RLA0_PIG
ID RLA0_PIG Reviewed; 318 AA.
AC Q29214; A5X2G5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=60S acidic ribosomal protein P0;
DE AltName: Full=60S ribosomal protein L10E;
GN Name=RPLP0;
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 [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=17469782; DOI=10.1016/s1673-8527(07)60011-3;
RA Wu X., Yang S.L., Zhu Z.M., Feng S.T., Li K.;
RT "Characterization of the full-length cDNA, chromosomal localization, and
RT polymorphism of the porcine RPLP0 gene.";
RL J. Genet. Genomics 34:104-108(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-93.
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
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; DQ316319; ABC47963.1; -; mRNA.
DR EMBL; F14800; CAA23264.1; -; mRNA.
DR RefSeq; NP_001092068.1; NM_001098598.1.
DR PDB; 3J7P; EM; 3.50 A; q=5-206.
DR PDBsum; 3J7P; -.
DR AlphaFoldDB; Q29214; -.
DR SMR; Q29214; -.
DR PeptideAtlas; Q29214; -.
DR PRIDE; Q29214; -.
DR Ensembl; ENSSSCT00025065433; ENSSSCP00025027911; ENSSSCG00025048049.
DR Ensembl; ENSSSCT00030026295; ENSSSCP00030011744; ENSSSCG00030019041.
DR Ensembl; ENSSSCT00035049606; ENSSSCP00035019844; ENSSSCG00035037418.
DR Ensembl; ENSSSCT00035049620; ENSSSCP00035019848; ENSSSCG00035037418.
DR Ensembl; ENSSSCT00045006865; ENSSSCP00045004695; ENSSSCG00045004115.
DR Ensembl; ENSSSCT00050019212; ENSSSCP00050007979; ENSSSCG00050014204.
DR Ensembl; ENSSSCT00055026729; ENSSSCP00055021251; ENSSSCG00055013468.
DR Ensembl; ENSSSCT00060072858; ENSSSCP00060031420; ENSSSCG00060053490.
DR Ensembl; ENSSSCT00065040083; ENSSSCP00065016936; ENSSSCG00065029708.
DR Ensembl; ENSSSCT00070013836; ENSSSCP00070011404; ENSSSCG00070007168.
DR Ensembl; ENSSSCT00070013856; ENSSSCP00070011422; ENSSSCG00070007168.
DR GeneID; 100049695; -.
DR KEGG; ssc:100049695; -.
DR CTD; 6175; -.
DR InParanoid; Q29214; -.
DR OMA; MAHVAEW; -.
DR OrthoDB; 1102823at2759; -.
DR Reactome; R-SSC-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SSC-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-SSC-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-SSC-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-SSC-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SSC-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 14.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0070180; F:large ribosomal subunit rRNA 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: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 3D-structure; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..318
FT /note="60S acidic ribosomal protein P0"
FT /id="PRO_0000154760"
FT REGION 298..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 8
FT /note="T -> P (in Ref. 2; CAA23264)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="E -> G (in Ref. 2; CAA23264)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="H -> Q (in Ref. 2; CAA23264)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 34359 MW; 8B3DA384D704E723 CRC64;
MPREDRATWK SNYFLKIIQL LDDYPKCFIV GADNVGSKQM QQIRMSLRGK AVVLMGKNTM
MRKAIRGHLE NNPALEKLLP HIRGNVGFVF TKEDLTEIRD MLLANKVPAA ARAGAIAPCE
VTVPAQNTGL GPEKTSFFQA LGITTKISRG TIEILSDVQL IKTGDKVGAS EATLLNMLNI
SPFSFGLIIQ QVFDNGSIYN PEVLDITEET LHSRFLEGVR NVASVCLQIG YPTVASVPHS
IINGYKRVLA LSVETDYTFP LAEKVKAFLA DPSAFVAAAP VAAATTAAPA AAAAAPAKVE
AKEESEESDE DMGFGLFD
