RS16A_ARATH
ID RS16A_ARATH Reviewed; 113 AA.
AC O65686;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=30S ribosomal protein S16-1, chloroplastic {ECO:0000303|PubMed:18453549};
DE AltName: Full=Small subunit ribosomal protein 16 {ECO:0000303|PubMed:8811862};
DE Flags: Precursor;
GN Name=RPS16-1 {ECO:0000303|PubMed:18453549};
GN Synonyms=S16-2 {ECO:0000303|PubMed:16368778},
GN SSR16 {ECO:0000303|PubMed:8811862};
GN OrderedLocusNames=At4g34620 {ECO:0000312|Araport:AT4G34620};
GN ORFNames=T4L20.200 {ECO:0000312|EMBL:CAA18841.1};
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 [MRNA], DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. No-0;
RX PubMed=8811862; DOI=10.1046/j.1365-313x.1996.10030479.x;
RA Tsugeki R., Kochieva E.Z., Fedoroff N.V.;
RT "A transposon insertion in the Arabidopsis SSR16 gene causes an embryo-
RT defective lethal mutation.";
RL Plant J. 10:479-489(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
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 [6]
RP NOMENCLATURE, AND GENE FAMILY.
RX PubMed=16368778; DOI=10.1093/molbev/msj080;
RA Bonen L., Calixte S.;
RT "Comparative analysis of bacterial-origin genes for plant mitochondrial
RT ribosomal proteins.";
RL Mol. Biol. Evol. 23:701-712(2006).
RN [7]
RP SUBCELLULAR LOCATION, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=18453549; DOI=10.1093/molbev/msn102;
RA Ueda M., Nishikawa T., Fujimoto M., Takanashi H., Arimura S., Tsutsumi N.,
RA Kadowaki K.;
RT "Substitution of the gene for chloroplast RPS16 was assisted by generation
RT of a dual targeting signal.";
RL Mol. Biol. Evol. 25:1566-1575(2008).
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18453549}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers, and, to a
CC lower extent, in roots. {ECO:0000269|PubMed:8811862}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethal, arresting development at the
CC transition from the globular to the heart stage of embryonic
CC development. {ECO:0000269|PubMed:8811862}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family.
CC {ECO:0000305}.
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DR EMBL; AL023094; CAA18841.1; -; Genomic_DNA.
DR EMBL; AL161585; CAB80179.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86401.1; -; Genomic_DNA.
DR EMBL; AF412081; AAL06534.1; -; mRNA.
DR EMBL; AY045607; AAK73965.1; -; mRNA.
DR EMBL; AY048218; AAK82481.1; -; mRNA.
DR EMBL; AY052220; AAK97690.1; -; mRNA.
DR EMBL; AY143795; AAN28734.1; -; mRNA.
DR EMBL; AY086956; AAM64519.1; -; mRNA.
DR PIR; T05282; T05282.
DR RefSeq; NP_195188.1; NM_119628.5.
DR AlphaFoldDB; O65686; -.
DR SMR; O65686; -.
DR STRING; 3702.AT4G34620.1; -.
DR iPTMnet; O65686; -.
DR PaxDb; O65686; -.
DR PRIDE; O65686; -.
DR ProteomicsDB; 226856; -.
DR EnsemblPlants; AT4G34620.1; AT4G34620.1; AT4G34620.
DR GeneID; 829614; -.
DR Gramene; AT4G34620.1; AT4G34620.1; AT4G34620.
DR KEGG; ath:AT4G34620; -.
DR Araport; AT4G34620; -.
DR TAIR; locus:2139624; AT4G34620.
DR eggNOG; KOG3419; Eukaryota.
DR HOGENOM; CLU_100590_2_0_1; -.
DR InParanoid; O65686; -.
DR OMA; GFYNPIA; -.
DR OrthoDB; 1630052at2759; -.
DR PhylomeDB; O65686; -.
DR PRO; PR:O65686; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65686; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0005840; C:ribosome; TAS:TAIR.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0003735; F:structural constituent of ribosome; ISS:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.30.1320.10; -; 1.
DR HAMAP; MF_00385; Ribosomal_S16; 1.
DR InterPro; IPR000307; Ribosomal_S16.
DR InterPro; IPR023803; Ribosomal_S16_dom_sf.
DR PANTHER; PTHR12919; PTHR12919; 1.
DR Pfam; PF00886; Ribosomal_S16; 1.
DR SUPFAM; SSF54565; SSF54565; 1.
DR TIGRFAMs; TIGR00002; S16; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Plastid; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..15
FT /note="Chloroplast"
FT /evidence="ECO:0000305|PubMed:18453549"
FT CHAIN 16..113
FT /note="30S ribosomal protein S16-1, chloroplastic"
FT /id="PRO_0000436964"
FT REGION 93..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 113 AA; 12699 MW; E9EEA2C2DC680358 CRC64;
MTVKIRLARL GCKHRPFYRV VVADEKSRRD GKQIEVLGFY DPLQGKEDAD RVSLKFDRIK
YWLSVGAQPT DTVESMLFRA GLIPPKPMVV VGSKNGQKST SQHVSPITGE ILN
