RL131_ARATH
ID RL131_ARATH Reviewed; 206 AA.
AC P41127; Q42280; Q8LFC4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=60S ribosomal protein L13-1;
DE AltName: Full=Protein BBC1 homolog;
GN Name=RPL13B; Synonyms=BBC1; OrderedLocusNames=At3g49010;
GN ORFNames=T2J13.150;
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 DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=8163191; DOI=10.1016/0378-1119(94)90573-8;
RA Bertauche N., Leung J., Giraudat J.;
RT "Conservation of the human breast basic conserved 1 gene in the plant
RT kingdom: characterization of a cDNA clone from Arabidopsis thaliana.";
RL Gene 141:211-214(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [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 125-206.
RC STRAIN=cv. Columbia;
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 [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 TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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=P41127-1; Sequence=Displayed;
CC -!- DEVELOPMENTAL STAGE: Regulated during fruit maturation.
CC {ECO:0000269|PubMed:8163191}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL13 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X75162; CAA53005.1; -; mRNA.
DR EMBL; AL132967; CAB62009.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78482.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78483.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78484.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65192.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65193.1; -; Genomic_DNA.
DR EMBL; AF428384; AAL16152.1; -; mRNA.
DR EMBL; AY050854; AAK92791.1; -; mRNA.
DR EMBL; AY065137; AAL38313.1; -; mRNA.
DR EMBL; AY079381; AAL85112.1; -; mRNA.
DR EMBL; AY081595; AAM10157.1; -; mRNA.
DR EMBL; AY084928; AAM61490.1; -; mRNA.
DR EMBL; Z34257; CAA84015.1; -; mRNA.
DR PIR; S37271; S37271.
DR RefSeq; NP_001030831.1; NM_001035754.1. [P41127-1]
DR RefSeq; NP_001327179.1; NM_001339393.1. [P41127-1]
DR RefSeq; NP_001327180.1; NM_001339394.1. [P41127-1]
DR RefSeq; NP_190470.1; NM_114760.4. [P41127-1]
DR RefSeq; NP_850672.1; NM_180341.3. [P41127-1]
DR AlphaFoldDB; P41127; -.
DR SMR; P41127; -.
DR BioGRID; 9380; 135.
DR IntAct; P41127; 1.
DR STRING; 3702.AT3G49010.3; -.
DR iPTMnet; P41127; -.
DR PaxDb; P41127; -.
DR PRIDE; P41127; -.
DR ProteomicsDB; 226393; -. [P41127-1]
DR EnsemblPlants; AT3G49010.1; AT3G49010.1; AT3G49010. [P41127-1]
DR EnsemblPlants; AT3G49010.2; AT3G49010.2; AT3G49010. [P41127-1]
DR EnsemblPlants; AT3G49010.3; AT3G49010.3; AT3G49010. [P41127-1]
DR EnsemblPlants; AT3G49010.6; AT3G49010.6; AT3G49010. [P41127-1]
DR EnsemblPlants; AT3G49010.7; AT3G49010.7; AT3G49010. [P41127-1]
DR GeneID; 824062; -.
DR Gramene; AT3G49010.1; AT3G49010.1; AT3G49010. [P41127-1]
DR Gramene; AT3G49010.2; AT3G49010.2; AT3G49010. [P41127-1]
DR Gramene; AT3G49010.3; AT3G49010.3; AT3G49010. [P41127-1]
DR Gramene; AT3G49010.6; AT3G49010.6; AT3G49010. [P41127-1]
DR Gramene; AT3G49010.7; AT3G49010.7; AT3G49010. [P41127-1]
DR KEGG; ath:AT3G49010; -.
DR Araport; AT3G49010; -.
DR TAIR; locus:2101283; AT3G49010.
DR eggNOG; KOG3295; Eukaryota.
DR InParanoid; P41127; -.
DR OMA; NQQIPHN; -.
DR PhylomeDB; P41127; -.
DR PRO; PR:P41127; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P41127; baseline and differential.
DR Genevisible; P41127; 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:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR HAMAP; MF_00499; Ribosomal_L13e; 1.
DR InterPro; IPR001380; Ribosomal_L13e.
DR InterPro; IPR018256; Ribosomal_L13e_CS.
DR PANTHER; PTHR11722; PTHR11722; 1.
DR Pfam; PF01294; Ribosomal_L13e; 1.
DR PROSITE; PS01104; RIBOSOMAL_L13E; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..206
FT /note="60S ribosomal protein L13-1"
FT /id="PRO_0000192930"
FT REGION 185..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 125
FT /note="F -> S (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="K -> M (in Ref. 5; AAM61490)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="A -> V (in Ref. 6; CAA84015)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 206 AA; 23767 MW; C67BA5E5534114C2 CRC64;
MKHNNVIPNG HFKKHWQNYV KTWFNQPARK TRRRIARQKK AVKIFPRPTS GPLRPVVHGQ
TLKYNMKVRT GKGFTLEELK AAGIPKKLAP TIGIAVDHRR KNRSLEGLQT NVQRLKTYKT
KLVIFPRRAR KVKAGDSTPE ELANATQVQG DYLPIVREKP TMELVKLTSE MKSFKAFDKI
RLERTNKRHA GARAKRAAEA EKEEKK
