ID   RLA1_MAIZE              Reviewed;         109 AA.
AC   P52855; O24414;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=60S acidic ribosomal protein P1;
DE   AltName: Full=L12;
GN   Name=RPP1A;
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. Wisconsin 22;
RA   Hamilton D.A., Turcich M.P., Bokhari-Riza A., Mascarenhas J.P.;
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-21.
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: Plays an important role in the elongation step of protein
CC       synthesis. {ECO:0000250}.
CC   -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC       {ECO:0000305}.
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DR   EMBL; U40147; AAA91168.1; -; mRNA.
DR   EMBL; U62752; AAB71079.1; -; mRNA.
DR   PIR; T02039; T02039.
DR   PIR; T02716; T02716.
DR   RefSeq; NP_001105701.1; NM_001112231.1.
DR   RefSeq; XP_008648318.1; XM_008650096.1.
DR   AlphaFoldDB; P52855; -.
DR   SMR; P52855; -.
DR   STRING; 4577.GRMZM2G032315_P01; -.
DR   PaxDb; P52855; -.
DR   GeneID; 542719; -.
DR   KEGG; zma:542719; -.
DR   MaizeGDB; 84941; -.
DR   eggNOG; KOG1762; Eukaryota.
DR   OrthoDB; 1633925at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P52855; baseline and differential.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:AgBase.
DR   GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:AgBase.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IBA:GO_Central.
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:0006414; P:translational elongation; IEA:InterPro.
DR   Gene3D; 1.10.10.1410; -; 1.
DR   HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR   InterPro; IPR038716; P1/P2_N_sf.
DR   InterPro; IPR027534; Ribosomal_L12/P1/P2.
DR   InterPro; IPR001859; T.cruzi_P2-like.
DR   PRINTS; PR00456; RIBOSOMALP2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Phosphoprotein; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..109
FT                   /note="60S acidic ribosomal protein P1"
FT                   /id="PRO_0000157699"
FT   REGION          85..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        9
FT                   /note="R -> T (in Ref. 2; AAB71079)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   109 AA;  11097 MW;  1BFEC8E34391F080 CRC64;
     MASGELACRY AALILSDDGI AITAEKIATI VKAANIKVES YWPALFAKLL EKRNVEDLIL
     SVGSGGGAAP VAAAAPAGGA AAAAAPAVEE KKEEAKEESD DDMGFSLFD