ID   RLA1_RAT                Reviewed;         114 AA.
AC   P19944;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=60S acidic ribosomal protein P1;
GN   Name=Rplp1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=1742361; DOI=10.1016/0300-9084(91)90127-m;
RA   Wool I.G., Chan Y.-L., Glueck A., Suzuki K.;
RT   "The primary structure of rat ribosomal proteins P0, P1, and P2 and a
RT   proposal for a uniform nomenclature for mammalian and yeast ribosomal
RT   proteins.";
RL   Biochimie 73:861-870(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plays an important role in the elongation step of protein
CC       synthesis.
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; X15097; CAA33200.1; -; mRNA.
DR   EMBL; BC058151; AAH58151.1; -; mRNA.
DR   PIR; S08022; R5RT12.
DR   RefSeq; NP_001007605.1; NM_001007604.2.
DR   RefSeq; XP_003752993.1; XM_003752945.2.
DR   RefSeq; XP_017456174.1; XM_017600685.1.
DR   RefSeq; XP_017456175.1; XM_017600686.1.
DR   AlphaFoldDB; P19944; -.
DR   BMRB; P19944; -.
DR   SMR; P19944; -.
DR   BioGRID; 1199657; 1.
DR   BioGRID; 250822; 3.
DR   IntAct; P19944; 2.
DR   STRING; 10116.ENSRNOP00000018820; -.
DR   iPTMnet; P19944; -.
DR   PhosphoSitePlus; P19944; -.
DR   jPOST; P19944; -.
DR   PaxDb; P19944; -.
DR   PRIDE; P19944; -.
DR   Ensembl; ENSRNOT00000018820; ENSRNOP00000018820; ENSRNOG00000013874.
DR   Ensembl; ENSRNOT00000107660; ENSRNOP00000087435; ENSRNOG00000063015.
DR   Ensembl; ENSRNOT00000111700; ENSRNOP00000092643; ENSRNOG00000063015.
DR   GeneID; 100360522; -.
DR   GeneID; 140661; -.
DR   KEGG; rno:140661; -.
DR   UCSC; RGD:621774; rat.
DR   CTD; 6176; -.
DR   RGD; 621774; Rplp1.
DR   eggNOG; KOG1762; Eukaryota.
DR   GeneTree; ENSGT00550000074698; -.
DR   HOGENOM; CLU_114656_1_2_1; -.
DR   InParanoid; P19944; -.
DR   OMA; TDVEPIW; -.
DR   OrthoDB; 1633925at2759; -.
DR   PhylomeDB; P19944; -.
DR   TreeFam; TF312932; -.
DR   Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-RNO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-RNO-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-RNO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:P19944; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000013874; Expressed in thymus and 19 other tissues.
DR   Genevisible; P19944; RN.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:RGD.
DR   GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR   GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IPI:RGD.
DR   GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
DR   GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR   GO; GO:1904401; P:cellular response to Thyroid stimulating hormone; IEP:RGD.
DR   GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR   GO; GO:0045727; P:positive regulation of translation; IDA:RGD.
DR   GO; GO:0006417; P:regulation of translation; ISO:RGD.
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.
PE   3: Inferred from homology;
KW   Acetylation; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW   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_0000157688"
FT   REGION          69..114
FT                   /note="Disordered"
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"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05386"
SQ   SEQUENCE   114 AA;  11498 MW;  27596FB8DCA06D99 CRC64;
     MASVSELACI YSALILHDDE VTVTEDKINA LIKAAGVNVE PFWPGLFAKA LANVNIGSLI
     CNVGAGGPAP AAGAAPAGGP APSAAAAPAE EKKVEAKKEE SEESEDDMGF GLFD