ID RL24_FELCA Reviewed; 157 AA.
AC Q66WF5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Large ribosomal subunit protein eL24 {ECO:0000305};
DE AltName: Full=60S ribosomal protein L24;
DE AltName: Full=Ribosomal protein L30;
GN Name=RPL24;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Pathak S., Pisipati S., Kapil S.;
RT "Felis catus ribosomal protein L30 mRNA.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. {ECO:0000250|UniProtKB:P83731}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P83731}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P83731}.
CC -!- PTM: Mono-ADP-ribosylation at Glu-4 by PARP16 inhibits polysome
CC assembly and mRNA loading, thereby inhibiting protein translation.
CC {ECO:0000250|UniProtKB:P83731}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family.
CC {ECO:0000305}.
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DR EMBL; AY700577; AAU06859.1; -; mRNA.
DR RefSeq; NP_001122313.1; NM_001128841.1.
DR RefSeq; XP_011281487.1; XM_011283185.2.
DR AlphaFoldDB; Q66WF5; -.
DR SMR; Q66WF5; -.
DR STRING; 9685.ENSFCAP00000003066; -.
DR PaxDb; 9685-ENSFCAP00000023603; -.
DR Ensembl; ENSFCAT00000003327.6; ENSFCAP00000003066.4; ENSFCAG00000003327.6.
DR GeneID; 100169965; -.
DR KEGG; fca:100169965; -.
DR VGNC; VGNC:102833; RPL24.
DR eggNOG; KOG1722; Eukaryota.
DR GeneTree; ENSGT00950000183105; -.
DR HOGENOM; CLU_106411_1_0_1; -.
DR InParanoid; Q66WF5; -.
DR OMA; IAWTQVF; -.
DR OrthoDB; 178748at2759; -.
DR Proteomes; UP000011712; Chromosome C2.
DR Bgee; ENSFCAG00000003327; Expressed in uterus and 10 other cell types or tissues.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; ISS:UniProtKB.
DR CDD; cd00472; Ribosomal_L24e_L24; 1.
DR Gene3D; 6.10.250.1270; -; 1.
DR Gene3D; 2.30.170.20; Ribosomal protein L24e; 1.
DR InterPro; IPR038630; L24e/L24_sf.
DR InterPro; IPR000988; Ribosomal_eL24-rel.
DR InterPro; IPR023442; Ribosomal_eL24_CS.
DR InterPro; IPR011017; TRASH_dom.
DR PANTHER; PTHR10792; 60S RIBOSOMAL PROTEIN L24; 1.
DR PANTHER; PTHR10792:SF44; 60S RIBOSOMAL PROTEIN L24; 1.
DR Pfam; PF01246; Ribosomal_L24e; 1.
DR SMART; SM00746; TRASH; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS01073; RIBOSOMAL_L24E; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ADP-ribosylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..157
FT /note="Large ribosomal subunit protein eL24"
FT /id="PRO_0000136866"
FT REGION 106..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT MOD_RES 27
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT MOD_RES 83
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT MOD_RES 93
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT MOD_RES 131
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BP67"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT CROSSLNK 2
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P83731"
SQ SEQUENCE 157 AA; 17779 MW; 1D48EEB7C0652574 CRC64;
MKVELCSFSG YKIYPGHGRR YARTDGKVFQ FLNAKCESAF LSKRNPRQIN WTVLYRRKHK
KGQSEEIQKK RTRRAVKFQR AITGASLADI MAKRNQKPEV RKAQREQAIR AAKEAKKAKQ
ASKKTAMAAA KAPTKAAPKQ KIVKPVKVSA PRVGGKR
//
