RL111_ARATH
ID RL111_ARATH Reviewed; 182 AA.
AC P42795; Q9SJI2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=60S ribosomal protein L11-1 {ECO:0000303|PubMed:11598216};
DE AltName: Full=L16A {ECO:0000303|PubMed:7655508};
GN Name=RPL11A {ECO:0000303|PubMed:11598216};
GN Synonyms=RPL16A {ECO:0000303|PubMed:7655508};
GN OrderedLocusNames=At2g42740 {ECO:0000312|Araport:AT2G42740};
GN ORFNames=F7D19.26 {ECO:0000312|EMBL:AAD21733.1};
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 [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7655508; DOI=10.1046/j.1365-313x.1995.08010065.x;
RA Williams M.E., Sussex I.M.;
RT "Developmental regulation of ribosomal protein L16 genes in Arabidopsis
RT thaliana.";
RL Plant J. 8:65-76(1995).
RN [2]
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 [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] OF 11-182.
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 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 INTERACTION WITH DEK3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=25387881; DOI=10.1105/tpc.114.129254;
RA Waidmann S., Kusenda B., Mayerhofer J., Mechtler K., Jonak C.;
RT "A DEK domain-containing protein modulates chromatin structure and function
RT in Arabidopsis.";
RL Plant Cell 26:4328-4344(2014).
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. {ECO:0000250|UniProtKB:P0C0W9}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (By similarity).
CC Interacts with DEK3 (PubMed:25387881). {ECO:0000250|UniProtKB:P0C0W9,
CC ECO:0000269|PubMed:25387881}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C0W9}. Cytoplasm
CC {ECO:0000250|UniProtKB:P0C0W9}.
CC -!- MISCELLANEOUS: There are four genes for RPL11 in A.thaliana.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD21733.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X81799; CAA57395.1; -; Genomic_DNA.
DR EMBL; AC006931; AAD21733.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10163.1; -; Genomic_DNA.
DR EMBL; AY074636; AAL69452.1; -; mRNA.
DR PIR; F84857; F84857.
DR RefSeq; NP_850376.2; NM_180045.4.
DR AlphaFoldDB; P42795; -.
DR SMR; P42795; -.
DR BioGRID; 4211; 119.
DR IntAct; P42795; 5.
DR STRING; 3702.AT2G42740.1; -.
DR iPTMnet; P42795; -.
DR PaxDb; P42795; -.
DR PRIDE; P42795; -.
DR ProteomicsDB; 226381; -.
DR EnsemblPlants; AT2G42740.1; AT2G42740.1; AT2G42740.
DR GeneID; 818874; -.
DR Gramene; AT2G42740.1; AT2G42740.1; AT2G42740.
DR KEGG; ath:AT2G42740; -.
DR Araport; AT2G42740; -.
DR TAIR; locus:2052432; AT2G42740.
DR eggNOG; KOG0397; Eukaryota.
DR HOGENOM; CLU_061015_3_0_1; -.
DR InParanoid; P42795; -.
DR OMA; MDFYCIM; -.
DR OrthoDB; 1340833at2759; -.
DR PhylomeDB; P42795; -.
DR PRO; PR:P42795; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P42795; baseline and differential.
DR Genevisible; P42795; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0006412; P:translation; TAS:TAIR.
DR Gene3D; 3.30.1440.10; -; 1.
DR InterPro; IPR002132; Ribosomal_L5.
DR InterPro; IPR031309; Ribosomal_L5_C.
DR InterPro; IPR020929; Ribosomal_L5_CS.
DR InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR InterPro; IPR031310; Ribosomal_L5_N.
DR PANTHER; PTHR11994; PTHR11994; 1.
DR Pfam; PF00281; Ribosomal_L5; 1.
DR Pfam; PF00673; Ribosomal_L5_C; 1.
DR PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR SUPFAM; SSF55282; SSF55282; 1.
DR PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..182
FT /note="60S ribosomal protein L11-1"
FT /id="PRO_0000125095"
FT CONFLICT 117
FT /note="K -> R (in Ref. 1; CAA57395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 20831 MW; 03FD7F69F23B921B CRC64;
MASEKKLSNP MRDIKVQKLV LNISVGESGD RLTRASKVLE QLSGQTPVFS KARYTVRSFG
IRRNEKIACY VTVRGEKAMQ LLESGLKVKE YELLRRNFSD TGCFGFGIQE HIDLGIKYDP
STGIYGMDFY VVLERPGYRV ARRRRCKARV GIQHRVTKDD AMKWFQVKYE GVILNKSQNI
TG
