RL101_ARATH
ID RL101_ARATH Reviewed; 220 AA.
AC Q93VT9; F4HUJ2; Q93VL0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=60S ribosomal protein L10-1 {ECO:0000303|PubMed:11598216};
DE AltName: Full=Ribosomal protein RPL10A {ECO:0000303|PubMed:11598216};
DE AltName: Full=Suppressor of ACAULIS 52 {ECO:0000303|PubMed:18694459};
GN Name=RPL10A {ECO:0000303|PubMed:11598216};
GN Synonyms=SAC52 {ECO:0000303|PubMed:18694459};
GN OrderedLocusNames=At1g14320 {ECO:0000312|Araport:AT1G14320};
GN ORFNames=F14L17.9 {ECO:0000312|EMBL:AAF43932.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 1).
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 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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-14, AND TISSUE
RP SPECIFICITY.
RX PubMed=18694459; DOI=10.1111/j.1365-313x.2008.03647.x;
RA Imai A., Komura M., Kawano E., Kuwashiro Y., Takahashi T.;
RT "A semi-dominant mutation in the ribosomal protein L10 gene suppresses the
RT dwarf phenotype of the acl5 mutant in Arabidopsis thaliana.";
RL Plant J. 56:881-890(2008).
RN [6]
RP FUNCTION, INTERACTION WITH NIK1, SUBCELLULAR LOCATION, PHOSPHORYLATION BY
RP NIK1, AND DISRUPTION PHENOTYPE.
RX PubMed=19112492; DOI=10.1371/journal.ppat.1000247;
RA Carvalho C.M., Santos A.A., Pires S.R., Rocha C.S., Saraiva D.I.,
RA Machado J.P., Mattos E.C., Fietto L.G., Fontes E.P.;
RT "Regulated nuclear trafficking of rpL10A mediated by NIK1 represents a
RT defense strategy of plant cells against virus.";
RL PLoS Pathog. 4:E1000247-E1000247(2008).
RN [7]
RP FUNCTION, INTERACTION WITH NIK1, PHOSPHORYLATION BY NIK1 AND NIK2, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18789471; DOI=10.1016/j.virol.2008.08.005;
RA Rocha C.S., Santos A.A., Machado J.P., Fontes E.P.;
RT "The ribosomal protein L10/QM-like protein is a component of the NIK-
RT mediated antiviral signaling.";
RL Virology 380:165-169(2008).
RN [8]
RP FUNCTION, DEVELOPMENTAL STAGE, IDENTIFICATION IN RIBOSOME, DISRUPTION
RP PHENOTYPE, AND LACK OF INDUCTION BY UV-B.
RX PubMed=20516338; DOI=10.1104/pp.110.157057;
RA Falcone Ferreyra M.L., Pezza A., Biarc J., Burlingame A.L., Casati P.;
RT "Plant L10 ribosomal proteins have different roles during development and
RT translation under ultraviolet-B stress.";
RL Plant Physiol. 153:1878-1894(2010).
RN [9]
RP LACK OF INDUCTION BY UV-B, AND MISCELLANEOUS.
RX PubMed=20855946; DOI=10.4161/psb.5.10.12758;
RA Ferreyra M.L., Biarc J., Burlingame A.L., Casati P.;
RT "Arabidopsis L10 ribosomal proteins in UV-B responses.";
RL Plant Signal. Behav. 5:1222-1225(2010).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=23886624; DOI=10.1104/pp.113.223222;
RA Falcone Ferreyra M.L., Casadevall R., Luciani M.D., Pezza A., Casati P.;
RT "New evidence for differential roles of l10 ribosomal proteins from
RT Arabidopsis.";
RL Plant Physiol. 163:378-391(2013).
RN [11]
RP FUNCTION, INTERACTION WITH LIMYB, AND TISSUE SPECIFICITY.
RX PubMed=25707794; DOI=10.1038/nature14171;
RA Zorzatto C., Machado J.P., Lopes K.V., Nascimento K.J., Pereira W.A.,
RA Brustolini O.J., Reis P.A., Calil I.P., Deguchi M., Sachetto-Martins G.,
RA Gouveia B.C., Loriato V.A., Silva M.A., Silva F.F., Santos A.A., Chory J.,
RA Fontes E.P.;
RT "NIK1-mediated translation suppression functions as a plant antiviral
RT immunity mechanism.";
RL Nature 520:679-682(2015).
CC -!- FUNCTION: Ribosomal protein involved in translational regulation
CC (PubMed:18694459). Contribute to general translation under UV-B stress
CC (PubMed:20516338, PubMed:23886624). Involved in the NIK1-mediated
CC defense response to geminivirus infection (PubMed:18789471,
CC PubMed:19112492). Acts coordinately with LIMYB as a transcriptional
CC repressor (PubMed:25707794). {ECO:0000269|PubMed:18694459,
CC ECO:0000269|PubMed:18789471, ECO:0000269|PubMed:19112492,
CC ECO:0000269|PubMed:20516338, ECO:0000269|PubMed:23886624,
CC ECO:0000269|PubMed:25707794}.
CC -!- SUBUNIT: Component of the small ribosomal subunit (PubMed:20516338).
CC Mature ribosomes consist of a small (40S) and a large (60S) subunit.
CC The 40S subunit contains about 33 different proteins and 1 molecule of
CC RNA (18S). The 60S subunit contains about 49 different proteins and 3
CC molecules of RNA (25S, 5.8S and 5S) (By similarity). Interacts with
CC NIK1 (PubMed:18789471, PubMed:19112492). Interacts with LIMYB
CC (PubMed:25707794). {ECO:0000250, ECO:0000269|PubMed:18789471,
CC ECO:0000269|PubMed:19112492, ECO:0000269|PubMed:20516338,
CC ECO:0000269|PubMed:25707794}.
CC -!- INTERACTION:
CC Q93VT9; Q9FFJ8: LIMYB; NbExp=6; IntAct=EBI-6391356, EBI-16146054;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19112492,
CC ECO:0000269|PubMed:23886624}. Nucleus {ECO:0000269|PubMed:19112492,
CC ECO:0000269|PubMed:23886624}. Note=Phosphorylation by NIK1 relocates
CC the cytosolic protein to the nucleus. {ECO:0000269|PubMed:19112492}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q93VT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q93VT9-2; Sequence=VSP_057660;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with the highest expression in flowers
CC (PubMed:18694459). Expressed in seedlings, leaves, roots, stems and
CC flowers (PubMed:25707794). Expressed in young leaves, mostly in
CC dividing cells and in the hydathodes, in the root tips and lateral root
CC primordia, in pistils, anthers, and pollen grains, and in developing
CC seeds (PubMed:23886624). {ECO:0000269|PubMed:18694459,
CC ECO:0000269|PubMed:23886624, ECO:0000269|PubMed:25707794}.
CC -!- DEVELOPMENTAL STAGE: Expressed in tissues with active division, with
CC the highest levels in 3-week-old leaves and lowest levels in senescent
CC leaves. {ECO:0000269|PubMed:20516338}.
CC -!- INDUCTION: Not regulated by UV-B. {ECO:0000269|PubMed:20516338,
CC ECO:0000269|PubMed:20855946}.
CC -!- PTM: Phosphorylated by NIK1 and NIK2 in vitro.
CC {ECO:0000269|PubMed:18789471, ECO:0000269|PubMed:19112492}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, when heterozygous
CC (PubMed:20516338). Lethality in the female gametophyte, when homozygous
CC (PubMed:18694459, PubMed:20516338). Enhanced susceptibility to
CC geminivirus infection (PubMed:18789471, PubMed:19112492).
CC {ECO:0000269|PubMed:18694459, ECO:0000269|PubMed:18789471,
CC ECO:0000269|PubMed:19112492, ECO:0000269|PubMed:20516338}.
CC -!- MISCELLANEOUS: Under UV-B conditions, RPL10 proteins interact with
CC several nuclear proteins, including RBG7 (glycine-rich RNA binding
CC protein), which has an important role in mediating innate immune
CC response to pathogens, and BTR1 that specifically binds to tomato
CC mosaic virus (ToMV) genomic RNA and inhibits the local spread of virus.
CC {ECO:0000269|PubMed:20855946}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL16 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK55705.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC012188; AAF43932.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29145.1; -; Genomic_DNA.
DR EMBL; AF428286; AAL16118.1; -; mRNA.
DR EMBL; AF428470; AAL16239.1; -; mRNA.
DR EMBL; AY045866; AAK76540.1; -; mRNA.
DR EMBL; AY113989; AAM45037.1; -; mRNA.
DR EMBL; BT000679; AAN31825.1; -; mRNA.
DR EMBL; AF378902; AAK55705.1; ALT_INIT; mRNA.
DR EMBL; AY050482; AAK91495.1; -; mRNA.
DR PIR; E86277; E86277.
DR RefSeq; NP_563945.2; NM_101298.3. [Q93VT9-1]
DR AlphaFoldDB; Q93VT9; -.
DR SMR; Q93VT9; -.
DR BioGRID; 23233; 144.
DR DIP; DIP-61516N; -.
DR IntAct; Q93VT9; 6.
DR STRING; 3702.AT1G14320.1; -.
DR MoonProt; Q93VT9; -.
DR MetOSite; Q93VT9; -.
DR PaxDb; Q93VT9; -.
DR PRIDE; Q93VT9; -.
DR EnsemblPlants; AT1G14320.1; AT1G14320.1; AT1G14320. [Q93VT9-1]
DR GeneID; 837993; -.
DR Gramene; AT1G14320.1; AT1G14320.1; AT1G14320. [Q93VT9-1]
DR KEGG; ath:AT1G14320; -.
DR Araport; AT1G14320; -.
DR TAIR; locus:2012612; AT1G14320.
DR eggNOG; KOG0857; Eukaryota.
DR HOGENOM; CLU_084051_0_0_1; -.
DR InParanoid; Q93VT9; -.
DR OMA; MSVRAKE; -.
DR PhylomeDB; Q93VT9; -.
DR PRO; PR:Q93VT9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93VT9; baseline and differential.
DR Genevisible; Q93VT9; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
DR GO; GO:0005840; C:ribosome; IPI:TAIR.
DR GO; GO:0005773; C:vacuole; 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:0071493; P:cellular response to UV-B; IMP:TAIR.
DR GO; GO:0051607; P:defense response to virus; IMP:CAFA.
DR GO; GO:0032502; P:developmental process; IMP:TAIR.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; TAS:TAIR.
DR CDD; cd01433; Ribosomal_L16_L10e; 1.
DR Gene3D; 3.90.1170.10; -; 1.
DR InterPro; IPR001197; Ribosomal_L10e.
DR InterPro; IPR016180; Ribosomal_L10e/L16.
DR InterPro; IPR036920; Ribosomal_L10e/L16_sf.
DR InterPro; IPR018255; Ribosomal_L10e_CS.
DR PANTHER; PTHR11726; PTHR11726; 1.
DR Pfam; PF00252; Ribosomal_L16; 1.
DR PIRSF; PIRSF005590; Ribosomal_L10; 1.
DR SUPFAM; SSF54686; SSF54686; 1.
DR TIGRFAMs; TIGR00279; uL16_euk_arch; 1.
DR PROSITE; PS01257; RIBOSOMAL_L10E; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein; Plant defense;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..220
FT /note="60S ribosomal protein L10-1"
FT /id="PRO_0000239930"
FT VAR_SEQ 77..133
FT /note="Missing (in isoform 2)"
FT /id="VSP_057660"
FT MUTAGEN 14
FT /note="G->S: In sac52-d; suppresses the dwarf phenotype of
FT the acl5 mutant."
FT /evidence="ECO:0000269|PubMed:18694459"
SQ SEQUENCE 220 AA; 24917 MW; 88A1C3DCB4F4D0F9 CRC64;
MGRRPARCYR QIKGKPYPKS RYCRGVPDPK IRIYDVGMKR KGVDEFPFCV HLVSWEKENV
SSEALEAARI ACNKYMVKSA GKDAFHLRIR VHPFHVLRIN KMLSCAGADR LQTGMRGAFG
KALGTCARVA IGQVLLSVRC KDAHGHHAQE ALRRAKFKFP GRQKIIVSRK WGFTKFNRAD
FTKLRQEKRV VPDGVNAKFL SCHGPLANRQ PGSAFLPAHY
