ID   RLA1_PIG                Reviewed;         114 AA.
AC   A1XQU7;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=60S acidic ribosomal protein P1;
GN   Name=RPLP1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Longissimus dorsi muscle;
RA   Cai G., Chen Y., Wang C., Li J., Peng G., Zhang H.;
RT   "Generation and analysis of cDNA sequences derived from a porcine skeletal
RT   muscle library.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in the elongation step of protein
CC       synthesis. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with RPLP2 at the lateral ribosomal stalk of the
CC       large ribosomal subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC       {ECO:0000305}.
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DR   EMBL; DQ629169; ABK55653.1; -; mRNA.
DR   RefSeq; NP_001123436.1; NM_001129964.1.
DR   AlphaFoldDB; A1XQU7; -.
DR   BMRB; A1XQU7; -.
DR   SMR; A1XQU7; -.
DR   STRING; 9823.ENSSSCP00000005345; -.
DR   GeneID; 100170119; -.
DR   CTD; 6176; -.
DR   eggNOG; KOG1762; Eukaryota.
DR   InParanoid; A1XQU7; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
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   3: Inferred from homology;
KW   Acetylation; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P05386"
FT   CHAIN           2..114
FT                   /note="60S acidic ribosomal protein P1"
FT                   /id="PRO_0000311175"
FT   REGION          67..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..89
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P05386"
SQ   SEQUENCE   114 AA;  11748 MW;  75D5F0089315D325 CRC64;
     MASVSELACI YSALILHDDE VTVPEDKINA LIKAAGVNVE PFWPGFFAKA LANVNIGSLI
     CNVGAGGPPP PAGAAPPGGP APPPPAAPAE EKKVEAKKEE FEESDDDMGF GFFD