RL5_CHICK
ID RL5_CHICK Reviewed; 297 AA.
AC P22451;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=60S ribosomal protein L5;
GN Name=RPL5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1840495; DOI=10.1016/0167-4781(91)90142-9;
RA Kenmochi N., Maeda N., Tanaka T.;
RT "The primary structure of chicken ribosomal protein L5.";
RL Biochim. Biophys. Acta 1088:445-447(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1398102; DOI=10.1016/0378-1119(92)90274-s;
RA Kenmochi N., Maeda N., Tanaka T.;
RT "The structure and complete sequence of the gene encoding chicken ribosomal
RT protein L5.";
RL Gene 119:215-219(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 202-297.
RC TISSUE=Gizzard;
RX PubMed=7649987; DOI=10.1074/jbc.270.34.20135;
RA Hirano K., Ito M., Hartshorne D.J.;
RT "Interaction of the ribosomal protein, L5, with protein phosphatase type
RT 1.";
RL J. Biol. Chem. 270:19786-19790(1995).
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}.
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DR EMBL; X57016; CAA40335.1; -; mRNA.
DR EMBL; D10737; BAA01581.1; -; Genomic_DNA.
DR EMBL; U31753; AAC59694.1; -; mRNA.
DR PIR; JC1308; JC1308.
DR RefSeq; NP_989912.1; NM_204581.4.
DR AlphaFoldDB; P22451; -.
DR SMR; P22451; -.
DR BioGRID; 675562; 1.
DR STRING; 9031.ENSGALP00000009511; -.
DR PaxDb; P22451; -.
DR Ensembl; ENSGALT00000068972; ENSGALP00000050466; ENSGALG00000005922.
DR GeneID; 395269; -.
DR KEGG; gga:395269; -.
DR CTD; 6125; -.
DR VEuPathDB; HostDB:geneid_395269; -.
DR eggNOG; KOG0875; Eukaryota.
DR GeneTree; ENSGT00950000183210; -.
DR HOGENOM; CLU_056222_1_0_1; -.
DR InParanoid; P22451; -.
DR OMA; KSQFQGY; -.
DR OrthoDB; 999609at2759; -.
DR PhylomeDB; P22451; -.
DR PRO; PR:P22451; -.
DR Proteomes; UP000000539; Chromosome 8.
DR Bgee; ENSGALG00000005922; Expressed in spermatid and 13 other tissues.
DR ExpressionAtlas; P22451; baseline and differential.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0008097; F:5S rRNA binding; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:Ensembl.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:2000435; P:negative regulation of protein neddylation; IEA:Ensembl.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IEA:Ensembl.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:Ensembl.
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..297
FT /note="60S ribosomal protein L5"
FT /id="PRO_0000131437"
FT REGION 253..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 297 AA; 34091 MW; E7FF0452D85DB0DD CRC64;
MGFVKVVKNK AYFKRYQVKF RRRREGKTDY YARKRLVIQD KNKYNTPKYR MIVRVTNRDI
ICQIAYARIE GDMIVCAAYA HELPKYGVKV GLTNYAAAYC TGLLLARRLL NKFGLDKIYE
GQVEVTGDEY NVESVDGKPG AFTCYLDAGL ARTTTGNKVF GALKGAVDGG LSIPHSTKRF
PGYDSESKEF NAEVHRKHIM GQNVADYMRY LMEEDEDAYK KQFSQYIKNN ITPDGMEEMY
KKAHAAIRDN PVHEKKPKRE VKKKRVNSTK MSLAQKKDRV AQKKASFLRA QERAADS
