ID   RL5A_XENLA              Reviewed;         296 AA.
AC   P15125;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=60S ribosomal protein L5-A;
GN   Name=rpl5-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2586520; DOI=10.1128/mcb.9.12.5281-5288.1989;
RA   Wormington W.M.;
RT   "Developmental expression and 5S rRNA-binding activity of Xenopus laevis
RT   ribosomal protein L5.";
RL   Mol. Cell. Biol. 9:5281-5288(1989).
CC   -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC       responsible for the synthesis of proteins in the cell. The small
CC       ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC       encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC       molecules. The large subunit (LSU) contains the ribosomal catalytic
CC       site termed the peptidyl transferase center (PTC), which catalyzes the
CC       formation of peptide bonds, thereby polymerizing the amino acids
CC       delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC       leave the ribosome through a tunnel in the LSU and interact with
CC       protein factors that function in enzymatic processing, targeting, and
CC       the membrane insertion of nascent chains at the exit of the ribosomal
CC       tunnel. As part of the 5S RNP/5S ribonucleoprotein particle it is an
CC       essential component of the LSU, required for its formation and the
CC       maturation of rRNAs. It also couples ribosome biogenesis to p53/TP53
CC       activation. As part of the 5S RNP it accumulates in the nucleoplasm and
CC       inhibits MDM2, when ribosome biogenesis is perturbed, mediating the
CC       stabilization and the activation of TP53.
CC       {ECO:0000250|UniProtKB:P46777}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit (LSU). Part of a LSU
CC       subcomplex, the 5S RNP which is composed of the 5S RNA, RPL5 and RPL11.
CC       {ECO:0000250|UniProtKB:P46777}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46777}.
CC       Nucleus, nucleolus {ECO:0000250|UniProtKB:P46777}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M29032; AAA49952.1; -; mRNA.
DR   PIR; A33823; A33823.
DR   AlphaFoldDB; P15125; -.
DR   SMR; P15125; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0008097; F:5S rRNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   HAMAP; MF_01337_A; Ribosomal_L18_A; 1.
DR   InterPro; IPR005485; Rbsml_L5_euk/L18_arc.
DR   InterPro; IPR025607; Rbsml_L5e_C.
DR   PANTHER; PTHR23410; PTHR23410; 1.
DR   Pfam; PF14204; Ribosomal_L18_c; 1.
DR   Pfam; PF17144; Ribosomal_L5e; 1.
DR   PRINTS; PR00058; RIBOSOMALL5.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P46777"
FT   CHAIN           2..296
FT                   /note="60S ribosomal protein L5-A"
FT                   /id="PRO_0000131438"
FT   REGION          251..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..296
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   296 AA;  34105 MW;  7B46548D7000AFDB CRC64;
     MGFVKVVKNK AYFKRYQVKF RRRREGKTDY YARKRLVIQD KNKYNTPKYR MIVRVTNRDI
     ICQIAYARIE GDMIVCAAYA HELPKYGIKV GLTNYAAAYC TGLLLARRLL NKFGLDKVYE
     GQVEVTGDEY NVESIDGEPG AFTCYLDAGL TRTTTGNKVF GALKGAVDGG LSIPHSTKRF
     PGYDSESKEF NPEVHRKHIF AQNVAEYMRL LMEEDEDAYK KQFSQYIKNG VTADQVEDLY
     KKAHAGIREN PVHEKKPKKE VKKKRWNRAK LSLEQKKDRV AQKKASFLRA QEKADS