ID   RLA0_BOVIN              Reviewed;         318 AA.
AC   Q95140; O18788; Q3T182; Q5E940;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 3.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=60S acidic ribosomal protein P0;
DE   AltName: Full=60S ribosomal protein L10E;
GN   Name=RPLP0;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-59.
RC   TISSUE=Adrenal cortex;
RA   Mandriota S.J., Pepper M.S.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 17-318.
RC   TISSUE=Aorta;
RA   Lileinsiek B., Rocha M., Umansky V., Benner A., Lin Y., Ziegler R.,
RA   Nawroth P.P., Schirrmacher V.;
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
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; BT021080; AAX09097.1; -; mRNA.
DR   EMBL; BC102074; AAI02075.1; -; mRNA.
DR   EMBL; U75275; AAB17671.1; -; mRNA.
DR   EMBL; AF013214; AAB65436.1; -; mRNA.
DR   RefSeq; NP_001012700.1; NM_001012682.1.
DR   AlphaFoldDB; Q95140; -.
DR   SMR; Q95140; -.
DR   IntAct; Q95140; 2.
DR   MINT; Q95140; -.
DR   STRING; 9913.ENSBTAP00000048183; -.
DR   PaxDb; Q95140; -.
DR   PeptideAtlas; Q95140; -.
DR   PRIDE; Q95140; -.
DR   GeneID; 286868; -.
DR   KEGG; bta:286868; -.
DR   CTD; 6175; -.
DR   eggNOG; KOG0815; Eukaryota.
DR   InParanoid; Q95140; -.
DR   OrthoDB; 1102823at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT   CHAIN           1..318
FT                   /note="60S acidic ribosomal protein P0"
FT                   /id="PRO_0000154757"
FT   REGION          293..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..318
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         305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05388"
FT   MOD_RES         308
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05388"
FT   CROSSLNK        298
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05388"
FT   CROSSLNK        298
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05388"
FT   CONFLICT        167
FT                   /note="V -> E (in Ref. 4; AAB65436)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        286
FT                   /note="A -> T (in Ref. 2; AAI02075)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   318 AA;  34371 MW;  8E3A9BB94094E723 CRC64;
     MPREDRATWK SNYFLKIIQL LDDYPKCFIV GADNVGSKQM QQIRMSLRGK AVVLMGKNTM
     MRKAIRGHLE NNPALEKLLP HIRGNVGFVF TKEDLTEIRD MLLANKVPAA ARAGAIAPCE
     VTVPAQNTGL GPEKTSFFQA LGITTKISRG TIEILSDVQL IKTGDKVGAS EATLLNMLNI
     SPFSFGLVIQ QVFDNGSIYN PEVLDITEET LHSRFLEGVR NVASVCLQIG YPTVASVPHS
     IINGYKRVLA LSVETDYTFP LAEKVKAFLA DPSAFVAAAP VAAAPAAAPA ATTAAPAKVE
     AKEESEESDE DMGFGLFD