -!- FUNCTION: Component of a nucleolar small nuclear ribonucleoprotein
CC particle (snoRNP) thought to participate in the processing and
CC modification of pre-ribosomal RNA. Regulation of cell size by ribosome
CC synthesis is an important parameter for stem cell maintenance and
CC function. {ECO:0000269|PubMed:19430468}.
CC -!- SUBUNIT: Component of U3 snoRNP complex. {ECO:0000269|PubMed:19430468}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19430468}.
CC Note=Asymmetric segregation of expression upon mitosis both in germline
CC stem cells (GSCs) and dividing larval neural stem cells (NSCs) (at
CC protein level).
CC -!- DISRUPTION PHENOTYPE: Induces premature differentiation of germline
CC stem cells (GSCs). {ECO:0000269|PubMed:19430468}.
CC -!- SIMILARITY: Belongs to the WD repeat UTP18 family. {ECO:0000305}.
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DR EMBL; AE013599; AAF58006.1; -; Genomic_DNA.
DR EMBL; AY119590; AAM50244.1; -; mRNA.
DR RefSeq; NP_611121.1; NM_137277.4.
DR AlphaFoldDB; Q9V7P1; -.
DR SMR; Q9V7P1; -.
DR BioGRID; 62547; 7.
DR DIP; DIP-23848N; -.
DR IntAct; Q9V7P1; 1.
DR STRING; 7227.FBpp0086314; -.
DR iPTMnet; Q9V7P1; -.
DR PaxDb; Q9V7P1; -.
DR PRIDE; Q9V7P1; -.
DR DNASU; 36831; -.
DR EnsemblMetazoa; FBtr0087170; FBpp0086314; FBgn0262560.
DR GeneID; 36831; -.
DR KEGG; dme:Dmel_CG7989; -.
DR CTD; 36831; -.
DR FlyBase; FBgn0262560; wcd.
DR VEuPathDB; VectorBase:FBgn0262560; -.
DR eggNOG; KOG2055; Eukaryota.
DR GeneTree; ENSGT00940000165670; -.
DR HOGENOM; CLU_011055_3_0_1; -.
DR InParanoid; Q9V7P1; -.
DR OMA; QFHPTST; -.
DR OrthoDB; 462558at2759; -.
DR PhylomeDB; Q9V7P1; -.
DR Reactome; R-DME-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 36831; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36831; -.
DR PRO; PR:Q9V7P1; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0262560; Expressed in eye disc (Drosophila) and 39 other tissues.
DR Genevisible; Q9V7P1; DM.
DR GO; GO:0042585; C:germinal vesicle; IDA:FlyBase.
DR GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0034388; C:Pwp2p-containing subcomplex of 90S preribosome; IBA:GO_Central.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IPI:FlyBase.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0048132; P:female germ-line stem cell asymmetric division; IMP:FlyBase.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:FlyBase.
DR GO; GO:0006364; P:rRNA processing; IMP:FlyBase.
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; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR18359; PTHR18359; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW rRNA processing; WD repeat.
FT CHAIN 1..506
FT /note="U3 small nucleolar RNA-associated protein 18
FT homolog"
FT /id="PRO_0000051409"
FT REPEAT 203..242
FT /note="WD 1"
FT REPEAT 331..370
FT /note="WD 2"
FT REPEAT 372..413
FT /note="WD 3"
FT REPEAT 469..505
FT /note="WD 4"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 506 AA; 56947 MW; 9E2C4A10FA21E5B1 CRC64;
MSSDESSDGL EELQSLKALY GQQEQEKPAK IKRERYIPKA SQAKELNYVE VPMEKVLFGD
RQRLLTNLAK SVGQKLPNDD EDEQEENPGQ AKPGDKRKAA WSDSDDEDLQ VGDVKKATKH
TGPLNHLRKD KSYKEYLTAR FQRTLNQPKW AEKKVKNEDD EDVSSDEELL RTVGFIDRKA
RNSDLPQKTL NFKRVKDLNR ATYAEGNATS IQFHPTSTAA LVAGMNGLAT IYAVDGQKNE
RLHNMRFKKF PLACSRIAPC GTRAFFGSVK PFYYSYDLLE AKESKLKLPG AMEFMHRFEV
SPCGKFIVTA GKFGAIHLLT AKTNELLHSF KQEGKVKGFT WSSDSKRILV CGSTSNVSVL
NLRQNLIEHI FMDDGCIHGE SIQLSPNQRL LATGSQEGVV NIYDYESIFA SKAPQPEKRF
MNLRTAITDL QFNHSSELLA MCSSEAPNAF KLAHFPSATV YSNFPAQNEK VGFVTSMAFS
PHSSFLAFAT KGKQVPLFRL KYFKGY
