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60S acidic ribosomal protein P0 (Apurinic-apyrimidinic endonuclease) (DNA-(apurinic or apyrimidinic site) lyase) (EC 4.2.99.18)

 RLA0_DROME              Reviewed;         317 AA.
P19889; Q5BHX7; Q9VNV9;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
25-OCT-2017, entry version 170.
RecName: Full=60S acidic ribosomal protein P0;
AltName: Full=Apurinic-apyrimidinic endonuclease;
AltName: Full=DNA-(apurinic or apyrimidinic site) lyase;
EC=4.2.99.18;
Name=RpLP0; Synonyms=AP3, Ape, RpP0; ORFNames=CG7490;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2471063; DOI=10.1128/MCB.9.3.965;
Kelley M.R., Venugopal S., Harless J., Deutsch W.A.;
"Antibody to a human DNA repair protein allows for cloning of a
Drosophila cDNA that encodes an apurinic endonuclease.";
Mol. Cell. Biol. 9:965-973(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Head;
Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
SIMILARITY TO RIBOSOMAL PROTEIN P0.
PubMed=1870984; DOI=10.1093/nar/19.15.4297;
Grabowski D.T., Deutsch W.A., Derda D., Kelley M.R.;
"Drosophila AP3, a presumptive DNA repair protein, is homologous to
human ribosomal associated protein P0.";
Nucleic Acids Res. 19:4297-4297(1991).
[7]
DNA REPAIR ACTIVITY.
PubMed=8932386; DOI=10.1093/nar/24.21.4298;
Yacoub A., Kelley M.R., Deutsch W.A.;
"Drosophila ribosomal protein PO contains apurinic/apyrimidinic
endonuclease activity.";
Nucleic Acids Res. 24:4298-4303(1996).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302 AND SER-304, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Ribosomal protein P0 is the functional equivalent of
E.coli protein L10.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate.
-!- SUBUNIT: P0 forms a pentameric complex by interaction with dimers
of P1 and P2. {ECO:0000250}.
-!- INTERACTION:
P08570:RpLP1; NbExp=4; IntAct=EBI-195497, EBI-125901;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- DEVELOPMENTAL STAGE: All stages of development. A larger
transcript is restricted to the embryonic and early larval stages.
-!- SIMILARITY: Belongs to the universal ribosomal protein uL10
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M25772; AAA53372.1; -; mRNA.
EMBL; AE014296; AAF51807.1; -; Genomic_DNA.
EMBL; AY075528; AAL68335.1; -; mRNA.
EMBL; BT021447; AAX33595.1; -; mRNA.
PIR; A30223; R5FFP0.
RefSeq; NP_001262202.1; NM_001275273.1.
RefSeq; NP_524211.1; NM_079487.4.
UniGene; Dm.7933; -.
ProteinModelPortal; P19889; -.
BioGrid; 65690; 24.
DIP; DIP-21968N; -.
IntAct; P19889; 4.
MINT; MINT-235412; -.
STRING; 7227.FBpp0306232; -.
MoonProt; P19889; -.
iPTMnet; P19889; -.
PaxDb; P19889; -.
PRIDE; P19889; -.
EnsemblMetazoa; FBtr0078481; FBpp0078134; FBgn0000100.
EnsemblMetazoa; FBtr0334113; FBpp0306232; FBgn0000100.
GeneID; 40451; -.
KEGG; dme:Dmel_CG7490; -.
CTD; 6175; -.
FlyBase; FBgn0000100; RpLP0.
eggNOG; KOG0815; Eukaryota.
eggNOG; COG0244; LUCA.
GeneTree; ENSGT00390000017839; -.
InParanoid; P19889; -.
KO; K02941; -.
OMA; FFQALQI; -.
OrthoDB; EOG091G0F47; -.
PhylomeDB; P19889; -.
Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-DME-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-DME-72689; Formation of a pool of free 40S subunits.
Reactome; R-DME-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-DME-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-DME-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
GenomeRNAi; 40451; -.
PRO; PR:P19889; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0000100; -.
ExpressionAtlas; P19889; differential.
Genevisible; P19889; DM.
GO; GO:0005829; C:cytosol; IDA:CAFA.
GO; GO:0022625; C:cytosolic large ribosomal subunit; TAS:FlyBase.
GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
GO; GO:0016363; C:nuclear matrix; IDA:CAFA.
GO; GO:0005654; C:nucleoplasm; IDA:CAFA.
GO; GO:0005840; C:ribosome; IDA:FlyBase.
GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-EC.
GO; GO:0140080; F:class III/IV DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-EC.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:CAFA.
GO; GO:0004519; F:endonuclease activity; IDA:CAFA.
GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
GO; GO:0006284; P:base-excision repair; IDA:CAFA.
GO; GO:0002181; P:cytoplasmic translation; TAS:FlyBase.
GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:CAFA.
GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro.
InterPro; IPR030670; L10E_eukaryotes.
InterPro; IPR001790; Ribosomal_L10P.
Pfam; PF00466; Ribosomal_L10; 1.
PIRSF; PIRSF039087; L10E; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; DNA damage; DNA repair; Lyase; Nucleus;
Phosphoprotein; Reference proteome; Ribonucleoprotein;
Ribosomal protein.
CHAIN 1 317 60S acidic ribosomal protein P0.
/FTId=PRO_0000154769.
MOD_RES 302 302 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 304 304 Phosphoserine; by CK1. {ECO:0000255}.
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


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