RK21_SPIOL
ID RK21_SPIOL Reviewed; 256 AA.
AC P24613; A0A0K9RKM9;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=50S ribosomal protein L21, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=CL21;
DE AltName: Full=CS-L7;
DE AltName: Full=Chloroplastic large ribosomal subunit protein bL21c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=RPL21; ORFNames=SOVF_056040;
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], AND PROTEIN SEQUENCE OF 56-67.
RX PubMed=2076556; DOI=10.1007/bf00327027;
RA Martin W., Lagrange T., Li Y.F., Bisanz-Seyer C., Mache R.;
RT "Hypothesis for the evolutionary origin of the chloroplast ribosomal
RT protein L21 of spinach.";
RL Curr. Genet. 18:553-556(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 56-75.
RC STRAIN=cv. Alwaro;
RX PubMed=2398071; DOI=10.1016/s0021-9258(17)46277-6;
RA Smooker P.M., Kruft V., Subramanian A.R.;
RT "A ribosomal protein is encoded in the chloroplast DNA in a lower plant but
RT in the nucleus in angiosperms. Isolation of the spinach L21 protein and
RT cDNA clone with transit and an unusual repeat sequence.";
RL J. Biol. Chem. 265:16699-16703(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver;
RX PubMed=8455634; DOI=10.1128/mcb.13.4.2614-2622.1993;
RA Lagrange T., Franzetti B., Axelos M., Mache R., Lerbs-Mache S.;
RT "Structure and expression of the nuclear gene coding for the chloroplast
RT ribosomal protein L21: developmental regulation of a housekeeping gene by
RT alternative promoters.";
RL Mol. Cell. Biol. 13:2614-2622(1993).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 56-61, 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 [6]
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 [7]
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 [8]
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, ECO:0000269|PubMed:28007896}.
CC -!- MASS SPECTROMETRY: Mass=22763.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL21 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; X56691; CAA40019.1; -; mRNA.
DR EMBL; M57413; AAA34041.1; -; mRNA.
DR EMBL; M64682; AAA74715.1; -; Genomic_DNA.
DR EMBL; KQ139519; KNA20045.1; -; Genomic_DNA.
DR PIR; A48103; A48103.
DR PDB; 4V61; EM; 9.40 A; BT=1-256.
DR PDB; 5H1S; EM; 3.50 A; T=56-256.
DR PDB; 5MLC; EM; 3.90 A; T=1-256.
DR PDB; 5MMI; EM; 3.25 A; S=1-256.
DR PDB; 5MMM; EM; 3.40 A; S=1-256.
DR PDB; 5X8P; EM; 3.40 A; S=56-256.
DR PDB; 5X8T; EM; 3.30 A; S=56-256.
DR PDB; 6ERI; EM; 3.00 A; AR=72-236.
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; P24613; -.
DR SMR; P24613; -.
DR IntAct; P24613; 1.
DR STRING; 3562.P24613; -.
DR OrthoDB; 1586807at2759; -.
DR EvolutionaryTrace; P24613; -.
DR Proteomes; UP000054095; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR HAMAP; MF_01363; Ribosomal_L21; 1.
DR InterPro; IPR036164; L21-like_sf.
DR InterPro; IPR028909; L21p-like.
DR InterPro; IPR001787; Ribosomal_L21.
DR InterPro; IPR018258; Ribosomal_L21_CS.
DR PANTHER; PTHR21349; PTHR21349; 1.
DR Pfam; PF00829; Ribosomal_L21p; 1.
DR SUPFAM; SSF141091; SSF141091; 1.
DR TIGRFAMs; TIGR00061; L21; 1.
DR PROSITE; PS01169; RIBOSOMAL_L21; 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..55
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046,
FT ECO:0000269|PubMed:2076556, ECO:0000269|PubMed:2398071"
FT CHAIN 56..256
FT /note="50S ribosomal protein L21, chloroplastic"
FT /id="PRO_0000030481"
FT CONFLICT 252..256
FT /note="EAVPV -> VPV (in Ref. 4; KNA20045)"
FT /evidence="ECO:0000305"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 181..191
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 215..226
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 256 AA; 28408 MW; 3FD2BE241C42BC79 CRC64;
MASATLAFSC SSLCATLKLP QNLNPLLLNV PPLSKPFSGV VSPPSLSRLS LLPVAAKRRR
FQEIPEELKA EFEEFQRPPN QKPQLSDVLP DDFQAPEPGT PEYNDIINQF LPKKGPPPPR
EEIFAVVVIG SRQYIVIPGR WIYTQRLKGA TVNDKIVLNK VLLVGTKAST YIGTPIVTNA
AVHAVVEEQL LDDKVIVFKY KKKKNYRRNI GHRQPITRIK ITGITGYEDY PASTLEAEVE
AKEEAEAEAE AEAVPV
