Q9VPU8 (KRR1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
KRR1 small subunit processome component homolog

Alternative name(s):
KRR-R motif-containing protein 1
Protein dribble

Gene names

Name:	dbe
Synonyms:	dribble
ORF Names:	CG4258

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Binds to RNA. Required for female germline development, cell viability during eye development and for survival of dividing cells and epithelial cells during early wing disk development. Ref.1 Ref.5
Subunit structure	Monomer. Component of the ribosomal small subunit (SSU) processome. Ref.5
Subcellular location	Nucleus › nucleolus. Note: Exogenous expression in embryos shows a predominant localization in nucleoplasm in some epidermal cells while most other cells show perinucleolar ring structure. In heat-shocked third instar larvae, localization varies among cells. In gut cells, some show localization in both nucleoplasm and nucleolus while in others localization is restricted to the center of the fibrillarin-positive part of the nucleolus, in the fibrillar center, where rRNA transcription occurs. On ectopic expression, a nuclear engrailed pattern is observed in embryonic epidermal cells. Ref.1
Developmental stage	Expression is detected in nurse cells during oogenesis throughout stage 10A and persists through stage 14 with some expression in the anterior part of the oocyte. Expression is ubiquitously detected at all stages of embryogenesis. Observed in salivary gland cells from heat shocked transgenic third instar larvae. Ref.1
Disruption phenotype	Homozygous mutant larvae show arrested development at the first instar stage as they fail to increase in size or develop into the second instar larval stage and die 2-3 days after hatching, without morphological defect. Mutant larvae show an overall reduction of most intermediate and mature rRNA as a consequence of abnormal pre-rRNA processing. Mutants show defects in rRNA processing and aberrant pre-rRNA species. An abnormal cleavage in the 3'-end of the pre-rRNA occurs within the presumptive 28S rRNA but it does not lead to accumulation of a truncated 28S rRNA. Ref.1
Sequence similarities	Belongs to the KRR1 family. Contains 1 KH domain.
Sequence caution	The sequence CAB09659.1 differs from that shown. Reason: Frameshift at positions 268, 269, 271 and 272.

Ontologies

Keywords
Biological process	Ribosome biogenesis rRNA processing
Cellular component	Nucleus
Domain	Coiled coil
Ligand	RNA-binding
Molecular function	Developmental protein Ribonucleoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW rRNA processing Inferred from mutant phenotype Ref.1. Source: FlyBase
Cellular_component	nucleolus Inferred from direct assay Ref.1. Source: FlyBase nucleoplasm Inferred from direct assay Ref.1. Source: FlyBase ribonucleoprotein complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 345	345	KRR1 small subunit processome component homolog		PRO_0000415500
Regions
	Domain	125 – 193	69	KH
	Coiled coil	270 – 298	29

Sequences

	Sequence		Length	Mass (Da)
	Q9VPU8 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 8EA77B47F712FF34	FASTA	345	39,843
	10 20 30 40 50 60 MSESEAEETK ISTEPVDNAW SMKIPAFRQE DNPHGMVEES SFATLFPKYR ERYLKEVWPL 70 80 90 100 110 120 VEQCLAEHHL KAELDLMEGS MVVKTSRKTW DPYIIIKARD MIKLMARSVP FEQAKRVLQD 130 140 150 160 170 180 DIGCDIIKIG NLVHKKEKFV KRRQRLIGPN GATLKSIELL TDCYVLVQGN TVSALGPYKG 190 200 210 220 230 240 LQQVRDIVLE TMNNVHPIYN IKALMIKREL MKDPRLANED WSRFLPKFKN KNISKRKQPK 250 260 270 280 290 300 VKKQKKEYTP FPPSQPESKV DKQLASGEYF LNQEQKQAKR NQERTEKQKE AAKRQDERRN 310 320 330 340 KDFVPPTEES AASSRKKEDG SSSSKVDVKA LKAKLIKANK KARSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Dribble, the Drosophila KRR1p homologue, is involved in rRNA processing." Chan H.Y., Brogna S., O'Kane C.J. Mol. Biol. Cell 12:1409-1419(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"Biophysical characterisation reveals structural disorder in the nucleolar protein, Dribble." Yiu C.P., Beavil R.L., Chan H.Y. Biochem. Biophys. Res. Commun. 343:311-318(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z96931 Genomic DNA. Translation: CAB09659.1. Frameshift. AE014134 Genomic DNA. Translation: AAF51440.1. AY069529 mRNA. Translation: AAL39674.1.
RefSeq	NP_477240.1. NM_057892.4.
UniGene	Dm.2087.
3D structure databases
ProteinModelPortal	Q9VPU8.
SMR	Q9VPU8. Positions 43-201.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VPU8. 1 interaction.
MINT	MINT-1588813.
STRING	7227.FBpp0077694.
Proteomic databases
PRIDE	Q9VPU8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0078030; FBpp0077694; FBgn0020305.
GeneID	33269.
KEGG	dme:Dmel_CG4258.
UCSC	CG4258-RA. d. melanogaster.
Organism-specific databases
CTD	33269.
FlyBase	FBgn0020305. dbe.
Phylogenomic databases
eggNOG	COG1094.
GeneTree	ENSGT00390000018775.
InParanoid	Q9VPU8.
KO	K06961.
OMA	ALMIKRE.
PhylomeDB	Q9VPU8.
Gene expression databases
Bgee	Q9VPU8.
Family and domain databases
InterPro	IPR004087. KH_dom. IPR024166. rRNA_assembly_KRR1. [Graphical view]
PANTHER	PTHR12581. PTHR12581. 1 hit.
PIRSF	PIRSF006515. KRR1. 1 hit.
SMART	SM00322. KH. 1 hit. [Graphical view]
PROSITE	PS50084. KH_TYPE_1. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	33269.
NextBio	782766.

Entry information

Entry name

KRR1_DROME

Accession

Primary (citable) accession number: Q9VPU8
Secondary accession number(s): O02394

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 22, 2012
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project