RK24_ARATH
ID RK24_ARATH Reviewed; 198 AA.
AC P92959; Q9FIU4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=50S ribosomal protein L24, chloroplastic;
DE AltName: Full=CL24;
DE AltName: Full=Protein SUPPRESSOR OF VARIEGATION 8 {ECO:0000303|PubMed:22900828};
DE Flags: Precursor;
GN Name=RPL24; Synonyms=SVR8 {ECO:0000303|PubMed:22900828};
GN OrderedLocusNames=At5g54600; ORFNames=MRB17.10;
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].
RC STRAIN=cv. Landsberg erecta;
RA Galichet A., Bach T.J.;
RT "Isolation of a cDNA from Arabidopsis thaliana encoding a plastid ribosomal
RT protein.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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 SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21923745; DOI=10.1111/j.1365-313x.2011.04791.x;
RA Tiller N., Weingartner M., Thiele W., Maximova E., Schoettler M.A.,
RA Bock R.;
RT "The plastid-specific ribosomal proteins of Arabidopsis thaliana can be
RT divided into non-essential proteins and genuine ribosomal proteins.";
RL Plant J. 69:302-316(2012).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22900828; DOI=10.1111/tpj.12000;
RA Romani I., Tadini L., Rossi F., Masiero S., Pribil M., Jahns P., Kater M.,
RA Leister D., Pesaresi P.;
RT "Versatile roles of Arabidopsis plastid ribosomal proteins in plant growth
RT and development.";
RL Plant J. 72:922-934(2012).
CC -!- FUNCTION: One of two assembly initiator proteins, it binds directly to
CC the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC subunit (By similarity). Required for optimal plastid performance in
CC terms of photosynthesis and growth. Required for the translation of
CC plastid mRNAs. Plays a critical role in biosynthesis of thylakoid
CC membrane proteins encoded by chloroplast genes (PubMed:22900828).
CC {ECO:0000250, ECO:0000269|PubMed:22900828}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21923745}.
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=P92959-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Reduced plant size and pale green leaves.
CC {ECO:0000269|PubMed:22900828}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC {ECO:0000305}.
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DR EMBL; Y09635; CAA70851.1; -; mRNA.
DR EMBL; AB016879; BAB09339.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96516.1; -; Genomic_DNA.
DR EMBL; BT001990; AAN72001.1; -; mRNA.
DR EMBL; BT006573; AAP21381.1; -; mRNA.
DR EMBL; AY086810; AAM63859.1; -; mRNA.
DR RefSeq; NP_851190.1; NM_180859.2. [P92959-1]
DR AlphaFoldDB; P92959; -.
DR SMR; P92959; -.
DR BioGRID; 20793; 12.
DR STRING; 3702.AT5G54600.1; -.
DR iPTMnet; P92959; -.
DR PaxDb; P92959; -.
DR PRIDE; P92959; -.
DR ProteomicsDB; 234808; -. [P92959-1]
DR EnsemblPlants; AT5G54600.1; AT5G54600.1; AT5G54600. [P92959-1]
DR GeneID; 835549; -.
DR Gramene; AT5G54600.1; AT5G54600.1; AT5G54600. [P92959-1]
DR KEGG; ath:AT5G54600; -.
DR Araport; AT5G54600; -.
DR TAIR; locus:2172154; AT5G54600.
DR eggNOG; KOG1708; Eukaryota.
DR HOGENOM; CLU_093315_1_0_1; -.
DR InParanoid; P92959; -.
DR OMA; ITKIYKH; -.
DR PhylomeDB; P92959; -.
DR PRO; PR:P92959; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P92959; baseline and differential.
DR Genevisible; P92959; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0032544; P:plastid translation; IMP:TAIR.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd06089; KOW_RPL26; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR HAMAP; MF_01326_B; Ribosomal_L24_B; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041988; KOW_RPL26/RPL24.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR003256; Ribosomal_L24.
DR InterPro; IPR005825; Ribosomal_L24/26_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR12903; PTHR12903; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF17136; ribosomal_L24; 1.
DR SMART; SM00739; KOW; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR TIGRFAMs; TIGR01079; rplX_bact; 1.
DR PROSITE; PS01108; RIBOSOMAL_L24; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chloroplast; Plastid; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..198
FT /note="50S ribosomal protein L24, chloroplastic"
FT /id="PRO_0000030489"
FT CONFLICT 147..148
FT /note="VV -> IL (in Ref. 1; CAA70851)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 21977 MW; 30B7DF233A1FA3FA CRC64;
MATMSALQSS FTSLSLSPSS SFLGQRLISP ISLSVTSPVK PAENPCLVLA KLKRWERKEC
KPNSLPILHK MHVKFGDTVK VISGRDKGKI GEVTKIFTHN STIVIKDVNL KTKHMKSREE
GEPGQIVKIE APIHSSNVML YSKEKDVVSR VGHKVLEDGQ KVRYLIKTGE LIDTIEKWKL
LKEAKDKETT QVAVTSAS
