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   03-AUG-2022, entry version 103.
DE   RecName: 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   -!- 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.ENSFCAP00000023603; -.
DR   Ensembl; ENSFCAT00000003327; ENSFCAP00000003066; ENSFCAG00000003327.
DR   GeneID; 100169965; -.
DR   GeneID; 101088757; -.
DR   KEGG; fca:100169965; -.
DR   KEGG; fca:101088757; -.
DR   CTD; 6152; -.
DR   VGNC; VGNC:102833; RPL24.
DR   eggNOG; KOG1722; Eukaryota.
DR   GeneTree; ENSGT00950000183105; -.
DR   HOGENOM; CLU_106411_1_0_1; -.
DR   InParanoid; Q66WF5; -.
DR   OMA; PGKGKIY; -.
DR   OrthoDB; 1502432at2759; -.
DR   Proteomes; UP000011712; Chromosome C2.
DR   Bgee; ENSFCAG00000003327; Expressed in uterus and 10 other tissues.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0042788; C:polysomal ribosome; IEA:Ensembl.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
DR   GO; GO:0003729; F:mRNA 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:0010458; P:exit from mitosis; IEA:Ensembl.
DR   GO; GO:0021554; P:optic nerve development; IEA:Ensembl.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IEA:Ensembl.
DR   CDD; cd00472; Ribosomal_L24e_L24; 1.
DR   Gene3D; 2.30.170.20; -; 1.
DR   InterPro; IPR038630; L24e/L24_sf.
DR   InterPro; IPR000988; Ribosomal_L24e-rel.
DR   InterPro; IPR023442; Ribosomal_L24e_CS.
DR   InterPro; IPR011017; TRASH_dom.
DR   PANTHER; PTHR10792; PTHR10792; 1.
DR   Pfam; PF01246; Ribosomal_L24e; 1.
DR   SMART; SM00746; TRASH; 1.
DR   PROSITE; PS01073; RIBOSOMAL_L24E; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT   CHAIN           1..157
FT                   /note="60S ribosomal protein L24"
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         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