RLA0_DROME
ID RLA0_DROME Reviewed; 317 AA.
AC P19889; Q5BHX7; Q9VNV9;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=60S acidic ribosomal protein P0;
DE AltName: Full=Apurinic-apyrimidinic endonuclease;
DE EC=3.1.-.- {ECO:0000269|PubMed:8932386};
GN Name=RpLP0; Synonyms=AP3, Ape, RpP0; ORFNames=CG7490;
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].
RX PubMed=2471063; DOI=10.1128/mcb.9.3.965-973.1989;
RA Kelley M.R., Venugopal S., Harless J., Deutsch W.A.;
RT "Antibody to a human DNA repair protein allows for cloning of a Drosophila
RT cDNA that encodes an apurinic endonuclease.";
RL Mol. Cell. Biol. 9:965-973(1989).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SIMILARITY TO RIBOSOMAL PROTEIN P0.
RX PubMed=1870984; DOI=10.1093/nar/19.15.4297;
RA Grabowski D.T., Deutsch W.A., Derda D., Kelley M.R.;
RT "Drosophila AP3, a presumptive DNA repair protein, is homologous to human
RT ribosomal associated protein P0.";
RL Nucleic Acids Res. 19:4297-4297(1991).
RN [7]
RP DNA REPAIR ACTIVITY, AND CATALYTIC ACTIVITY.
RX PubMed=8932386; DOI=10.1093/nar/24.21.4298;
RA Yacoub A., Kelley M.R., Deutsch W.A.;
RT "Drosophila ribosomal protein PO contains apurinic/apyrimidinic
RT endonuclease activity.";
RL Nucleic Acids Res. 24:4298-4303(1996).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302 AND SER-304, 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: Ribosomal protein P0 is the functional equivalent of E.coli
CC protein L10.
CC -!- SUBUNIT: P0 forms a pentameric complex by interaction with dimers of P1
CC and P2. {ECO:0000250}.
CC -!- INTERACTION:
CC P19889; P08570: RpLP1; NbExp=4; IntAct=EBI-195497, EBI-125901;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- DEVELOPMENTAL STAGE: All stages of development. A larger transcript is
CC restricted to the embryonic and early larval stages.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000305}.
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DR EMBL; M25772; AAA53372.1; -; mRNA.
DR EMBL; AE014296; AAF51807.1; -; Genomic_DNA.
DR EMBL; AY075528; AAL68335.1; -; mRNA.
DR EMBL; BT021447; AAX33595.1; -; mRNA.
DR PIR; A30223; R5FFP0.
DR RefSeq; NP_001262202.1; NM_001275273.1.
DR RefSeq; NP_524211.1; NM_079487.4.
DR AlphaFoldDB; P19889; -.
DR SMR; P19889; -.
DR BioGRID; 65690; 108.
DR DIP; DIP-21968N; -.
DR IntAct; P19889; 4.
DR MINT; P19889; -.
DR STRING; 7227.FBpp0306232; -.
DR MoonProt; P19889; -.
DR iPTMnet; P19889; -.
DR PaxDb; P19889; -.
DR PRIDE; P19889; -.
DR DNASU; 40451; -.
DR EnsemblMetazoa; FBtr0078481; FBpp0078134; FBgn0000100.
DR EnsemblMetazoa; FBtr0334113; FBpp0306232; FBgn0000100.
DR GeneID; 40451; -.
DR KEGG; dme:Dmel_CG7490; -.
DR CTD; 6175; -.
DR FlyBase; FBgn0000100; RpLP0.
DR VEuPathDB; VectorBase:FBgn0000100; -.
DR eggNOG; KOG0815; Eukaryota.
DR GeneTree; ENSGT00390000017839; -.
DR HOGENOM; CLU_053173_1_1_1; -.
DR InParanoid; P19889; -.
DR OMA; MAHVAEW; -.
DR OrthoDB; 1102823at2759; -.
DR PhylomeDB; P19889; -.
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; P19889; -.
DR BioGRID-ORCS; 40451; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 40451; -.
DR PRO; PR:P19889; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000100; Expressed in egg cell and 22 other tissues.
DR ExpressionAtlas; P19889; baseline and differential.
DR Genevisible; P19889; DM.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0016363; C:nuclear matrix; IDA:CAFA.
DR GO; GO:0005654; C:nucleoplasm; IDA:CAFA.
DR GO; GO:0005840; C:ribosome; IDA:CAFA.
DR GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
DR GO; GO:0052720; F:class II DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:FlyBase.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:CAFA.
DR GO; GO:0004519; F:endonuclease activity; IDA:CAFA.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0006284; P:base-excision repair; IDA:CAFA.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:CAFA.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR Gene3D; 3.30.70.1730; -; 1.
DR Gene3D; 3.90.105.20; -; 1.
DR InterPro; IPR030670; L10E_eukaryotes.
DR InterPro; IPR043141; Ribosomal_L10-like_sf.
DR InterPro; IPR001790; Ribosomal_L10P.
DR InterPro; IPR043164; RL10_insert_sf.
DR InterPro; IPR040637; RL10P_insert.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR Pfam; PF17777; RL10P_insert; 1.
DR PIRSF; PIRSF039087; L10E; 1.
DR SUPFAM; SSF160369; SSF160369; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA damage; DNA repair; Hydrolase; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..317
FT /note="60S acidic ribosomal protein P0"
FT /id="PRO_0000154769"
FT REGION 280..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..317
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 304
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000255"
SQ SEQUENCE 317 AA; 34202 MW; 36E9DD5DD8CF7E1F CRC64;
MVRENKAAWK AQYFIKVVEL FDEFPKCFIV GADNVGSKQM QNIRTSLRGL AVVLMGKNTM
MRKAIRGHLE NNPQLEKLLP HIKGNVGFVF TKGDLAEVRD KLLESKVRAP ARPGAIAPLH
VIIPAQNTGL GPEKTSFFQA LSIPTKISKG TIEIINDVPI LKPGDKVGAS EATLLNMLNI
SPFSYGLIVN QVYDSGSIFS PEILDIKPED LRAKFQQGVA NLAAVCLSVG YPTIASAPHS
IANGFKNLLA IAATTEVEFK EATTIKEYIK DPSKFAAAAS ASAAPAAGGA TEKKEEAKKP
ESESEEEDDD MGFGLFD
