RL11_DROME
ID RL11_DROME Reviewed; 184 AA.
AC P46222; Q9V8U9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=60S ribosomal protein L11;
GN Name=RpL11; Synonyms=RPL11A; ORFNames=CG7726;
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 [MRNA].
RC STRAIN=Oregon-R;
RX PubMed=7893752; DOI=10.1016/0167-4781(95)00010-e;
RA Larochelle S., Suter B.;
RT "Molecular cloning of the Drosophila homologue of the rat ribosomal protein
RT L11 gene.";
RL Biochim. Biophys. Acta 1261:147-150(1995).
RN [2]
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 [3]
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]
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 [5]
RP INTERACTION WITH FMR1.
RX PubMed=12368261; DOI=10.1101/gad.1022002;
RA Ishizuka A., Siomi M.C., Siomi H.;
RT "A Drosophila fragile X protein interacts with components of RNAi and
RT ribosomal proteins.";
RL Genes Dev. 16:2497-2508(2002).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. {ECO:0000250|UniProtKB:P0C0W9}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (By similarity).
CC Interacts with Fmr1 to form the RNA-induced silencing complex (RISC), a
CC ribonucleoprotein (RNP) complex involved in translation regulation,
CC other components of the complex are RpL5, Rm62, AGO2 and Dcr-1
CC (PubMed:12368261). {ECO:0000250|UniProtKB:P0C0W9,
CC ECO:0000269|PubMed:12368261}.
CC -!- INTERACTION:
CC P46222; Q9NFU0: Fmr1; NbExp=5; IntAct=EBI-183104, EBI-422631;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C0W9}. Cytoplasm
CC {ECO:0000250|UniProtKB:P0C0W9}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000305}.
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DR EMBL; U15643; AAC46585.1; -; mRNA.
DR EMBL; AE013599; AAF57560.1; -; Genomic_DNA.
DR EMBL; AY094790; AAM11143.1; -; mRNA.
DR PIR; S60245; S60245.
DR RefSeq; NP_001286614.1; NM_001299685.1.
DR RefSeq; NP_477054.1; NM_057706.5.
DR PDB; 4V6W; EM; 6.00 A; CJ=1-184.
DR PDB; 6XU6; EM; 3.50 A; CJ=1-182.
DR PDB; 6XU7; EM; 4.90 A; CJ=1-182.
DR PDB; 6XU8; EM; 3.00 A; CJ=1-182.
DR PDBsum; 4V6W; -.
DR PDBsum; 6XU6; -.
DR PDBsum; 6XU7; -.
DR PDBsum; 6XU8; -.
DR AlphaFoldDB; P46222; -.
DR SMR; P46222; -.
DR BioGRID; 62897; 94.
DR DIP; DIP-18297N; -.
DR IntAct; P46222; 4.
DR MINT; P46222; -.
DR STRING; 7227.FBpp0085717; -.
DR PaxDb; P46222; -.
DR PRIDE; P46222; -.
DR DNASU; 37235; -.
DR EnsemblMetazoa; FBtr0086533; FBpp0085717; FBgn0013325.
DR EnsemblMetazoa; FBtr0340533; FBpp0309436; FBgn0013325.
DR GeneID; 37235; -.
DR KEGG; dme:Dmel_CG7726; -.
DR CTD; 6135; -.
DR FlyBase; FBgn0013325; RpL11.
DR VEuPathDB; VectorBase:FBgn0013325; -.
DR eggNOG; KOG0397; Eukaryota.
DR GeneTree; ENSGT00910000144211; -.
DR HOGENOM; CLU_061015_3_0_1; -.
DR InParanoid; P46222; -.
DR OMA; QTETIKW; -.
DR OrthoDB; 1340833at2759; -.
DR PhylomeDB; P46222; -.
DR Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DME-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-DME-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DME-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-DME-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DME-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P46222; -.
DR BioGRID-ORCS; 37235; 0 hits in 1 CRISPR screen.
DR ChiTaRS; RpL11; fly.
DR GenomeRNAi; 37235; -.
DR PRO; PR:P46222; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0013325; Expressed in seminal fluid secreting gland and 12 other tissues.
DR ExpressionAtlas; P46222; baseline and differential.
DR Genevisible; P46222; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; TAS:FlyBase.
DR Gene3D; 3.30.1440.10; -; 1.
DR InterPro; IPR002132; Ribosomal_L5.
DR InterPro; IPR031309; Ribosomal_L5_C.
DR InterPro; IPR020929; Ribosomal_L5_CS.
DR InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR InterPro; IPR031310; Ribosomal_L5_N.
DR PANTHER; PTHR11994; PTHR11994; 1.
DR Pfam; PF00281; Ribosomal_L5; 1.
DR Pfam; PF00673; Ribosomal_L5_C; 1.
DR PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR SUPFAM; SSF55282; SSF55282; 1.
DR PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..184
FT /note="60S ribosomal protein L11"
FT /id="PRO_0000125089"
FT CONFLICT 14..18
FT /note="KNPMR -> QEPDE (in Ref. 1; AAC46585)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 184 AA; 21112 MW; E64EF5568A530C09 CRC64;
MAAVTKKIKR DPAKNPMRDL HIRKLCLNIC VGESGDRLTR AAKVLEQLTG QQPVFSKARY
TVRSFGIRRN EKIAVHCTVR GAKAEEILER GLKVREYELR RENFSSTGNF GFGIQEHIDL
GIKYDPSIGI YGLDFYVVLG RPGYNVNHRK RKSGTVGFQH RLTKEDAMKW FQQKYDGIIL
NTKK
