RS51_ARATH
ID RS51_ARATH Reviewed; 207 AA.
AC Q9ZUT9; Q8L967;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=40S ribosomal protein S5-1;
DE AltName: Full=AtRPS5B {ECO:0000303|PubMed:11684664};
GN Name=RPS5A {ECO:0000303|PubMed:11598216}; OrderedLocusNames=At2g37270;
GN ORFNames=F3G5.6;
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 TISSUE SPECIFICITY.
RX PubMed=11684664; DOI=10.1242/dev.128.21.4289;
RA Weijers D., Franke-van Dijk M., Vencken R.J., Quint A., Hooykaas P.,
RA Offringa R.;
RT "An Arabidopsis Minute-like phenotype caused by a semi-dominant mutation in
RT a RIBOSOMAL PROTEIN S5 gene.";
RL Development 128:4289-4299(2001).
RN [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- TISSUE SPECIFICITY: Expressed in epidermal cells of root tips, lateral
CC root primordia, root hairs and shoot primordia.
CC {ECO:0000269|PubMed:11684664}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 family.
CC {ECO:0000305}.
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DR EMBL; AC005896; AAC98068.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09375.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09376.1; -; Genomic_DNA.
DR EMBL; AY059849; AAL24331.1; -; mRNA.
DR EMBL; AY081669; AAM10231.1; -; mRNA.
DR EMBL; AY088613; AAM66936.1; -; mRNA.
DR PIR; F84790; F84790.
DR RefSeq; NP_001031502.1; NM_001036425.2.
DR RefSeq; NP_181264.1; NM_129283.4.
DR AlphaFoldDB; Q9ZUT9; -.
DR SMR; Q9ZUT9; -.
DR BioGRID; 3648; 119.
DR IntAct; Q9ZUT9; 1.
DR STRING; 3702.AT2G37270.2; -.
DR iPTMnet; Q9ZUT9; -.
DR PaxDb; Q9ZUT9; -.
DR PRIDE; Q9ZUT9; -.
DR ProteomicsDB; 226533; -.
DR EnsemblPlants; AT2G37270.1; AT2G37270.1; AT2G37270.
DR EnsemblPlants; AT2G37270.2; AT2G37270.2; AT2G37270.
DR GeneID; 818304; -.
DR Gramene; AT2G37270.1; AT2G37270.1; AT2G37270.
DR Gramene; AT2G37270.2; AT2G37270.2; AT2G37270.
DR KEGG; ath:AT2G37270; -.
DR Araport; AT2G37270; -.
DR TAIR; locus:2049862; AT2G37270.
DR eggNOG; KOG3291; Eukaryota.
DR HOGENOM; CLU_063975_0_0_1; -.
DR InParanoid; Q9ZUT9; -.
DR OMA; KMNIVER; -.
DR OrthoDB; 1532160at2759; -.
DR PhylomeDB; Q9ZUT9; -.
DR PRO; PR:Q9ZUT9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUT9; baseline and differential.
DR Genevisible; Q9ZUT9; AT.
DR GO; GO:0009507; C:chloroplast; 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:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd14867; uS7_Eukaryote; 1.
DR Gene3D; 1.10.455.10; -; 1.
DR InterPro; IPR000235; Ribosomal_S5/S7.
DR InterPro; IPR005716; Ribosomal_S5/S7_euk/arc.
DR InterPro; IPR020606; Ribosomal_S7_CS.
DR InterPro; IPR023798; Ribosomal_S7_dom.
DR InterPro; IPR036823; Ribosomal_S7_dom_sf.
DR PANTHER; PTHR11205; PTHR11205; 1.
DR Pfam; PF00177; Ribosomal_S7; 1.
DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1.
DR SUPFAM; SSF47973; SSF47973; 1.
DR TIGRFAMs; TIGR01028; uS7_euk_arch; 1.
DR PROSITE; PS00052; RIBOSOMAL_S7; 1.
PE 1: Evidence at protein level;
KW Acetylation; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..207
FT /note="40S ribosomal protein S5-1"
FT /id="PRO_0000124534"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 162
FT /note="R -> G (in Ref. 4; AAM66936)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 207 AA; 22991 MW; 7D49B07EDD58DAB7 CRC64;
MAASAEIDAE IQQQLTNEVK LFNRWSFDDV SVTDISLVDY IGVQPSKHAT FVPHTAGRYS
VKRFRKAQCP IVERLTNSLM MHGRNNGKKL MAVRIVKHAM EIIHLLSDLN PIQVIIDAIV
NSGPREDATR IGSAGVVRRQ AVDISPLRRV NQAIFLLTTG AREAAFRNIK TIAECLADEL
INAAKGSSNS YAIKKKDEIE RVAKANR
