ID   RL5_RABIT               Reviewed;         101 AA.
AC   P19949; O19046;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=60S ribosomal protein L5;
DE   Flags: Fragments;
GN   Name=RPL5;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2960523; DOI=10.1111/j.1432-1033.1987.tb13584.x;
RA   Nendza R., Digweed M., Meyer H.E., Erdmann V.A., Mayr G.W.;
RT   "5S-rRNA-containing ribonucleoproteins from rabbit muscle and liver.
RT   Complex and partial primary structures.";
RL   Eur. J. Biochem. 169:85-95(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 47-101.
RC   STRAIN=New Zealand;
RA   Brunet A., Henrion G., Duranthon V., Renard J.P.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
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. Interacts with RRP1B.
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       Interacts with NVL in an ATP-dependent manner. Interacts with RRP1B (By
CC       similarity). Interacts with IPO5, IPO7 and KPNB1; these interactions
CC       may be involved in RPL5 nuclear import for the assembly of ribosomal
CC       subunits (By similarity). {ECO:0000250|UniProtKB:P46777}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46777}.
CC       Nucleus, nucleolus {ECO:0000250|UniProtKB:P46777}. Note=Although RP5 is
CC       functional within the cytoplasm, the assembly of ribosomal subunits
CC       occurs in the nucleus. RPL5 nuclear import is mediated by IPO5/RanBP5,
CC       IPO7/RanBP7, KPNB1/importin-beta or TPNO1/Trn.
CC       {ECO:0000250|UniProtKB:P46777}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC       {ECO:0000305}.
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DR   EMBL; AF007880; AAB63282.1; -; mRNA.
DR   PIR; S00178; S00178.
DR   AlphaFoldDB; P19949; -.
DR   SMR; P19949; -.
DR   eggNOG; KOG0875; Eukaryota.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
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   InterPro; IPR005485; Rbsml_L5_euk/L18_arc.
DR   InterPro; IPR025607; Rbsml_L5e_C.
DR   PANTHER; PTHR23410; PTHR23410; 2.
DR   Pfam; PF14204; Ribosomal_L18_c; 1.
DR   Pfam; PF17144; Ribosomal_L5e; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Nucleus;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..101
FT                   /note="60S ribosomal protein L5"
FT                   /id="PRO_0000131435"
FT   REGION          59..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000250|UniProtKB:P46777"
FT   MOD_RES         4
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P46777"
FT   NON_CONS        46..47
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   101 AA;  12228 MW;  C76FE95CC982C1A0 CRC64;
     GFVKVVKNKA YFKRYQVKFR RRREGKTDYY ARKRLVIQDK NKYNTPAHAA IRENPVYEKK
     PKREVKKKRW NRPKMSLAQK KDRVAQKKAS FLRAQERAAE S