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60S acidic ribosomal protein P0 (60S ribosomal protein L10E) (Large ribosomal subunit protein uL10)

 RLA0_HUMAN              Reviewed;         317 AA.
P05388; Q3B7A4; Q9BVK4;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
22-NOV-2017, entry version 198.
RecName: Full=60S acidic ribosomal protein P0;
AltName: Full=60S ribosomal protein L10E;
AltName: Full=Large ribosomal subunit protein uL10 {ECO:0000303|PubMed:24524803};
Name=RPLP0;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBUNIT.
PubMed=3323886; DOI=10.1128/MCB.7.11.4065;
Rich B.E., Steitz J.A.;
"Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of
cDNA clones, in vitro synthesis, and assembly.";
Mol. Cell. Biol. 7:4065-4074(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, Cervix, Colon, Lung, Lymph, Muscle, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 17-38; 84-92; 135-146; 150-162; 248-264 AND
267-297, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 218-310.
PubMed=9582194;
Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
Hudson T.J., Tanaka T., Page D.C.;
"A map of 75 human ribosomal protein genes.";
Genome Res. 8:509-523(1998).
[6]
IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
Johnsen A.H., Christiansen J., Nielsen F.C.;
"Molecular composition of IMP1 ribonucleoprotein granules.";
Mol. Cell. Proteomics 6:798-811(2007).
[7]
INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, AND
SUBCELLULAR LOCATION.
PubMed=19188445; DOI=10.1128/MCB.01337-08;
Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M.,
Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A.,
Quadrifoglio F., Tell G.;
"APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in
the rRNA quality control process.";
Mol. Cell. Biol. 29:1834-1854(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
NOMENCLATURE.
PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
Williamson J.R., Wilson D., Yonath A., Yusupov M.;
"A new system for naming ribosomal proteins.";
Curr. Opin. Struct. Biol. 24:165-169(2014).
[13]
INTERACTION WITH FMR1.
PubMed=24658146; DOI=10.1371/journal.pone.0091465;
Taha M.S., Nouri K., Milroy L.G., Moll J.M., Herrmann C.,
Brunsveld L., Piekorz R.P., Ahmadian M.R.;
"Subcellular fractionation and localization studies reveal a direct
interaction of the fragile X mental retardation protein (FMRP) with
nucleolin.";
PLoS ONE 9:E91465-E91465(2014).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-297, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[16]
STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
PubMed=23636399; DOI=10.1038/nature12104;
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
Wilson D.N., Beckmann R.;
"Structures of the human and Drosophila 80S ribosome.";
Nature 497:80-85(2013).
-!- FUNCTION: Ribosomal protein P0 is the functional equivalent of
E.coli protein L10.
-!- SUBUNIT: P0 forms a pentameric complex by interaction with dimers
of P1 and P2 (PubMed:3323886). Identified in a IGF2BP1-dependent
mRNP granule complex containing untranslated mRNAs
(PubMed:17289661). Interacts with APEX1 (PubMed:19188445).
Interacts with FMR1 isoform 6 (PubMed:24658146). Interacts with
Lassa virus Z protein. {ECO:0000269|PubMed:17289661,
ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:24658146,
ECO:0000269|PubMed:3323886}.
-!- INTERACTION:
O95273:CCNDBP1; NbExp=3; IntAct=EBI-354101, EBI-748961;
O95793:STAU1; NbExp=4; IntAct=EBI-354101, EBI-358174;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19188445}.
Cytoplasm {ECO:0000269|PubMed:19188445}. Note=Localized in
cytoplasmic mRNP granules containing untranslated mRNAs
(PubMed:19188445, PubMed:17289661). {ECO:0000269|PubMed:17289661,
ECO:0000269|PubMed:19188445}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P05388-1; Sequence=Displayed;
Name=2;
IsoId=P05388-2; Sequence=VSP_055867;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the universal ribosomal protein uL10
family. {ECO:0000305}.
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EMBL; M17885; AAA36470.1; -; mRNA.
EMBL; AC004263; AAC05176.1; -; Genomic_DNA.
EMBL; BC000087; AAH00087.1; -; mRNA.
EMBL; BC000345; AAH00345.1; -; mRNA.
EMBL; BC000752; AAH00752.1; -; mRNA.
EMBL; BC001127; AAH01127.1; -; mRNA.
EMBL; BC001834; AAH01834.1; -; mRNA.
EMBL; BC003655; AAH03655.1; -; mRNA.
EMBL; BC005863; AAH05863.1; -; mRNA.
EMBL; BC008092; AAH08092.1; -; mRNA.
EMBL; BC008594; AAH08594.1; -; mRNA.
EMBL; BC009867; AAH09867.1; -; mRNA.
EMBL; BC015173; AAH15173.1; -; mRNA.
EMBL; BC015690; AAH15690.1; -; mRNA.
EMBL; BC107717; AAI07718.1; -; mRNA.
EMBL; AB007187; BAA25845.1; -; Genomic_DNA.
CCDS; CCDS9193.1; -. [P05388-1]
PIR; A27125; R5HUP0.
RefSeq; NP_000993.1; NM_001002.3. [P05388-1]
RefSeq; NP_444505.1; NM_053275.3. [P05388-1]
UniGene; Hs.546285; -.
PDB; 4V6W; EM; 6.00 A; q=5-227.
PDB; 4V6X; EM; 5.00 A; Cq=1-317.
PDB; 5AJ0; EM; 3.50 A; AK=1-317.
PDBsum; 4V6W; -.
PDBsum; 4V6X; -.
PDBsum; 5AJ0; -.
ProteinModelPortal; P05388; -.
SMR; P05388; -.
BioGrid; 112094; 210.
CORUM; P05388; -.
IntAct; P05388; 52.
MINT; MINT-193149; -.
STRING; 9606.ENSP00000339027; -.
iPTMnet; P05388; -.
PhosphoSitePlus; P05388; -.
SwissPalm; P05388; -.
BioMuta; RPLP0; -.
DMDM; 133041; -.
REPRODUCTION-2DPAGE; P05388; -.
EPD; P05388; -.
MaxQB; P05388; -.
PaxDb; P05388; -.
PeptideAtlas; P05388; -.
PRIDE; P05388; -.
TopDownProteomics; P05388-1; -. [P05388-1]
DNASU; 6175; -.
Ensembl; ENST00000228306; ENSP00000339027; ENSG00000089157. [P05388-1]
Ensembl; ENST00000313104; ENSP00000366471; ENSG00000089157. [P05388-2]
Ensembl; ENST00000392514; ENSP00000376299; ENSG00000089157. [P05388-1]
Ensembl; ENST00000551150; ENSP00000449328; ENSG00000089157. [P05388-1]
GeneID; 6175; -.
KEGG; hsa:6175; -.
UCSC; uc001txp.4; human. [P05388-1]
CTD; 6175; -.
DisGeNET; 6175; -.
EuPathDB; HostDB:ENSG00000089157.15; -.
GeneCards; RPLP0; -.
HGNC; HGNC:10371; RPLP0.
HPA; HPA003512; -.
MIM; 180510; gene.
neXtProt; NX_P05388; -.
OpenTargets; ENSG00000089157; -.
PharmGKB; PA34772; -.
eggNOG; KOG0815; Eukaryota.
eggNOG; COG0244; LUCA.
GeneTree; ENSGT00390000017839; -.
HOGENOM; HOG000210987; -.
HOVERGEN; HBG000711; -.
InParanoid; P05388; -.
KO; K02941; -.
OMA; FFQALQI; -.
OrthoDB; EOG091G0F47; -.
PhylomeDB; P05388; -.
TreeFam; TF300849; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-156902; Peptide chain elongation.
Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-HSA-192823; Viral mRNA Translation.
Reactome; R-HSA-2408557; Selenocysteine synthesis.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-HSA-72764; Eukaryotic Translation Termination.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
ChiTaRS; RPLP0; human.
GeneWiki; RPLP0; -.
GenomeRNAi; 6175; -.
PRO; PR:P05388; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000089157; -.
CleanEx; HS_RPLP0; -.
ExpressionAtlas; P05388; baseline and differential.
Genevisible; P05388; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003735; F:structural constituent of ribosome; IDA:GO_Central.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
GO; GO:0006364; P:rRNA processing; TAS:Reactome.
GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
GO; GO:0006412; P:translation; NAS:UniProtKB.
GO; GO:0006413; P:translational initiation; TAS:Reactome.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
InterPro; IPR030670; L10E_eukaryotes.
InterPro; IPR001790; Ribosomal_L10P.
Pfam; PF00466; Ribosomal_L10; 1.
PIRSF; PIRSF039087; L10E; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Host-virus interaction; Isopeptide bond;
Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
Ribosomal protein; Ubl conjugation.
CHAIN 1 317 60S acidic ribosomal protein P0.
/FTId=PRO_0000154758.
MOD_RES 24 24 Phosphotyrosine.
{ECO:0000250|UniProtKB:P14869}.
MOD_RES 59 59 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 307 307 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
CROSSLNK 297 297 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 297 297 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211}.
VAR_SEQ 156 217 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055867.
CONFLICT 246 246 K -> E (in Ref. 3; AAH01127).
{ECO:0000305}.
SEQUENCE 317 AA; 34274 MW; 255AD25571C51199 CRC64;
MPREDRATWK SNYFLKIIQL LDDYPKCFIV GADNVGSKQM QQIRMSLRGK AVVLMGKNTM
MRKAIRGHLE NNPALEKLLP HIRGNVGFVF TKEDLTEIRD MLLANKVPAA ARAGAIAPCE
VTVPAQNTGL GPEKTSFFQA LGITTKISRG TIEILSDVQL IKTGDKVGAS EATLLNMLNI
SPFSFGLVIQ QVFDNGSIYN PEVLDITEET LHSRFLEGVR NVASVCLQIG YPTVASVPHS
IINGYKRVLA LSVETDYTFP LAEKVKAFLA DPSAFVAAAP VAAATTAAPA AAAAPAKVEA
KEESEESDED MGFGLFD


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EIAAB33379 60S ribosomal protein L39 pseudogene 5,Homo sapiens,Human,Putative 60S ribosomal protein L39-like 5,RPL39P5
29-221 RPL32 is a ribosomal protein that is a component of the 60S subunit. RPL32 belongs to the L32E family of ribosomal proteins. It is located in the cytoplasm. Although some studies have mapped this gene 0.1 mg
EIAAB35096 60S ribosomal protein L39-2,60S ribosomal protein L39-like,Homo sapiens,Human,RPL39L,RPL39L1
EIAAB35108 60S ribosomal protein L1,60S ribosomal protein L4,Homo sapiens,Human,RPL1,RPL4
EIAAB35071 60S ribosomal protein L36a,60S ribosomal protein L44,Mouse,Mus musculus,Rpl36a,Rpl44
EIAAB35072 60S ribosomal protein L36a,60S ribosomal protein L44,Rat,Rattus norvegicus,Rpl36a,Rpl44
EIAAB35249 39S ribosomal protein L23, mitochondrial,Homo sapiens,Human,L23 mitochondrial-related protein,L23MRP,L23mt,MRPL23,MRP-L23,Ribosomal protein L23-like,RPL23L


 

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