RL5_PIG
ID RL5_PIG Reviewed; 125 AA.
AC Q95276;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=60S ribosomal protein L5;
DE Flags: Fragment;
GN Name=RPL5;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
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; Z81207; CAB03565.1; -; mRNA.
DR STRING; 9823.ENSSSCP00000007354; -.
DR PaxDb; Q95276; -.
DR PeptideAtlas; Q95276; -.
DR PRIDE; Q95276; -.
DR eggNOG; KOG0875; Eukaryota.
DR InParanoid; Q95276; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0008097; F:5S rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR InterPro; IPR005485; Rbsml_L5_euk/L18_arc.
DR PANTHER; PTHR23410; PTHR23410; 1.
DR Pfam; PF17144; Ribosomal_L5e; 1.
DR PRINTS; PR00058; RIBOSOMALL5.
PE 2: Evidence at transcript level;
KW Acetylation; 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..>125
FT /note="60S ribosomal protein L5"
FT /id="PRO_0000131434"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT NON_TER 125
SQ SEQUENCE 125 AA; 14670 MW; 831E0423B58FB042 CRC64;
MGFVKVVKNK AYFKRYQVKF RRRREGKTDY YARKRLVIQD KNKYNTPKYR MIVRVTNRDI
ICQIAYARIE GDMIVCAAYA HELPKYGVKV GLTNYAAAYC TGLLLARRLL NRFGMXKIYG
GQVEV
