RLA22_ARATH
ID RLA22_ARATH Reviewed; 115 AA.
AC Q9SLF7; Q8LB03;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=60S acidic ribosomal protein P2-2;
GN Name=RPP2B; OrderedLocusNames=At2g27710; ORFNames=F15K20.19;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 IDENTIFICATION BY 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: Plays an important role in the elongation step of protein
CC synthesis.
CC -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
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=Q9SLF7-1; Sequence=Displayed;
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC {ECO:0000305}.
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DR EMBL; AC005824; AAC73029.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08029.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08030.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08031.1; -; Genomic_DNA.
DR EMBL; AF428429; AAL16198.1; -; mRNA.
DR EMBL; AY062854; AAL32932.1; -; mRNA.
DR EMBL; BT006518; AAP21326.1; -; mRNA.
DR EMBL; AY087501; AAM65044.1; -; mRNA.
DR PIR; A84676; A84676.
DR RefSeq; NP_180339.1; NM_128330.4. [Q9SLF7-1]
DR RefSeq; NP_850106.1; NM_179775.2. [Q9SLF7-1]
DR RefSeq; NP_973549.1; NM_201820.1. [Q9SLF7-1]
DR AlphaFoldDB; Q9SLF7; -.
DR BioGRID; 2667; 46.
DR STRING; 3702.AT2G27710.1; -.
DR iPTMnet; Q9SLF7; -.
DR PaxDb; Q9SLF7; -.
DR PRIDE; Q9SLF7; -.
DR ProteomicsDB; 228127; -. [Q9SLF7-1]
DR EnsemblPlants; AT2G27710.1; AT2G27710.1; AT2G27710. [Q9SLF7-1]
DR EnsemblPlants; AT2G27710.2; AT2G27710.2; AT2G27710. [Q9SLF7-1]
DR EnsemblPlants; AT2G27710.3; AT2G27710.3; AT2G27710. [Q9SLF7-1]
DR GeneID; 817317; -.
DR Gramene; AT2G27710.1; AT2G27710.1; AT2G27710. [Q9SLF7-1]
DR Gramene; AT2G27710.2; AT2G27710.2; AT2G27710. [Q9SLF7-1]
DR Gramene; AT2G27710.3; AT2G27710.3; AT2G27710. [Q9SLF7-1]
DR KEGG; ath:AT2G27710; -.
DR Araport; AT2G27710; -.
DR TAIR; locus:2042062; AT2G27710.
DR eggNOG; KOG3449; Eukaryota.
DR HOGENOM; CLU_114656_0_0_1; -.
DR InParanoid; Q9SLF7; -.
DR OMA; GHAFIST; -.
DR PhylomeDB; Q9SLF7; -.
DR PRO; PR:Q9SLF7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SLF7; baseline and differential.
DR Genevisible; Q9SLF7; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:InterPro.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0002182; P:cytoplasmic translational elongation; IEA:InterPro.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
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 Alternative splicing; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..115
FT /note="60S acidic ribosomal protein P2-2"
FT /id="PRO_0000157659"
FT REGION 63..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LH85"
FT CONFLICT 61
FT /note="K -> N (in Ref. 4; AAM65044)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="S -> P (in Ref. 4; AAM65044)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 115 AA; 11444 MW; 66DF1FA9E0AEE2AE CRC64;
MKVVAAYLLA VLSGKASPTS ADIKTILGSV GAETEDSQIE LLLKEVKGKD LAELIAAGRE
KLASVPSGGG GGVAVASATS GGGGGGGASA AESKKEEKKE EKEESDDDMG FSLFE
