RK24_SPIOL
ID RK24_SPIOL Reviewed; 192 AA.
AC P27683; A0A0K9QFU9; Q53WU0;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=50S ribosomal protein L24, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=CL24;
DE AltName: Full=Chloroplastic large ribosomal subunit protein uL24c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=RPL24; ORFNames=SOVF_183870;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1889743; DOI=10.1016/0378-1119(91)90266-e;
RA Carol P., Li Y.F., Mache R.;
RT "Conservation and evolution of the nucleus-encoded and chloroplast-specific
RT ribosomal proteins in pea and spinach.";
RL Gene 103:139-145(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Li Y., Zhou D.X., Seyer P., Massenet O., Dorne A.M., Mache R.;
RT "Analysis of two full length cDNAs coding for chloroplast precursor
RT ribosomal proteins homologous to the E. coli L12 and L24 ribosomal proteins
RT respectively.";
RL Submitted (OCT-1988) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Viroflay; TISSUE=Leaf;
RX PubMed=24352233; DOI=10.1038/nature12817;
RA Dohm J.C., Minoche A.E., Holtgraewe D., Capella-Gutierrez S.,
RA Zakrzewski F., Tafer H., Rupp O., Soerensen T.R., Stracke R., Reinhardt R.,
RA Goesmann A., Kraft T., Schulz B., Stadler P.F., Schmidt T., Gabaldon T.,
RA Lehrach H., Weisshaar B., Himmelbauer H.;
RT "The genome of the recently domesticated crop plant sugar beet (Beta
RT vulgaris).";
RL Nature 505:546-549(2014).
RN [4]
RP PROTEIN SEQUENCE OF 48-56, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RC STRAIN=cv. Alwaro; TISSUE=Leaf;
RX PubMed=10874046; DOI=10.1074/jbc.m005012200;
RA Yamaguchi K., Subramanian A.R.;
RT "The plastid ribosomal proteins. Identification of all the proteins in the
RT 50S subunit of an organelle ribosome (chloroplast).";
RL J. Biol. Chem. 275:28466-28482(2000).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.4 ANGSTROMS).
RX PubMed=18042701; DOI=10.1073/pnas.0709856104;
RA Sharma M.R., Wilson D.N., Datta P.P., Barat C., Schluenzen F., Fucini P.,
RA Agrawal R.K.;
RT "Cryo-EM study of the spinach chloroplast ribosome reveals the structural
RT and functional roles of plastid-specific ribosomal proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19315-19320(2007).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS).
RX PubMed=27762343; DOI=10.1038/srep35793;
RA Ahmed T., Yin Z., Bhushan S.;
RT "Cryo-EM structure of the large subunit of the spinach chloroplast
RT ribosome.";
RL Sci. Rep. 6:35793-35793(2016).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.25 ANGSTROMS), SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=28007896; DOI=10.15252/embj.201695959;
RA Bieri P., Leibundgut M., Saurer M., Boehringer D., Ban N.;
RT "The complete structure of the chloroplast 70S ribosome in complex with
RT translation factor pY.";
RL EMBO J. 36:475-486(2017).
CC -!- FUNCTION: Component of the chloroplast ribosome (chloro-ribosome), a
CC dedicated translation machinery responsible for the synthesis of
CC chloroplast genome-encoded proteins, including proteins of the
CC transcription and translation machinery and components of the
CC photosynthetic apparatus. {ECO:0000305|PubMed:10874046,
CC ECO:0000305|PubMed:28007896}.
CC -!- SUBUNIT: Component of the chloroplast large ribosomal subunit (LSU).
CC Mature 70S chloroplast ribosomes of higher plants consist of a small
CC (30S) and a large (50S) subunit. The 30S small subunit contains 1
CC molecule of ribosomal RNA (16S rRNA) and 24 different proteins. The 50S
CC large subunit contains 3 rRNA molecules (23S, 5S and 4.5S rRNA) and 33
CC different proteins. {ECO:0000269|PubMed:10874046,
CC ECO:0000269|PubMed:28007896}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:10874046}.
CC -!- MASS SPECTROMETRY: Mass=16425.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC {ECO:0000305}.
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DR EMBL; M58522; AAA34042.1; -; mRNA.
DR EMBL; X13154; CAA31552.1; -; mRNA.
DR EMBL; KQ185264; KNA06132.1; -; Genomic_DNA.
DR PIR; JH0585; JH0585.
DR PDB; 4V61; EM; 9.40 A; BW=1-192.
DR PDB; 5H1S; EM; 3.50 A; W=48-192.
DR PDB; 5MLC; EM; 3.90 A; W=1-192.
DR PDB; 5MMI; EM; 3.25 A; V=1-192.
DR PDB; 5MMM; EM; 3.40 A; V=1-192.
DR PDB; 5X8P; EM; 3.40 A; V=48-192.
DR PDB; 5X8T; EM; 3.30 A; V=48-192.
DR PDB; 6ERI; EM; 3.00 A; AU=49-175.
DR PDBsum; 4V61; -.
DR PDBsum; 5H1S; -.
DR PDBsum; 5MLC; -.
DR PDBsum; 5MMI; -.
DR PDBsum; 5MMM; -.
DR PDBsum; 5X8P; -.
DR PDBsum; 5X8T; -.
DR PDBsum; 6ERI; -.
DR AlphaFoldDB; P27683; -.
DR SMR; P27683; -.
DR IntAct; P27683; 1.
DR STRING; 3562.P27683; -.
DR EvolutionaryTrace; P27683; -.
DR Proteomes; UP000054095; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
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 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Plastid;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046"
FT CHAIN 48..192
FT /note="50S ribosomal protein L24, chloroplastic"
FT /id="PRO_0000030491"
FT CONFLICT 5..6
FT /note="AA -> V (in Ref. 1; AAA34042 and 2; CAA31552)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="M -> R (in Ref. 1; AAA34042 and 2; CAA31552)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="L -> F (in Ref. 1; AAA34042 and 2; CAA31552)"
FT /evidence="ECO:0000305"
FT CONFLICT 138..139
FT /note="YS -> IL (in Ref. 1; AAA34042 and 2; CAA31552)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="S -> D (in Ref. 1; AAA34042 and 2; CAA31552)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="G -> V (in Ref. 1; AAA34042 and 2; CAA31552)"
FT /evidence="ECO:0000305"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:5X8T"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5X8T"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 105..127
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 192 AA; 21377 MW; 7615B885AFADF1FE CRC64;
MAAMAALQSS FTSLSLSSNS FLGQRLFPSP TTLQVKTEGH SPCLIVMRIK RWERKDCKPN
SLPKLHKMHV KVGDTVKVIS GGEKGKIGEI SKIHKHNSTV IIKDLNLKTK HVKSKEEGEQ
GQIIKIEAAI HSSNVMLYSK EQEVASRVGH KILEDGRKVR YLIKTGEIVD TPDRWKEIQN
KKESETAVAV AA
