RLA23_ARATH
ID RLA23_ARATH Reviewed; 115 AA.
AC Q9LH85;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=60S acidic ribosomal protein P2-3;
GN Name=RPP2C; OrderedLocusNames=At3g28500; ORFNames=T20D4.1;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-105, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Plays an important role in the elongation step of protein
CC synthesis. {ECO:0000250}.
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; AP002059; BAB01952.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77453.1; -; Genomic_DNA.
DR EMBL; BT003971; AAO42015.1; -; mRNA.
DR EMBL; BT005087; AAO50620.1; -; mRNA.
DR EMBL; AY086773; AAM63824.1; -; mRNA.
DR RefSeq; NP_189491.1; NM_113770.3.
DR AlphaFoldDB; Q9LH85; -.
DR SMR; Q9LH85; -.
DR BioGRID; 7809; 1.
DR STRING; 3702.AT3G28500.1; -.
DR iPTMnet; Q9LH85; -.
DR PaxDb; Q9LH85; -.
DR PRIDE; Q9LH85; -.
DR ProteomicsDB; 228018; -.
DR EnsemblPlants; AT3G28500.1; AT3G28500.1; AT3G28500.
DR GeneID; 822480; -.
DR Gramene; AT3G28500.1; AT3G28500.1; AT3G28500.
DR KEGG; ath:AT3G28500; -.
DR Araport; AT3G28500; -.
DR TAIR; locus:2098653; AT3G28500.
DR eggNOG; KOG3449; Eukaryota.
DR HOGENOM; CLU_114656_0_2_1; -.
DR InParanoid; Q9LH85; -.
DR OMA; GITMIKG; -.
DR OrthoDB; 1626327at2759; -.
DR PhylomeDB; Q9LH85; -.
DR PRO; PR:Q9LH85; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LH85; baseline and differential.
DR Genevisible; Q9LH85; AT.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:InterPro.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
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_L12/P1/P2.
DR InterPro; IPR044076; Ribosomal_P2.
DR PANTHER; PTHR21141; PTHR21141; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..115
FT /note="60S acidic ribosomal protein P2-3"
FT /id="PRO_0000245776"
FT REGION 78..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
SQ SEQUENCE 115 AA; 11735 MW; 90F28CD3F28AE81A CRC64;
MKVIAAFLLA KLGGNENPTS NDLKKILESV GAEIDETKID LLFSLIKDHD VTELIAAGRE
KMSALSSGGP AVAMVAGGGG GGAASAAEPV AESKKKVEEV KDESSDDAGM MGLFD
