RL51_ARATH
ID RL51_ARATH Reviewed; 301 AA.
AC Q8LBI1; B9DHP6; Q940R7;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=60S ribosomal protein L5-1 {ECO:0000303|PubMed:12711688};
DE Short=Ribosomal protein L5 A {ECO:0000303|PubMed:11598216};
DE AltName: Full=Protein ASYMMETRIC LEAVES1/2 ENHANCER 6 {ECO:0000303|PubMed:18305007};
DE AltName: Full=Protein OLIGOCELLULA 5 {ECO:0000303|PubMed:19392710};
DE AltName: Full=Protein PIGGYBACK 3 {ECO:0000303|PubMed:18305008};
GN Name=RPL5A {ECO:0000303|PubMed:11598216};
GN Synonyms=AE6 {ECO:0000303|PubMed:18305007},
GN ATL5 {ECO:0000303|PubMed:12711688}, OLI5 {ECO:0000303|PubMed:19392710},
GN PGY3 {ECO:0000303|PubMed:18305008};
GN OrderedLocusNames=At3g25520 {ECO:0000312|Araport:AT3G25520};
GN ORFNames=MWL2.17 {ECO:0000312|EMBL:AB025639};
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], AND SUBCELLULAR LOCATION.
RX PubMed=12711688; DOI=10.1093/nar/gkg335;
RA Mathieu O., Yukawa Y., Prieto J.-L., Vaillant I., Sugiura M., Tourmente S.;
RT "Identification and characterization of transcription factor IIIA and
RT ribosomal protein L5 from Arabidopsis thaliana.";
RL Nucleic Acids Res. 31:2424-2433(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-301.
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18305008; DOI=10.1242/dev.016469;
RA Pinon V., Etchells J.P., Rossignol P., Collier S.A., Arroyo J.M.,
RA Martienssen R.A., Byrne M.E.;
RT "Three PIGGYBACK genes that specifically influence leaf patterning encode
RT ribosomal proteins.";
RL Development 135:1315-1324(2008).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=18305007; DOI=10.1242/dev.017913;
RA Yao Y., Ling Q., Wang H., Huang H.;
RT "Ribosomal proteins promote leaf adaxial identity.";
RL Development 135:1325-1334(2008).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19392710; DOI=10.1111/j.1365-313x.2009.03886.x;
RA Fujikura U., Horiguchi G., Ponce M.R., Micol J.L., Tsukaya H.;
RT "Coordination of cell proliferation and cell expansion mediated by
RT ribosome-related processes in the leaves of Arabidopsis thaliana.";
RL Plant J. 59:499-508(2009).
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. Seems involved in the regulation of cell proliferation
CC (PubMed:19392710). Essential in leaf polarity establishment, probably
CC having a role for translation in leaf dorsoventral patterning to
CC specify leaf adaxial identity (PubMed:18305008, PubMed:18305007).
CC {ECO:0000250|UniProtKB:P26321, ECO:0000269|PubMed:18305007,
CC ECO:0000269|PubMed:18305008, ECO:0000269|PubMed:19392710}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (LSU).
CC {ECO:0000250|UniProtKB:P26321}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18305007}. Nucleus
CC {ECO:0000269|PubMed:18305007}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:18305007}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:18305007}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8LBI1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, stems, leaves,
CC inflorescences and siliques. {ECO:0000269|PubMed:18305007}.
CC -!- DEVELOPMENTAL STAGE: Detected in the embryo and leaf primordia at
CC earlier developmental stages (PubMed:18305007). In reproductive organs,
CC expressed in the inflorescence meristem, floral primordia and four
CC types of young floral organs (PubMed:18305007).
CC {ECO:0000269|PubMed:18305007}.
CC -!- DISRUPTION PHENOTYPE: Moderate reduction in cell number
CC (PubMed:19392710). Slightly pointed leaves and prominent marginal
CC serrations (PubMed:18305008). Delayed leaf growth and abnormal leaf
CC patterning, with the abaxial mesophyll features appearing in the
CC adaxial mesophyll domain (PubMed:18305007). More proximal vein
CC branching in the petiole and reduced number of small veins at later
CC leaf developmental stages (PubMed:18305007). Abnormal inflorescences
CC terminating early and producing several secondary inflorescences
CC (PubMed:18305007). Double mutant ae6-1 as2-101 exhibits an increased
CC number of lotus- and needle-like leaves, rough adaxial surface of
CC expanded leaves (PubMed:18305007). Double mutants oli2 oli5 have
CC further reduced cell number but exhibit also excessive postmitotic cell
CC enlargement in leaves (compensation phenotype) (PubMed:19392710). Plant
CC missing both OLI5 and GIF1/AN3 have a strong compensation phenotype
CC (PubMed:19392710). The double mutant as1 pgy3 exhibits narrow and
CC elongated leaves with adaxial ectopic lamina (PubMed:18305008). The
CC double mutant ae6 as1/2 produces severe abaxialized leaves
CC (PubMed:18305007). {ECO:0000269|PubMed:18305007,
CC ECO:0000269|PubMed:18305008, ECO:0000269|PubMed:19392710}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC {ECO:0000305}.
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DR EMBL; AY186611; AAO73340.1; -; mRNA.
DR EMBL; AB025639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE77019.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65929.1; -; Genomic_DNA.
DR EMBL; AY054161; AAL06822.1; -; mRNA.
DR EMBL; AY065103; AAL38279.1; -; mRNA.
DR EMBL; AY081701; AAM10263.1; -; mRNA.
DR EMBL; AY136319; AAM96985.1; -; mRNA.
DR EMBL; BT000411; AAN15730.1; -; mRNA.
DR EMBL; BT002427; AAO00787.1; -; mRNA.
DR EMBL; BT008705; AAP42718.1; -; mRNA.
DR EMBL; AY087197; AAM64753.1; -; mRNA.
DR EMBL; AK317600; BAH20263.1; -; mRNA.
DR RefSeq; NP_001327862.1; NM_001338753.1. [Q8LBI1-1]
DR RefSeq; NP_566767.1; NM_113448.5. [Q8LBI1-1]
DR AlphaFoldDB; Q8LBI1; -.
DR SMR; Q8LBI1; -.
DR BioGRID; 7469; 111.
DR IntAct; Q8LBI1; 7.
DR STRING; 3702.AT3G25520.1; -.
DR iPTMnet; Q8LBI1; -.
DR MetOSite; Q8LBI1; -.
DR PaxDb; Q8LBI1; -.
DR PRIDE; Q8LBI1; -.
DR ProteomicsDB; 236489; -. [Q8LBI1-1]
DR EnsemblPlants; AT3G25520.1; AT3G25520.1; AT3G25520. [Q8LBI1-1]
DR EnsemblPlants; AT3G25520.3; AT3G25520.3; AT3G25520. [Q8LBI1-1]
DR GeneID; 822138; -.
DR Gramene; AT3G25520.1; AT3G25520.1; AT3G25520. [Q8LBI1-1]
DR Gramene; AT3G25520.3; AT3G25520.3; AT3G25520. [Q8LBI1-1]
DR KEGG; ath:AT3G25520; -.
DR Araport; AT3G25520; -.
DR TAIR; locus:2094508; AT3G25520.
DR eggNOG; KOG0875; Eukaryota.
DR HOGENOM; CLU_056222_1_0_1; -.
DR InParanoid; Q8LBI1; -.
DR OMA; IYEAQVE; -.
DR PhylomeDB; Q8LBI1; -.
DR PRO; PR:Q8LBI1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LBI1; baseline and differential.
DR Genevisible; Q8LBI1; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0008097; F:5S rRNA binding; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0009955; P:adaxial/abaxial pattern specification; IMP:UniProtKB.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0009965; P:leaf morphogenesis; IMP:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; TAS:TAIR.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0010015; P:root morphogenesis; IMP:TAIR.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR HAMAP; MF_01337_A; Ribosomal_L18_A; 1.
DR InterPro; IPR005485; Rbsml_L5_euk/L18_arc.
DR InterPro; IPR025607; Rbsml_L5e_C.
DR PANTHER; PTHR23410; PTHR23410; 1.
DR Pfam; PF14204; Ribosomal_L18_c; 1.
DR Pfam; PF17144; Ribosomal_L5e; 1.
DR PRINTS; PR00058; RIBOSOMALL5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Nucleus;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..301
FT /note="60S ribosomal protein L5-1"
FT /id="PRO_0000239919"
FT CONFLICT 202
FT /note="H -> D (in Ref. 6; BAH20263)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="K -> R (in Ref. 5; AAM64753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 34358 MW; 9485CE63AB6ECD58 CRC64;
MVFVKSTKSN AYFKRYQVKF RRRRDGKTDY RARIRLINQD KNKYNTPKYR FVVRFTNKDI
VAQIVSASIA GDIVKASAYA HELPQYGLTV GLTNYAAAYC TGLLLARRVL KMLEMDDEYE
GNVEATGEDF SVEPTDSRRP FRALLDVGLI RTTTGNRVFG ALKGALDGGL DIPHSDKRFA
GFHKENKQLD AEIHRNYIYG GHVSNYMKLL GEDEPEKLQT HFSAYIKKGV EAESIEELYK
KVHAAIRADP NPKKTVKPAP KQHKRYNLKK LTYEERKNKL IERVKALNGA GGDDDDEDDE
E
