RL13_DROME
ID RL13_DROME Reviewed; 218 AA.
AC P41126; A4V0I6; B7FNN5; Q9VL55;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=60S ribosomal protein L13;
DE AltName: Full=BBC1 protein homolog;
GN Name=RpL13; Synonyms=bbc1; ORFNames=CG4651;
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 [GENOMIC DNA].
RC STRAIN=Brighton; TISSUE=Embryo;
RX PubMed=7557437; DOI=10.1016/0378-1119(95)00356-b;
RA Helps N.R., Adams S.M., Brammar W.J., Varley J.M.;
RT "The Drosophila melanogaster homologue of the human BBC1 gene is highly
RT expressed during embryogenesis.";
RL Gene 162:245-248(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;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME,
RP FUNCTION, AND SUBCELLULAR LOCATION.
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
CC (PubMed:23636399). The small ribosomal subunit (SSU) binds messenger
CC RNAs (mRNAs) and translates the encoded message by selecting cognate
CC aminoacyl-transfer RNA (tRNA) molecules (Probable). The large subunit
CC (LSU) contains the ribosomal catalytic site termed the peptidyl
CC transferase center (PTC), which catalyzes the formation of peptide
CC bonds, thereby polymerizing the amino acids delivered by tRNAs into a
CC polypeptide chain (Probable). The nascent polypeptides leave the
CC ribosome through a tunnel in the LSU and interact with protein factors
CC that function in enzymatic processing, targeting, and the membrane
CC insertion of nascent chains at the exit of the ribosomal tunnel
CC (Probable). As part of the LSU, it is probably required for its
CC formation and the maturation of rRNAs (Probable).
CC {ECO:0000269|PubMed:23636399, ECO:0000305,
CC ECO:0000305|PubMed:23636399}.
CC -!- SUBUNIT: Component of the 60S large ribosomal subunit (LSU).
CC {ECO:0000305|PubMed:23636399}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23636399}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL13 family.
CC {ECO:0000305}.
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DR EMBL; X77926; CAA54898.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52842.1; -; Genomic_DNA.
DR EMBL; AE014134; ABC65888.1; -; Genomic_DNA.
DR EMBL; BT053725; ACK77643.1; -; mRNA.
DR EMBL; BT128812; AEM72508.1; -; mRNA.
DR PIR; JC4260; JC4260.
DR PIR; S42877; S42877.
DR RefSeq; NP_001033891.1; NM_001038802.2.
DR RefSeq; NP_001260312.1; NM_001273383.2.
DR RefSeq; NP_523530.1; NM_078806.4.
DR PDB; 4V6W; EM; 6.00 A; CL=1-218.
DR PDB; 6XU6; EM; 3.50 A; CL=2-211.
DR PDB; 6XU7; EM; 4.90 A; CL=2-211.
DR PDB; 6XU8; EM; 3.00 A; CL=2-211.
DR PDBsum; 4V6W; -.
DR PDBsum; 6XU6; -.
DR PDBsum; 6XU7; -.
DR PDBsum; 6XU8; -.
DR AlphaFoldDB; P41126; -.
DR SMR; P41126; -.
DR BioGRID; 60423; 105.
DR DIP; DIP-19420N; -.
DR IntAct; P41126; 2.
DR MINT; P41126; -.
DR STRING; 7227.FBpp0079484; -.
DR PaxDb; P41126; -.
DR PRIDE; P41126; -.
DR DNASU; 34329; -.
DR EnsemblMetazoa; FBtr0079888; FBpp0079484; FBgn0011272.
DR EnsemblMetazoa; FBtr0100164; FBpp0099517; FBgn0011272.
DR EnsemblMetazoa; FBtr0310482; FBpp0302626; FBgn0011272.
DR GeneID; 34329; -.
DR KEGG; dme:Dmel_CG4651; -.
DR CTD; 6137; -.
DR FlyBase; FBgn0011272; RpL13.
DR VEuPathDB; VectorBase:FBgn0011272; -.
DR eggNOG; KOG3295; Eukaryota.
DR GeneTree; ENSGT00390000007818; -.
DR HOGENOM; CLU_075696_1_0_1; -.
DR InParanoid; P41126; -.
DR OMA; NQQIPHN; -.
DR OrthoDB; 1239434at2759; -.
DR PhylomeDB; P41126; -.
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 BioGRID-ORCS; 34329; 1 hit in 1 CRISPR screen.
DR ChiTaRS; RpL13; fly.
DR GenomeRNAi; 34329; -.
DR PRO; PR:P41126; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0011272; Expressed in eye disc (Drosophila) and 23 other tissues.
DR ExpressionAtlas; P41126; baseline and differential.
DR Genevisible; P41126; DM.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; TAS:FlyBase.
DR HAMAP; MF_00499; Ribosomal_L13e; 1.
DR InterPro; IPR001380; Ribosomal_L13e.
DR InterPro; IPR018256; Ribosomal_L13e_CS.
DR PANTHER; PTHR11722; PTHR11722; 1.
DR Pfam; PF01294; Ribosomal_L13e; 1.
DR PROSITE; PS01104; RIBOSOMAL_L13E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..218
FT /note="60S ribosomal protein L13"
FT /id="PRO_0000192925"
FT REGION 196..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 218 AA; 24951 MW; 2DBCF34B2E650A63 CRC64;
MGKGNNMIPN QHYHKWWQRH VKTWFNQPAR KVRRHANRVK KAKAVFPRPA SGALRPVVRC
PTIRYHTKLR AGRGFTLEEL KGAGIGANFA KTIGIAVDRR RKNKSLESRQ RNIQRLKEYR
SKLILFPINE KKIRAGESSL EECKLATQLK GPVLPIKNEQ PAVVEFREVT KDEKKFKAFA
TLRKARTDAR LVGIRAKRAK EAAESEDAAK GDPKKAKK
