RL27A_DROME
ID RL27A_DROME Reviewed; 149 AA.
AC P41092; Q94530; Q9VR02;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=60S ribosomal protein L27a;
GN Name=RpL27A; Synonyms=RpL27a2, RpL27Aa, RpL27Ab; ORFNames=CG15442;
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=Canton-S; TISSUE=Larva;
RX PubMed=8297386; DOI=10.1006/bbrc.1994.1108;
RA Garwood J., Lepesant J.-A.;
RT "The Drosophila melanogaster homolog of ribosomal protein L27a.";
RL Biochem. Biophys. Res. Commun. 198:748-754(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Canton-S; TISSUE=Eye imaginal disk;
RX PubMed=9055824; DOI=10.1016/s0378-1119(96)00656-7;
RA Soehnge H., Huang X., Becker M., Conover D., Stern M.;
RT "Cloning and sequencing of ribosomal protein L27a and a gene similar to
RT human GS1 in Drosophila.";
RL Gene 185:257-263(1997).
RN [3]
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 [4]
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 [5]
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 [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 -!- SIMILARITY: Belongs to the universal ribosomal protein uL15 family.
CC {ECO:0000305}.
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DR EMBL; X74484; CAA52601.1; -; mRNA.
DR EMBL; U66357; AAC47475.1; -; Genomic_DNA.
DR EMBL; U66358; AAC47472.1; -; mRNA.
DR EMBL; AE014134; AAF51006.3; -; Genomic_DNA.
DR EMBL; AY071144; AAL48766.1; -; mRNA.
DR PIR; JC2392; JC2392.
DR PIR; JC6202; JC6202.
DR RefSeq; NP_001188689.2; NM_001201760.2.
DR RefSeq; NP_001285601.1; NM_001298672.1.
DR RefSeq; NP_476963.1; NM_057615.6.
DR PDB; 4V6W; EM; 6.00 A; Ca=1-149.
DR PDB; 6XU6; EM; 3.50 A; Ca=1-149.
DR PDB; 6XU7; EM; 4.90 A; Ca=1-149.
DR PDB; 6XU8; EM; 3.00 A; Ca=1-149.
DR PDBsum; 4V6W; -.
DR PDBsum; 6XU6; -.
DR PDBsum; 6XU7; -.
DR PDBsum; 6XU8; -.
DR AlphaFoldDB; P41092; -.
DR SMR; P41092; -.
DR BioGRID; 59848; 89.
DR DIP; DIP-18398N; -.
DR IntAct; P41092; 8.
DR STRING; 7227.FBpp0077142; -.
DR PaxDb; P41092; -.
DR PRIDE; P41092; -.
DR DNASU; 33654; -.
DR EnsemblMetazoa; FBtr0077452; FBpp0077142; FBgn0285948.
DR EnsemblMetazoa; FBtr0335136; FBpp0307135; FBgn0285948.
DR EnsemblMetazoa; FBtr0345285; FBpp0311452; FBgn0285948.
DR GeneID; 33654; -.
DR KEGG; dme:Dmel_CG15442; -.
DR CTD; 6157; -.
DR FlyBase; FBgn0285948; RpL27A.
DR VEuPathDB; VectorBase:FBgn0285948; -.
DR eggNOG; KOG1742; Eukaryota.
DR GeneTree; ENSGT00390000005534; -.
DR HOGENOM; CLU_109163_1_0_1; -.
DR InParanoid; P41092; -.
DR OMA; WGRVGQH; -.
DR OrthoDB; 1445443at2759; -.
DR PhylomeDB; P41092; -.
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; P41092; -.
DR BioGRID-ORCS; 33654; 1 hit in 1 CRISPR screen.
DR ChiTaRS; RpL27A; fly.
DR GenomeRNAi; 33654; -.
DR PRO; PR:P41092; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0285948; Expressed in seminal fluid secreting gland and 12 other tissues.
DR ExpressionAtlas; P41092; baseline and differential.
DR Genevisible; P41092; 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:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; TAS:FlyBase.
DR HAMAP; MF_01341; Ribosomal_L15; 1.
DR InterPro; IPR036227; L18e/L15P_sf.
DR InterPro; IPR030878; Ribosomal_L15.
DR InterPro; IPR001196; Ribosomal_L15_CS.
DR InterPro; IPR021131; Ribosomal_L18e/L15P.
DR Pfam; PF00828; Ribosomal_L27A; 1.
DR SUPFAM; SSF52080; SSF52080; 1.
DR PROSITE; PS00475; RIBOSOMAL_L15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..149
FT /note="60S ribosomal protein L27a"
FT /id="PRO_0000104886"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 2
FT /note="S -> R (in Ref. 1; CAA52601)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="A -> L (in Ref. 1; CAA52601)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="K -> E (in Ref. 1; CAA52601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 149 AA; 17022 MW; 7777397307B89DCC CRC64;
MSNIKRKKTR KLRGHVSHGH GRIGKHRKHP GGRGNAGGMH HHRINFDKYH PGYFGKVGMR
NFHLRRQHKF RPEINLDKLW SLVGAEKFAE LEKEKSTKAP VIDLVKFGYY KLLGRGHLPA
RPVIVKAKYF SKKAEDKIKK AGGVCLLSA
