RS23_ARATH
ID RS23_ARATH Reviewed; 285 AA.
AC P49688; O22936;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 161.
DE RecName: Full=40S ribosomal protein S2-3 {ECO:0000303|PubMed:11598216};
DE Short=AtRPS2C {ECO:0000303|PubMed:11598216, ECO:0000303|PubMed:28229965};
GN Name=RPS2C {ECO:0000303|PubMed:11598216, ECO:0000303|PubMed:28229965};
GN OrderedLocusNames=At2g41840 {ECO:0000312|Araport:AT2G41840};
GN ORFNames=T11A07.6 {ECO:0000312|EMBL:AAC02764.1};
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=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] OF 119-285.
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
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].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
RP IDENTIFICATION BY 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 [8]
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).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH MBD6.
RX PubMed=28229965; DOI=10.1007/s12038-016-9658-1;
RA Parida A.P., Sharma A., Sharma A.K.;
RT "AtMBD6, a methyl CpG binding domain protein, maintains gene silencing in
RT Arabidopsis by interacting with RNA binding proteins.";
RL J. Biosci. 42:57-68(2017).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. Plays a role in the assembly and function of the 40S ribosomal
CC subunit. Mutations in this protein affects the control of translational
CC fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and
CC ribosome assembly (By similarity). Also involved in RNA-directed DNA
CC methylation (RdDM) (PubMed:28229965). {ECO:0000250|UniProtKB:P25443,
CC ECO:0000269|PubMed:28229965}.
CC -!- SUBUNIT: Interacts with MBD6. {ECO:0000269|PubMed:28229965}.
CC -!- DISRUPTION PHENOTYPE: Reduced DNA methylation in some of the targets of
CC RNA-directed DNA methylation (RdDM). {ECO:0000269|PubMed:28229965}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC002339; AAC02764.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10039.1; -; Genomic_DNA.
DR EMBL; AY048250; AAK82512.1; -; mRNA.
DR EMBL; AY133561; AAM91391.1; -; mRNA.
DR EMBL; Z17622; CAA79017.1; -; mRNA.
DR PIR; G84846; G84846.
DR RefSeq; NP_181715.1; NM_129748.4.
DR AlphaFoldDB; P49688; -.
DR SMR; P49688; -.
DR BioGRID; 4121; 116.
DR IntAct; P49688; 2.
DR STRING; 3702.AT2G41840.1; -.
DR iPTMnet; P49688; -.
DR PaxDb; P49688; -.
DR PRIDE; P49688; -.
DR ProteomicsDB; 226548; -.
DR EnsemblPlants; AT2G41840.1; AT2G41840.1; AT2G41840.
DR GeneID; 818784; -.
DR Gramene; AT2G41840.1; AT2G41840.1; AT2G41840.
DR KEGG; ath:AT2G41840; -.
DR Araport; AT2G41840; -.
DR TAIR; locus:2054406; AT2G41840.
DR eggNOG; KOG0877; Eukaryota.
DR HOGENOM; CLU_065898_0_2_1; -.
DR InParanoid; P49688; -.
DR OMA; DLKNWVP; -.
DR OrthoDB; 1197354at2759; -.
DR PhylomeDB; P49688; -.
DR PRO; PR:P49688; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P49688; baseline and differential.
DR Genevisible; P49688; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR000851; Ribosomal_S5.
DR InterPro; IPR005324; Ribosomal_S5_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005711; Ribosomal_S5_euk/arc.
DR InterPro; IPR013810; Ribosomal_S5_N.
DR InterPro; IPR018192; Ribosomal_S5_N_CS.
DR PANTHER; PTHR13718; PTHR13718; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR01020; uS5_euk_arch; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-mediated gene silencing.
FT CHAIN 1..285
FT /note="40S ribosomal protein S2-3"
FT /id="PRO_0000131682"
FT DOMAIN 96..159
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 268..269
FT /note="AS -> ST (in Ref. 4; CAA79017)"
FT /evidence="ECO:0000305"
FT CONFLICT 272..281
FT /note="LSTSKPDPVV -> VSATKVITEG (in Ref. 4; CAA79017)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 30879 MW; 68C8C98091D4995B CRC64;
MAERGGERGV ERGGERGDFG RGFGGRGGRG DRGGRGRGGR GGRRGGRASE EEKWVPVTKL
GRLVAAGHIK QIEQIYLHSL PVKEYQIIDM LIGPTLKDEV MKIMPVQKQT RAGQRTRFKA
FVVVGDGNGH VGLGVKCSKE VATAIRGAII LAKLSVVPVR RGYWGNKIGK PHTVPCKVTG
KCGSVTVRMV PAPRGSGIVA ARVPKKVLQF AGIDDVFTSS RGSTKTLGNF VKATFDCLQK
TYGFLTPEFW KETRFSRSPY QEHTDFLASK ALSTSKPDPV VEDQA
