RL122_ARATH
ID RL122_ARATH Reviewed; 166 AA.
AC Q9LFH5;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=60S ribosomal protein L12-2;
DE AltName: Full=ABI1-binding protein 11;
GN Name=RPL12B; Synonyms=ABIP11; OrderedLocusNames=At3g53430;
GN ORFNames=F4P12_130;
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=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 [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].
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 INTERACTION WITH ABI1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19874541; DOI=10.1111/j.1365-313x.2009.04054.x;
RA Nishimura N., Sarkeshik A., Nito K., Park S.-Y., Wang A., Carvalho P.C.,
RA Lee S., Caddell D.F., Cutler S.R., Chory J., Yates J.R., Schroeder J.I.;
RT "PYR/PYL/RCAR family members are major in-vivo ABI1 protein phosphatase 2C-
RT interacting proteins in Arabidopsis.";
RL Plant J. 61:290-299(2010).
CC -!- FUNCTION: Binds directly to 26S ribosomal RNA. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ABI1. {ECO:0000269|PubMed:19874541}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC {ECO:0000305}.
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DR EMBL; AL132966; CAB67650.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79085.1; -; Genomic_DNA.
DR EMBL; AY140102; AAM98243.1; -; mRNA.
DR EMBL; BT002590; AAO00950.1; -; mRNA.
DR PIR; T45883; T45883.
DR RefSeq; NP_190911.1; NM_115203.3.
DR AlphaFoldDB; Q9LFH5; -.
DR SMR; Q9LFH5; -.
DR BioGRID; 9828; 64.
DR IntAct; Q9LFH5; 1.
DR STRING; 3702.AT3G53430.1; -.
DR PaxDb; Q9LFH5; -.
DR PRIDE; Q9LFH5; -.
DR ProteomicsDB; 236193; -.
DR EnsemblPlants; AT3G53430.1; AT3G53430.1; AT3G53430.
DR GeneID; 824511; -.
DR Gramene; AT3G53430.1; AT3G53430.1; AT3G53430.
DR KEGG; ath:AT3G53430; -.
DR Araport; AT3G53430; -.
DR TAIR; locus:2084036; AT3G53430.
DR eggNOG; KOG0886; Eukaryota.
DR HOGENOM; CLU_074237_5_0_1; -.
DR OMA; DINSGAY; -.
DR OrthoDB; 1279477at2759; -.
DR PhylomeDB; Q9LFH5; -.
DR PRO; PR:Q9LFH5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LFH5; baseline and differential.
DR Genevisible; Q9LFH5; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; HDA:TAIR.
DR GO; GO:0015934; C:large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd00349; Ribosomal_L11; 1.
DR Gene3D; 1.10.10.250; -; 1.
DR Gene3D; 3.30.1550.10; -; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1.
DR InterPro; IPR000911; Ribosomal_L11/L12.
DR InterPro; IPR036796; Ribosomal_L11/L12_N_sf.
DR InterPro; IPR020783; Ribosomal_L11_C.
DR InterPro; IPR036769; Ribosomal_L11_C_sf.
DR InterPro; IPR020785; Ribosomal_L11_CS.
DR InterPro; IPR020784; Ribosomal_L11_N.
DR PANTHER; PTHR11661; PTHR11661; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF46906; SSF46906; 1.
DR SUPFAM; SSF54747; SSF54747; 1.
DR PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..166
FT /note="60S ribosomal protein L12-2"
FT /id="PRO_0000240128"
SQ SEQUENCE 166 AA; 17970 MW; 226DFC60EE38DF81 CRC64;
MPPKLDPSQI VDVYVRVTGG EVGAASSLAP KIGPLGLAPK KIGEDIAKET AKEWKGLRVT
VKLTVQNRQA KVTVVPSAAA LVIKALKEPE RDRKKVKNIK HNGNISFDDV TEIARIMRPR
SIAKELSGTV REILGTCVSV GCTVDGKDPK DLQQEIQEGE IEIPEN