ID   RLA0_CAEEL              Reviewed;         312 AA.
AC   Q93572;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=60S acidic ribosomal protein P0;
GN   Name=rla-0 {ECO:0000312|WormBase:F25H2.10};
GN   Synonyms=rpa-0 {ECO:0000312|WormBase:F25H2.10};
GN   ORFNames=F25H2.10 {ECO:0000312|WormBase:F25H2.10};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-16.
RC   STRAIN=Bristol N2;
RX   PubMed=9150941; DOI=10.1002/elps.1150180337;
RA   Bini L., Heid H., Liberatori S., Geier G., Pallini V., Zwilling R.;
RT   "Two-dimensional gel electrophoresis of Caenorhabditis elegans homogenates
RT   and identification of protein spots by microsequencing.";
RL   Electrophoresis 18:557-562(1997).
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.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC       {ECO:0000305}.
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DR   EMBL; Z79754; CAB02098.1; -; Genomic_DNA.
DR   PIR; T21351; T21351.
DR   RefSeq; NP_492766.1; NM_060365.7.
DR   AlphaFoldDB; Q93572; -.
DR   SMR; Q93572; -.
DR   BioGRID; 38357; 108.
DR   DIP; DIP-26018N; -.
DR   IntAct; Q93572; 4.
DR   STRING; 6239.F25H2.10; -.
DR   World-2DPAGE; 0011:Q93572; -.
DR   World-2DPAGE; 0020:Q93572; -.
DR   EPD; Q93572; -.
DR   PaxDb; Q93572; -.
DR   PeptideAtlas; Q93572; -.
DR   EnsemblMetazoa; F25H2.10.1; F25H2.10.1; WBGene00004408.
DR   GeneID; 172943; -.
DR   KEGG; cel:CELE_F25H2.10; -.
DR   UCSC; F25H2.10.1; c. elegans.
DR   CTD; 172943; -.
DR   WormBase; F25H2.10; CE09655; WBGene00004408; rla-0.
DR   eggNOG; KOG0815; Eukaryota.
DR   GeneTree; ENSGT00390000017839; -.
DR   HOGENOM; CLU_053173_1_1_1; -.
DR   InParanoid; Q93572; -.
DR   OMA; MAHVAEW; -.
DR   OrthoDB; 1102823at2759; -.
DR   PhylomeDB; Q93572; -.
DR   Reactome; R-CEL-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-CEL-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-CEL-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-CEL-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-CEL-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-CEL-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-CEL-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   SignaLink; Q93572; -.
DR   PRO; PR:Q93572; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00004408; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
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   Direct protein sequencing; Phosphoprotein; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9150941"
FT   CHAIN           2..312
FT                   /note="60S acidic ribosomal protein P0"
FT                   /id="PRO_0000154766"
FT   REGION          287..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   312 AA;  33774 MW;  0D90B15C30BDCB30 CRC64;
     MVREDRSTWK ANYFTKLVEL FEEYPKCLLV GVDNVGSKQM QEIRQAMRGH AEILMGKNTM
     IRKALRGHLG KNPSLEKLLP HIVENVGFVF TKEDLGEIRS KLLENRKGAP AKAGAIAPCD
     VKLPPQNTGM GPEKTSFFQA LQIPTKIARG TIEILNDVHL IKEGDKVGAS ESALLNMLGV
     TPFSYGLVVR QVYDDGTLYT PEVLDMTTEE LRKRFLSGVR NVASVSLAVN YPTLASVAHS
     LANGLQNMLG VAAVTDVSFK EAETIKAFIA DPSKFAAAAP AAAAAPAAAA PAAKKEEPKE
     ESDDDMGFGL FD