RPS1_ARATH
ID RPS1_ARATH Reviewed; 416 AA.
AC Q93VC7;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=30S ribosomal protein S1, chloroplastic {ECO:0000305};
DE AltName: Full=Plastid ribosomal protein S1 {ECO:0000303|PubMed:22900828};
DE Short=PRPS1 {ECO:0000303|PubMed:22900828};
DE Flags: Precursor;
GN Name=RPS1 {ECO:0000312|EMBL:AED93877.1};
GN OrderedLocusNames=At5g30510 {ECO:0000312|Araport:AT5G30510};
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 {ECO:0000312|EMBL:AAL24396.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-45, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-44, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22900828; DOI=10.1111/tpj.12000;
RA Romani I., Tadini L., Rossi F., Masiero S., Pribil M., Jahns P., Kater M.,
RA Leister D., Pesaresi P.;
RT "Versatile roles of Arabidopsis plastid ribosomal proteins in plant growth
RT and development.";
RL Plant J. 72:922-934(2012).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY HEAT STRESS, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22570631; DOI=10.1371/journal.pgen.1002669;
RA Yu H.D., Yang X.F., Chen S.T., Wang Y.T., Li J.K., Shen Q., Liu X.L.,
RA Guo F.Q.;
RT "Downregulation of chloroplast RPS1 negatively modulates nuclear heat-
RT responsive expression of HsfA2 and its target genes in Arabidopsis.";
RL PLoS Genet. 8:E1002669-E1002669(2012).
CC -!- FUNCTION: Required for optimal plastid performance in terms of
CC photosynthesis and growth. Required for the translation of plastid
CC mRNAs (PubMed:22900828). Involved in cellular heat stress response and
CC required for heat tolerance. Required for transcriptional activation of
CC HSFA2 and its target genes in response to heat stress. Plays a critical
CC role in biosynthesis of thylakoid membrane proteins encoded by
CC chloroplast genes (PubMed:22570631). {ECO:0000269|PubMed:22570631,
CC ECO:0000269|PubMed:22900828}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255,
CC ECO:0000269|PubMed:22570631}.
CC -!- INDUCTION: By heat stress (at protein level).
CC {ECO:0000269|PubMed:22570631}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant size and pale green leaves.
CC {ECO:0000269|PubMed:22570631, ECO:0000269|PubMed:22900828}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000305}.
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DR EMBL; AC069554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93877.1; -; Genomic_DNA.
DR EMBL; AF370232; AAK44047.1; -; mRNA.
DR EMBL; AY059914; AAL24396.1; -; mRNA.
DR EMBL; AY142540; AAN13122.1; -; mRNA.
DR EMBL; AY088230; AAM65771.1; -; mRNA.
DR RefSeq; NP_850903.1; NM_180572.2.
DR AlphaFoldDB; Q93VC7; -.
DR STRING; 3702.AT5G30510.1; -.
DR iPTMnet; Q93VC7; -.
DR MetOSite; Q93VC7; -.
DR World-2DPAGE; 0003:Q93VC7; -.
DR PaxDb; Q93VC7; -.
DR PRIDE; Q93VC7; -.
DR ProMEX; Q93VC7; -.
DR ProteomicsDB; 228250; -.
DR EnsemblPlants; AT5G30510.1; AT5G30510.1; AT5G30510.
DR GeneID; 833138; -.
DR Gramene; AT5G30510.1; AT5G30510.1; AT5G30510.
DR KEGG; ath:AT5G30510; -.
DR Araport; AT5G30510; -.
DR TAIR; locus:2145860; AT5G30510.
DR eggNOG; ENOG502QUY8; Eukaryota.
DR HOGENOM; CLU_015805_0_1_1; -.
DR InParanoid; Q93VC7; -.
DR OMA; YDYHFSP; -.
DR OrthoDB; 828313at2759; -.
DR PhylomeDB; Q93VC7; -.
DR PRO; PR:Q93VC7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93VC7; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 3.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR Pfam; PF00575; S1; 2.
DR SMART; SM00316; S1; 3.
DR SUPFAM; SSF50249; SSF50249; 3.
DR PROSITE; PS50126; S1; 3.
PE 1: Evidence at protein level;
KW Acetylation; Chloroplast; Plastid; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 45..416
FT /note="30S ribosomal protein S1, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000435323"
FT DOMAIN 99..169
FT /note="S1 motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 187..251
FT /note="S1 motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 264..332
FT /note="S1 motif 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 416 AA; 45110 MW; CF841A48D559417C CRC64;
MASLAQQFSG LRCSPLSSSS RLSRRASKNF PQNKSASVSP TIVAAVAMSS GQTKERLELK
KMFEDAYERC RTSPMEGVAF TVDDFAAAIE QYDFNSEIGT RVKGTVFKTD ANGALVDISA
KSSAYLSVEQ ACIHRIKHVE EAGIVPGMVE EFVIIGENES DDSLLLSLRN IQYELAWERC
RQLQAEDVIV KAKVIGANKG GLVALVEGLR GFVPFSQISS KAAAEELLEK EIPLKFVEVD
EEQTKLVLSN RKAVADSQAQ LGIGSVVLGV VQSLKPYGAF IDIGGINGLL HVSQISHDRV
SDIATVLQPG DTLKVMILSH DRDRGRVSLS TKKLEPTPGD MIRNPKLVFE KAEEMAQTFR
QRIAQAEAMA RADMLRFQPE SGLTLSSDGI LGPLGSELPD DGVDLTVDDI PSAVDI
