RK2_MAIZE
ID RK2_MAIZE Reviewed; 273 AA.
AC P17788;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=50S ribosomal protein L2, chloroplastic;
GN Name=rpl2-A;
GN and
GN Name=rpl2-B;
OS Zea mays (Maize).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. FR9CMSSR37;
RX PubMed=2377464; DOI=10.1093/nar/18.14.4244;
RA Kavousi M., Giese K., Larrinua I.M., Subramanian A.R.;
RT "Nucleotide sequence and map positions of the duplicated gene for maize
RT (Zea mays) chloroplast ribosomal protein L2.";
RL Nucleic Acids Res. 18:4244-4244(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=7666415; DOI=10.1006/jmbi.1995.0460;
RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.;
RT "Complete sequence of the maize chloroplast genome: gene content, hotspots
RT of divergence and fine tuning of genetic information by transcript
RT editing.";
RL J. Mol. Biol. 251:614-628(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-150, AND RNA EDITING OF INITIATOR CODON.
RX PubMed=1653905; DOI=10.1038/353178a0;
RA Hoch B., Maier R.M., Appel K., Igloi G.L., Koessel H.;
RT "Editing of a chloroplast mRNA by creation of an initiation codon.";
RL Nature 353:178-180(1991).
RN [4]
RP RNA EDITING OF INITIATOR CODON.
RC TISSUE=Seedling;
RX PubMed=8252066; DOI=10.1046/j.1365-313x.1993.04040621.x;
RA Freyer R., Hoch B., Neckermann K., Maier R.M., Koessel H.;
RT "RNA editing in maize chloroplasts is a processing step independent of
RT splicing and cleavage to monocistronic mRNAs.";
RL Plant J. 4:621-629(1993).
RN [5]
RP EXPRESSION DURING GREENING.
RC STRAIN=cv. FR9cms X FR37;
RC TISSUE=Bundle sheath cell, Etiolated seedling, and Mesophyll cell;
RX PubMed=10430884; DOI=10.1073/pnas.96.16.8997;
RA Zhao Y.-Y., Xu T., Zucchi P., Bogorad L.;
RT "Subpopulations of chloroplast ribosomes change during photoregulated
RT development of Zea mays leaves: ribosomal proteins L2, L21, and L29.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8997-9002(1999).
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- DEVELOPMENTAL STAGE: Present in both bundle sheat and mesophyll cells
CC of etiolated seedlings, protein levels increase in bundle sheath cells
CC but not in mesophyll cells upon illumination.
CC -!- RNA EDITING: Modified_positions=1 {ECO:0000269|PubMed:1653905,
CC ECO:0000269|PubMed:8252066}; Note=The initiator methionine is created
CC by RNA editing.;
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000305}.
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DR EMBL; X53066; CAA37241.1; -; Genomic_DNA.
DR EMBL; X86563; CAA60329.1; -; Genomic_DNA.
DR EMBL; X86563; CAA60371.1; -; Genomic_DNA.
DR EMBL; X62070; CAA43983.1; -; mRNA.
DR PIR; S10500; R5ZM2.
DR RefSeq; NP_043066.1; NC_001666.2.
DR RefSeq; NP_043110.1; NC_001666.2.
DR AlphaFoldDB; P17788; -.
DR SMR; P17788; -.
DR STRING; 4577.GRMZM2G309193_P01; -.
DR PaxDb; P17788; -.
DR PRIDE; P17788; -.
DR GeneID; 845215; -.
DR GeneID; 845216; -.
DR KEGG; zma:845215; -.
DR KEGG; zma:845216; -.
DR MaizeGDB; 66413; -.
DR eggNOG; KOG0438; Eukaryota.
DR OrthoDB; 1156335at2759; -.
DR Proteomes; UP000007305; Chloroplast.
DR ExpressionAtlas; P17788; baseline.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR HAMAP; MF_01320_B; Ribosomal_L2_B; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR005880; Ribosomal_L2_bac/org-type.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR022671; Ribosomal_L2_CS.
DR InterPro; IPR014726; Ribosomal_L2_dom3.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR13691; PTHR13691; 1.
DR Pfam; PF00181; Ribosomal_L2; 1.
DR Pfam; PF03947; Ribosomal_L2_C; 1.
DR PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR SMART; SM01383; Ribosomal_L2; 1.
DR SMART; SM01382; Ribosomal_L2_C; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR01171; rplB_bact; 1.
DR PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Plastid; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA editing.
FT CHAIN 1..273
FT /note="50S ribosomal protein L2, chloroplastic"
FT /id="PRO_0000129681"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..273
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 273 AA; 30065 MW; BA65197231EA3CA0 CRC64;
MAKHLYKTPI PSTRKGTVDR QVKSNPRNKL IHGRHRCGKG RNARGIITAR HRGGGHKRLY
RKIDFRRNQK DISGRIITIE YDPNRNAYIC LIHYGDGEKR YILHPRGAII GDTIVSGTKV
PISMGNALPL TDMPLGTAIH NIEITRGRGG QLARAAGAVA KLIAKEGKLA TLRLPSGEVR
LVSQNCLATV GQVGNVGVNQ KSLGRAGSKC WLGKRPVVRG VVMNPVDHPH GGGEGKAPIG
RKKPTTPWGY PALGRRTRKR KKYSDSFILR RRK