RL112_ARATH
ID RL112_ARATH Reviewed; 182 AA.
AC P42794; P42796; Q42195; Q8LD47; Q9LXT1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 25-MAY-2022, entry version 166.
DE RecName: Full=60S ribosomal protein L11-2;
DE AltName: Full=L16;
GN Name=RPL11B; OrderedLocusNames=At3g58700; ORFNames=T20N10_50;
GN and
GN Name=RPL11C; Synonyms=RPL16B; OrderedLocusNames=At4g18730;
GN ORFNames=F28A21.140;
GN and
GN Name=RPL11D; OrderedLocusNames=At5g45775; ORFNames=MRA19.26, MRA19_21;
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 / MRNA] (RPL11C).
RC STRAIN=cv. Columbia, and 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] (RPL11C).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (RPL11B).
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (RPL11D).
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (RPL11C AND RPL11D; 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (RPL11B; RPL11C AND RPL11D; ISOFORM
RP 2).
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-85 (RPL11D; ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Shoot;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [9]
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).
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.
CC {ECO:0000250|UniProtKB:P0C0W9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C0W9}. Cytoplasm
CC {ECO:0000250|UniProtKB:P0C0W9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P42794-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P42794-2; Sequence=VSP_008901;
CC -!- MISCELLANEOUS: There are four genes for RPL11 in A.thaliana.
CC -!- MISCELLANEOUS: [Isoform 2]: Shown to be produced only by RPL11D so far.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA57396.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA82293.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X81798; CAA57394.1; -; mRNA.
DR EMBL; X81800; CAA57396.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL035526; CAB37458.1; -; Genomic_DNA.
DR EMBL; AL161549; CAB78875.1; -; Genomic_DNA.
DR EMBL; AL353032; CAB88287.1; -; Genomic_DNA.
DR EMBL; AB012245; BAB09220.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79819.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84082.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95296.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95297.1; -; Genomic_DNA.
DR EMBL; AF326876; AAG41458.1; -; mRNA.
DR EMBL; AF339697; AAK00379.1; -; mRNA.
DR EMBL; AY039570; AAK62625.1; -; mRNA.
DR EMBL; AY129487; AAM91073.1; -; mRNA.
DR EMBL; AF385722; AAK60313.1; -; mRNA.
DR EMBL; AY078021; AAL77722.1; -; mRNA.
DR EMBL; AY085232; AAM62465.1; -; mRNA.
DR EMBL; AY086211; AAM64289.1; -; mRNA.
DR EMBL; AY086300; AAM64372.1; -; mRNA.
DR EMBL; Z29034; CAA82293.1; ALT_FRAME; mRNA.
DR PIR; S49033; S49033.
DR PIR; T49153; T49153.
DR RefSeq; NP_191429.1; NM_115732.4. [P42794-1]
DR RefSeq; NP_567563.1; NM_117989.4. [P42794-1]
DR RefSeq; NP_568649.2; NM_123945.4. [P42794-1]
DR RefSeq; NP_851137.1; NM_180806.1. [P42794-2]
DR AlphaFoldDB; P42794; -.
DR SMR; P42794; -.
DR BioGRID; 10354; 110.
DR BioGRID; 12900; 109.
DR BioGRID; 19866; 109.
DR STRING; 3702.AT3G58700.1; -.
DR iPTMnet; P42794; -.
DR PaxDb; P42794; -.
DR PRIDE; P42794; -.
DR ProteomicsDB; 226296; -. [P42794-1]
DR EnsemblPlants; AT3G58700.1; AT3G58700.1; AT3G58700. [P42794-1]
DR EnsemblPlants; AT4G18730.1; AT4G18730.1; AT4G18730. [P42794-1]
DR EnsemblPlants; AT5G45775.1; AT5G45775.1; AT5G45775. [P42794-2]
DR EnsemblPlants; AT5G45775.2; AT5G45775.2; AT5G45775. [P42794-1]
DR GeneID; 825039; -.
DR GeneID; 827607; -.
DR GeneID; 834617; -.
DR Gramene; AT3G58700.1; AT3G58700.1; AT3G58700. [P42794-1]
DR Gramene; AT4G18730.1; AT4G18730.1; AT4G18730. [P42794-1]
DR Gramene; AT5G45775.1; AT5G45775.1; AT5G45775. [P42794-2]
DR Gramene; AT5G45775.2; AT5G45775.2; AT5G45775. [P42794-1]
DR KEGG; ath:AT3G58700; -.
DR KEGG; ath:AT4G18730; -.
DR KEGG; ath:AT5G45775; -.
DR Araport; AT3G58700; -.
DR Araport; AT4G18730; -.
DR Araport; AT5G45775; -.
DR TAIR; locus:2099024; AT3G58700.
DR TAIR; locus:2124112; AT4G18730.
DR TAIR; locus:505006673; AT5G45775.
DR eggNOG; KOG0397; Eukaryota.
DR HOGENOM; CLU_061015_3_0_1; -.
DR InParanoid; P42794; -.
DR OMA; HELRICK; -.
DR PhylomeDB; P42794; -.
DR PRO; PR:P42794; -.
DR Proteomes; UP000006548; Chromosome 3.
DR Proteomes; UP000006548; Chromosome 4.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P42794; baseline and differential.
DR Genevisible; P42794; AT.
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:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; 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 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Nucleus; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..182
FT /note="60S ribosomal protein L11-2"
FT /id="PRO_0000125096"
FT VAR_SEQ 1..10
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_008901"
FT CONFLICT 46
FT /note="Missing (in Ref. 8; CAA82293)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="D -> E (in Ref. 1; CAA57394)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 20861 MW; 03FD62DF294B921B CRC64;
MASEKKLSNP MRDIKVQKLV LNISVGESGD RLTRASKVLE QLSGQTPVFS KARYTVRSFG
IRRNEKIACY VTVRGEKAMQ LLESGLKVKE YELLRRNFSD TGCFGFGIQE HIDLGIKYDP
STGIYGMDFY VVLERPGYRV ARRRRCKTRV GIQHRVTKDD AMKWFQVKYE GVILNKSQNI
TG
