RL23A_BOVIN
ID RL23A_BOVIN Reviewed; 156 AA.
AC Q24JY1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=60S ribosomal protein L23a;
GN Name=RPL23A;
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].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) 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. Binds a specific region on the 26S rRNA. May
CC promote p53/TP53 degradation possibly through the stimulation of MDM2-
CC mediated TP53 polyubiquitination. {ECO:0000250|UniProtKB:P62750}.
CC -!- SUBUNIT: Component of the large ribosomal subunit. Interacts with LYAR
CC and GNL2. Interacts with MDM2; this interaction may promote MDM2-
CC mediated p53/TP53 polyubiquitination. Directly interacts (via BIB
CC domain) with IPO5, IPO7, KPNB1 and TNPO1; these interactions are
CC involved in RPL23A nuclear import for the assembly of ribosomal
CC subunits. Interacts with IPO8. {ECO:0000250|UniProtKB:P62750}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62750}. Nucleus
CC {ECO:0000250|UniProtKB:P62750}. Note=Although RPL23A is functional
CC within the cytoplasm, the assembly of ribosomal subunits occurs in the
CC nucleus. RPL23A nuclear import is mediated by IPO5/RanBP5, IPO7/RanBP7,
CC KPNB1/importin-beta or TPNO1/Trn. {ECO:0000250|UniProtKB:P62750}.
CC -!- DOMAIN: The N-terminal beta-like import receptor binding (BIB) domain
CC mediates interaction with IPO5, IPO7, KPNB1 and TNPO1.
CC {ECO:0000250|UniProtKB:P62750}.
CC -!- PTM: N-terminus is methylated by METTL11A/NTM1.
CC {ECO:0000250|UniProtKB:P62751}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:P62751}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC {ECO:0000305}.
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DR EMBL; BC114200; AAI14201.1; -; mRNA.
DR RefSeq; NP_001039423.1; NM_001045958.2.
DR AlphaFoldDB; Q24JY1; -.
DR SMR; Q24JY1; -.
DR STRING; 9913.ENSBTAP00000030092; -.
DR PaxDb; Q24JY1; -.
DR PeptideAtlas; Q24JY1; -.
DR PRIDE; Q24JY1; -.
DR GeneID; 507168; -.
DR KEGG; bta:507168; -.
DR CTD; 6147; -.
DR eggNOG; KOG1751; Eukaryota.
DR HOGENOM; CLU_037562_0_2_1; -.
DR InParanoid; Q24JY1; -.
DR OrthoDB; 1436090at2759; -.
DR TreeFam; TF314116; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:1904841; F:TORC2 complex binding; ISS:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_01369_A; Ribosomal_L23_A; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR019985; Ribosomal_L23.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR InterPro; IPR001014; Ribosomal_L23/L25_CS.
DR InterPro; IPR005633; Ribosomal_L23/L25_N.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR PANTHER; PTHR11620; PTHR11620; 1.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR Pfam; PF03939; Ribosomal_L23eN; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
DR TIGRFAMs; TIGR03636; uL23_arch; 1.
DR PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Citrullination; Cytoplasm; Isopeptide bond; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62751"
FT CHAIN 2..156
FT /note="60S ribosomal protein L23a"
FT /id="PRO_0000240144"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 32..74
FT /note="Beta-like import receptor binding (BIB) domain"
FT /evidence="ECO:0000250|UniProtKB:P62750"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..64
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N,N,N-trimethylalanine"
FT /evidence="ECO:0000250|UniProtKB:P62751"
FT MOD_RES 41
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P62751"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62750"
FT MOD_RES 45
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62750"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62751"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62750"
SQ SEQUENCE 156 AA; 17695 MW; 3980E77B47FAB70E CRC64;
MAPKAKKEAP APPKAEAKAK ALKAKKAVLK GVHSHKKKKI RTSPTFRRPK TLRLRRQPKY
PRKSAPRRNK LDHYAIIKFP LTTESAMKKI EDNNTLVFIV DVKANKHQIK QAVKKLYDID
VAKVNTLIRP DGEKKAYVRL APDYDALDVA NKIGII
