KRR1_DROME
ID KRR1_DROME Reviewed; 345 AA.
AC Q9VPU8; O02394;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=KRR1 small subunit processome component homolog {ECO:0000250|UniProtKB:Q8BGA5};
DE AltName: Full=KRR-R motif-containing protein 1 {ECO:0000250|UniProtKB:Q8BGA5};
DE AltName: Full=Protein dribble {ECO:0000312|EMBL:AAF51440.1};
GN Name=dbe;
GN Synonyms=dribble {ECO:0000303|PubMed:11359931,
GN ECO:0000312|EMBL:CAB09659.1}; ORFNames=CG4258;
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] {ECO:0000305, ECO:0000312|EMBL:CAB09659.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11359931; DOI=10.1091/mbc.12.5.1409;
RA Chan H.Y., Brogna S., O'Kane C.J.;
RT "Dribble, the Drosophila KRR1p homologue, is involved in rRNA processing.";
RL Mol. Biol. Cell 12:1409-1419(2001).
RN [2] {ECO:0000312|EMBL:AAF51440.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [3] {ECO:0000312|EMBL:AAF51440.1}
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 [4] {ECO:0000312|EMBL:AAL39674.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16542639; DOI=10.1016/j.bbrc.2006.02.153;
RA Yiu C.P., Beavil R.L., Chan H.Y.;
RT "Biophysical characterisation reveals structural disorder in the nucleolar
RT protein, Dribble.";
RL Biochem. Biophys. Res. Commun. 343:311-318(2006).
CC -!- FUNCTION: Required for 40S ribosome biogenesis. Involved in nucleolar
CC processing of pre-18S ribosomal RNA and ribosome assembly. Binds to
CC RNA. Required for female germline development, cell viability during
CC eye development and for survival of dividing cells and epithelial cells
CC during early wing disk development. {ECO:0000269|PubMed:11359931,
CC ECO:0000269|PubMed:16542639}.
CC -!- SUBUNIT: Monomer. Component of the ribosomal small subunit (SSU)
CC processome. {ECO:0000269|PubMed:16542639}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11359931}.
CC Note=Exogenous expression in embryos shows a predominant localization
CC in nucleoplasm in some epidermal cells while most other cells show
CC perinucleolar ring structure. In heat-shocked third instar larvae,
CC localization varies among cells. In gut cells, some show localization
CC in both nucleoplasm and nucleolus while in others localization is
CC restricted to the center of the fibrillarin-positive part of the
CC nucleolus, in the fibrillar center, where rRNA transcription occurs. On
CC ectopic expression, a nuclear engrailed pattern is observed in
CC embryonic epidermal cells. {ECO:0000269|PubMed:11359931}.
CC -!- DEVELOPMENTAL STAGE: Expression is detected in nurse cells during
CC oogenesis throughout stage 10A and persists through stage 14 with some
CC expression in the anterior part of the oocyte. Expression is
CC ubiquitously detected at all stages of embryogenesis. Observed in
CC salivary gland cells from heat shocked transgenic third instar larvae.
CC {ECO:0000269|PubMed:11359931}.
CC -!- DISRUPTION PHENOTYPE: Homozygous mutant larvae show arrested
CC development at the first instar stage as they fail to increase in size
CC or develop into the second instar larval stage and die 2-3 days after
CC hatching, without morphological defect. Mutant larvae show an overall
CC reduction of most intermediate and mature rRNA as a consequence of
CC abnormal pre-rRNA processing. Mutants show defects in rRNA processing
CC and aberrant pre-rRNA species. An abnormal cleavage in the 3'-end of
CC the pre-rRNA occurs within the presumptive 28S rRNA but it does not
CC lead to accumulation of a truncated 28S rRNA.
CC {ECO:0000269|PubMed:11359931}.
CC -!- SIMILARITY: Belongs to the KRR1 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB09659.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z96931; CAB09659.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE014134; AAF51440.1; -; Genomic_DNA.
DR EMBL; AY069529; AAL39674.1; -; mRNA.
DR RefSeq; NP_477240.1; NM_057892.4.
DR AlphaFoldDB; Q9VPU8; -.
DR SMR; Q9VPU8; -.
DR BioGRID; 59523; 7.
DR IntAct; Q9VPU8; 1.
DR STRING; 7227.FBpp0077694; -.
DR PaxDb; Q9VPU8; -.
DR PRIDE; Q9VPU8; -.
DR DNASU; 33269; -.
DR EnsemblMetazoa; FBtr0078030; FBpp0077694; FBgn0020305.
DR GeneID; 33269; -.
DR KEGG; dme:Dmel_CG4258; -.
DR UCSC; CG4258-RA; d. melanogaster.
DR CTD; 33269; -.
DR FlyBase; FBgn0020305; dbe.
DR VEuPathDB; VectorBase:FBgn0020305; -.
DR eggNOG; KOG2874; Eukaryota.
DR GeneTree; ENSGT00390000018775; -.
DR HOGENOM; CLU_040185_0_2_1; -.
DR InParanoid; Q9VPU8; -.
DR OMA; HKKEKFV; -.
DR OrthoDB; 944899at2759; -.
DR PhylomeDB; Q9VPU8; -.
DR Reactome; R-DME-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 33269; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33269; -.
DR PRO; PR:Q9VPU8; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0020305; Expressed in cleaving embryo and 40 other tissues.
DR Genevisible; Q9VPU8; DM.
DR GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:CAFA.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:CAFA.
DR GO; GO:0006364; P:rRNA processing; IMP:FlyBase.
DR DisProt; DP00540; -.
DR Gene3D; 3.30.1370.10; -; 2.
DR InterPro; IPR041174; KH_8.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR024166; rRNA_assembly_KRR1.
DR PANTHER; PTHR12581; PTHR12581; 1.
DR Pfam; PF17903; KH_8; 1.
DR PIRSF; PIRSF006515; KRR1; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Developmental protein; Nucleus; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..345
FT /note="KRR1 small subunit processome component homolog"
FT /id="PRO_0000415500"
FT DOMAIN 125..193
FT /note="KH"
FT /evidence="ECO:0000255"
FT REGION 232..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 270..298
FT /evidence="ECO:0000255, ECO:0000269|PubMed:16542639"
FT COMPBIAS 277..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 39843 MW; 8EA77B47F712FF34 CRC64;
MSESEAEETK ISTEPVDNAW SMKIPAFRQE DNPHGMVEES SFATLFPKYR ERYLKEVWPL
VEQCLAEHHL KAELDLMEGS MVVKTSRKTW DPYIIIKARD MIKLMARSVP FEQAKRVLQD
DIGCDIIKIG NLVHKKEKFV KRRQRLIGPN GATLKSIELL TDCYVLVQGN TVSALGPYKG
LQQVRDIVLE TMNNVHPIYN IKALMIKREL MKDPRLANED WSRFLPKFKN KNISKRKQPK
VKKQKKEYTP FPPSQPESKV DKQLASGEYF LNQEQKQAKR NQERTEKQKE AAKRQDERRN
KDFVPPTEES AASSRKKEDG SSSSKVDVKA LKAKLIKANK KARSS
