RLA0_RAT
ID RLA0_RAT Reviewed; 317 AA.
AC P19945;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=60S acidic ribosomal protein P0;
DE AltName: Full=60S ribosomal protein L10E;
GN Name=Rplp0; Synonyms=Arbp;
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 [MRNA].
RC TISSUE=Myeloid;
RA Loedemel O., Molven A., Houge G.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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).
RN [4]
RP PROTEIN SEQUENCE OF 17-38; 84-92; 135-146 AND 150-162, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with APEX1. Interacts with
CC FMR1. {ECO:0000250|UniProtKB:P05388}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P05388}. Cytoplasm
CC {ECO:0000250|UniProtKB:P05388}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P05388}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000305}.
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DR EMBL; X15096; CAA33199.1; -; mRNA.
DR EMBL; Z29530; CAA82647.1; -; mRNA.
DR EMBL; BC062028; AAH62028.1; -; mRNA.
DR PIR; S08021; R5RT10.
DR RefSeq; NP_071797.1; NM_022402.2.
DR AlphaFoldDB; P19945; -.
DR SMR; P19945; -.
DR BioGRID; 249011; 7.
DR IntAct; P19945; 10.
DR MINT; P19945; -.
DR STRING; 10116.ENSRNOP00000001518; -.
DR iPTMnet; P19945; -.
DR PhosphoSitePlus; P19945; -.
DR jPOST; P19945; -.
DR PaxDb; P19945; -.
DR PRIDE; P19945; -.
DR Ensembl; ENSRNOT00000001518; ENSRNOP00000001518; ENSRNOG00000001148.
DR GeneID; 64205; -.
DR KEGG; rno:64205; -.
DR CTD; 6175; -.
DR RGD; 621247; Rplp0.
DR eggNOG; KOG0815; Eukaryota.
DR GeneTree; ENSGT00390000017839; -.
DR HOGENOM; CLU_053173_1_1_1; -.
DR InParanoid; P19945; -.
DR OMA; MAHVAEW; -.
DR OrthoDB; 1102823at2759; -.
DR PhylomeDB; P19945; -.
DR TreeFam; TF300849; -.
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:P19945; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001148; Expressed in spleen and 19 other tissues.
DR Genevisible; P19945; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:RGD.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; ISO:RGD.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IDA: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:0071353; P:cellular response to interleukin-4; ISO:RGD.
DR GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; 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:0007595; P:lactation; IEP:RGD.
DR GO; GO:0010269; P:response to selenium ion; IEP:RGD.
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 Cytoplasm; Direct protein sequencing; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..317
FT /note="60S acidic ribosomal protein P0"
FT /id="PRO_0000154761"
FT REGION 294..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14869"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05388"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05388"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05388"
FT CONFLICT 281
FT /note="V -> L (in Ref. 1; CAA33199)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="A -> L (in Ref. 1; CAA33199)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="Missing (in Ref. 1; CAA33199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 34215 MW; 7B842971C0E027EC CRC64;
MPREDRATWK SNYFLKIIQL LDDYPKCFIV GADNVGSKQM QQIRMSLRGK AVVLMGKNTM
MRKAIRGHLE NNPALEKLLP HIRGNVGFVF TKEDLTEIRD MLLANKVPAA ARAGAIAPCE
VTVPAQNTGL GPEKTSFFQA LGITTKISRG TIEILSDVQL IKTGDKVGAS EATLLNMLNI
SPFSFGLIIQ QVFDNGSIYS PEVLDITEQA LHTRFLEGVR NVASVCLQIG YPTVASVPHS
IINGYKRVLA LSVETDYTFP LAEKVKAFLA DPSAFAAAAP VAAATTAAPA AAAAPAKVEA
KEESEESDED MGFGLFD
