RLA02_ARATH
ID RLA02_ARATH Reviewed; 320 AA.
AC Q42112; Q8LCI7; Q9SR42; Q9SS70;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=60S acidic ribosomal protein P0-2;
GN Name=RPP0B; OrderedLocusNames=At3g09200; ORFNames=F3L24.7, MZB10.24;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 234-320.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [6]
RP PROTEIN SEQUENCE OF 299-320, AND PHOSPHORYLATION AT SER-305.
RX PubMed=16962150; DOI=10.1016/j.phytochem.2006.07.010;
RA Laugesen S., Messinese E., Hem S., Pichereaux C., Grat S., Ranjeva R.,
RA Rossignol M., Bono J.-J.;
RT "Phosphoproteins analysis in plants: a proteomic approach.";
RL Phytochemistry 67:2208-2214(2006).
RN [7]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=11598216; DOI=10.1104/pp.010265;
RA Barakat A., Szick-Miranda K., Chang I.-F., Guyot R., Blanc G., Cooke R.,
RA Delseny M., Bailey-Serres J.;
RT "The organization of cytoplasmic ribosomal protein genes in the Arabidopsis
RT genome.";
RL Plant Physiol. 127:398-415(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q42112-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000305}.
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DR EMBL; AC009326; AAD56335.1; -; Genomic_DNA.
DR EMBL; AC011436; AAF14020.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74736.1; -; Genomic_DNA.
DR EMBL; AF370225; AAK44040.1; -; mRNA.
DR EMBL; AY059117; AAL15223.1; -; mRNA.
DR EMBL; AY086582; AAM63644.1; -; mRNA.
DR EMBL; Z26534; CAA81305.1; -; mRNA.
DR RefSeq; NP_187531.1; NM_111754.4. [Q42112-1]
DR AlphaFoldDB; Q42112; -.
DR SMR; Q42112; -.
DR BioGRID; 5410; 132.
DR STRING; 3702.AT3G09200.1; -.
DR iPTMnet; Q42112; -.
DR PaxDb; Q42112; -.
DR PRIDE; Q42112; -.
DR EnsemblPlants; AT3G09200.1; AT3G09200.1; AT3G09200. [Q42112-1]
DR GeneID; 820076; -.
DR Gramene; AT3G09200.1; AT3G09200.1; AT3G09200. [Q42112-1]
DR KEGG; ath:AT3G09200; -.
DR Araport; AT3G09200; -.
DR TAIR; locus:2083564; AT3G09200.
DR eggNOG; KOG0815; Eukaryota.
DR HOGENOM; CLU_053173_1_1_1; -.
DR InParanoid; Q42112; -.
DR OMA; MAHVAEW; -.
DR PhylomeDB; Q42112; -.
DR PRO; PR:Q42112; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q42112; baseline and differential.
DR Genevisible; Q42112; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
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 Alternative splicing; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..320
FT /note="60S acidic ribosomal protein P0-2"
FT /id="PRO_0000154776"
FT REGION 289..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..320
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16962150,
FT ECO:0007744|PubMed:18433157, ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 310
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P57691"
FT CONFLICT 48
FT /note="R -> L (in Ref. 4; AAM63644)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 34133 MW; 644CE3BC0DC045E6 CRC64;
MVKATKAEKK IAYDTKLCQL IDEYTQILVV AADNVGSTQL QNIRKGLRGD SVVLMGKNTM
MKRSVRIHSE NTGNTAILNL LPLLQGNVGL IFTKGDLKEV SEEVAKYKVG APARVGLVAP
IDVVVQPGNT GLDPSQTSFF QVLNIPTKIN KGTVEIITPV ELIKQGDKVG SSEAALLAKL
GIRPFSYGLV VQSVYDNGSV FSPEVLDLTE DQLVEKFASG ISMVTSLALA VSYPTLAAAP
HMFINAYKNA LAIAVATEYT FPQAEKVKEY LKDPSKFAVA SVAAVSADAG GGAPAAAKVE
EKEESDEEDY GGDFGLFDEE
