ID RLA2_DROME Reviewed; 113 AA.
AC P05389; A4UZK7; Q8MRV1; Q9V7R6;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 27-MAR-2024, entry version 171.
DE RecName: Full=Large ribosomal subunit protein P2 {ECO:0000305};
DE AltName: Full=60S acidic ribosomal protein P2;
DE AltName: Full=Acidic ribosomal protein RPA1;
GN Name=RpLP2; Synonyms=rpA1, RpP1; ORFNames=CG4918;
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 / MRNA].
RC STRAIN=Canton-S, and Oregon-R;
RX PubMed=3103101; DOI=10.1093/nar/15.3.987;
RA Qian S., Zhang J.-Y., Kay M.A., Jacobs-Lorena M.;
RT "Structural analysis of the Drosophila rpA1 gene, a member of the
RT eucaryotic 'A' type ribosomal protein family.";
RL Nucleic Acids Res. 15:987-1003(1987).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100 AND SER-102, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Plays an important role in the elongation step of protein
CC synthesis.
CC -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC {ECO:0000305}.
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DR EMBL; X05016; CAA28672.1; -; Genomic_DNA.
DR EMBL; X05466; CAA29026.1; -; mRNA.
DR EMBL; AE013599; AAF57979.1; -; Genomic_DNA.
DR EMBL; AY119253; AAM51113.1; -; mRNA.
DR PIR; A26401; R6FFP2.
DR RefSeq; NP_523764.1; NM_079040.4.
DR AlphaFoldDB; P05389; -.
DR SMR; P05389; -.
DR BioGRID; 62568; 107.
DR DIP; DIP-19859N; -.
DR IntAct; P05389; 11.
DR STRING; 7227.FBpp0086252; -.
DR iPTMnet; P05389; -.
DR PaxDb; 7227-FBpp0089424; -.
DR DNASU; 36855; -.
DR EnsemblMetazoa; FBtr0087105; FBpp0086252; FBgn0003274.
DR GeneID; 36855; -.
DR KEGG; dme:Dmel_CG4918; -.
DR AGR; FB:FBgn0003274; -.
DR CTD; 6181; -.
DR FlyBase; FBgn0003274; RpLP2.
DR VEuPathDB; VectorBase:FBgn0003274; -.
DR eggNOG; KOG3449; Eukaryota.
DR GeneTree; ENSGT00550000074828; -.
DR HOGENOM; CLU_114656_0_2_1; -.
DR InParanoid; P05389; -.
DR OMA; NIEDVIC; -.
DR OrthoDB; 5485067at2759; -.
DR PhylomeDB; P05389; -.
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; P05389; -.
DR BioGRID-ORCS; 36855; 0 hits in 1 CRISPR screen.
DR ChiTaRS; RpLP2; fly.
DR GenomeRNAi; 36855; -.
DR PRO; PR:P05389; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003274; Expressed in mouthpart and 23 other cell types or tissues.
DR ExpressionAtlas; P05389; baseline and differential.
DR Genevisible; P05389; DM.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; TAS:FlyBase.
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 GO; GO:0002182; P:cytoplasmic translational elongation; IEA:InterPro.
DR CDD; cd05833; Ribosomal_P2; 1.
DR Gene3D; 1.10.10.1410; -; 1.
DR HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR InterPro; IPR038716; P1/P2_N_sf.
DR InterPro; IPR027534; Ribosomal_P1/P2.
DR InterPro; IPR044076; Ribosomal_P2.
DR PANTHER; PTHR21141; 60S ACIDIC RIBOSOMAL PROTEIN FAMILY MEMBER; 1.
DR PANTHER; PTHR21141:SF5; 60S ACIDIC RIBOSOMAL PROTEIN P2; 1.
DR Pfam; PF00428; Ribosomal_60s; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..113
FT /note="Large ribosomal subunit protein P2"
FT /id="PRO_0000157652"
FT REGION 66..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 21
FT /note="S -> G (in Ref. 1; CAA29026 and 4; AAM51113)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="A -> V (in Ref. 4; AAM51113)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 113 AA; 11757 MW; DDA5F5A4219BD65A CRC64;
MRYVAAYLLA VLGGKDSPAN SDLEKILSSV GVEVDAERLT KVIKELAGKS IDDLIKEGRE
KLSSMPVGGG GAVAAADAAP AAAAGGDKKE AKKEEKKEES ESEDDDMGFA LFE
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