RLA0_MAIZE
ID RLA0_MAIZE Reviewed; 319 AA.
AC O24573;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=60S acidic ribosomal protein P0;
GN Name=RP-P0;
OS Zea mays (Maize).
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 [MRNA].
RC STRAIN=cv. A188;
RA Cordts S., Loerz H., Dresselhaus T.;
RT "A transcript encoding the large subunit acidic ribosomal protein P0 is
RT stored in unfertilized egg cells of maize.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-12, AND PHOSPHORYLATION.
RC STRAIN=cv. B73; TISSUE=Ear of corn;
RX PubMed=9276949; DOI=10.1104/pp.114.4.1293;
RA Bailey-Serres J., Vangala S., Szick K., Lee C.H.;
RT "Acidic phosphoprotein complex of the 60S ribosomal subunit of maize
RT seedling roots. Components and changes in response to flooding.";
RL Plant Physiol. 114:1293-1305(1997).
CC -!- FUNCTION: Ribosomal protein P0 is the functional equivalent of E.coli
CC protein L10.
CC -!- SUBUNIT: P0 forms a pentameric complex by interaction with dimers of P1
CC and P2. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:9276949}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000305}.
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DR EMBL; Y07959; CAA69256.1; -; mRNA.
DR PIR; T03944; T03944.
DR RefSeq; NP_001105482.1; NM_001112012.1.
DR AlphaFoldDB; O24573; -.
DR SMR; O24573; -.
DR STRING; 4577.GRMZM2G066460_P01; -.
DR PaxDb; O24573; -.
DR PRIDE; O24573; -.
DR GeneID; 542454; -.
DR eggNOG; KOG0815; Eukaryota.
DR OrthoDB; 1102823at2759; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; O24573; baseline and differential.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:AgBase.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:AgBase.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0034059; P:response to anoxia; IDA:AgBase.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR Gene3D; 3.30.70.1730; -; 1.
DR Gene3D; 3.90.105.20; -; 1.
DR InterPro; IPR030670; L10E_eukaryotes.
DR InterPro; IPR043141; Ribosomal_L10-like_sf.
DR InterPro; IPR001790; Ribosomal_L10P.
DR InterPro; IPR043164; RL10_insert_sf.
DR InterPro; IPR040637; RL10P_insert.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR Pfam; PF17777; RL10P_insert; 1.
DR PIRSF; PIRSF039087; L10E; 1.
DR SUPFAM; SSF160369; SSF160369; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9276949"
FT CHAIN 2..319
FT /note="60S acidic ribosomal protein P0"
FT /id="PRO_0000154780"
FT REGION 286..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..319
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 11
FT /note="K -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 34505 MW; AB111A7DE5700FA3 CRC64;
MAIKRTKAEK KIAYDKKLCS LLDEYTKVLI ALADNVGSKQ LQDIRRGLRG DSVVLMGKNT
LIRRCIKVYA EKTGNHTFDP LMDLLVGNVG LIFTKGDLKE VREEVAKYKV GAPARVGLVA
PVDVVVPPGN TGLDPSQTSF FQVLNIPTKI NKGTVEIITP VELIKKGEKV GSSESALLAK
LGIRPFSYGL QVTSVYEDGS VFSPEVLDLS EEDLIEKFAT GVSMVASLSL AISYPTLAAV
PHMFINGYKN VLAVAVETDY SYPHADKIKE YLKDPSKFAV AAPVAAGDSG ASAAPKEEEK
AAEPEEESDE EMGFSLFDD