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RL23A_RAT
ID   RL23A_RAT               Reviewed;         156 AA.
AC   P62752; P29316; P39024; Q92774;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=60S ribosomal protein L23a;
GN   Name=Rpl23a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=8428950; DOI=10.1016/s0021-9258(18)53838-2;
RA   Suzuki K., Wool I.G.;
RT   "The primary structure of rat ribosomal protein L23a. The application of
RT   homology search to the identification of genes for mammalian and yeast
RT   ribosomal proteins and a correlation of rat and yeast ribosomal proteins.";
RL   J. Biol. Chem. 268:2755-2761(1993).
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; X65228; CAA46336.1; -; mRNA.
DR   PIR; A45214; R3RT3A.
DR   RefSeq; NP_001101753.1; NM_001108283.1.
DR   AlphaFoldDB; P62752; -.
DR   SMR; P62752; -.
DR   BioGRID; 262033; 6.
DR   IntAct; P62752; 8.
DR   MINT; P62752; -.
DR   STRING; 10116.ENSRNOP00000036391; -.
DR   iPTMnet; P62752; -.
DR   PhosphoSitePlus; P62752; -.
DR   jPOST; P62752; -.
DR   PaxDb; P62752; -.
DR   PRIDE; P62752; -.
DR   GeneID; 360572; -.
DR   KEGG; rno:360572; -.
DR   CTD; 6147; -.
DR   RGD; 1304897; Rpl23a.
DR   VEuPathDB; HostDB:ENSRNOG00000023344; -.
DR   eggNOG; KOG1751; Eukaryota.
DR   HOGENOM; CLU_037562_0_2_1; -.
DR   InParanoid; P62752; -.
DR   OMA; IPHVPRM; -.
DR   OrthoDB; 1436090at2759; -.
DR   PhylomeDB; P62752; -.
DR   TreeFam; TF314116; -.
DR   PRO; PR:P62752; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000023344; Expressed in ovary and 19 other tissues.
DR   ExpressionAtlas; P62752; baseline and differential.
DR   Genevisible; P62752; RN.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:RGD.
DR   GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0070180; F:large ribosomal subunit rRNA binding; IDA:RGD.
DR   GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
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_0000129469"
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
 
 
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