RL5_BOVIN
ID RL5_BOVIN Reviewed; 297 AA.
AC Q58DW5; Q3MHL0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=60S ribosomal protein L5;
GN Name=RPL5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX46329.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BT021482; AAX46329.1; ALT_FRAME; mRNA.
DR EMBL; BC105198; AAI05199.1; -; mRNA.
DR RefSeq; NP_001030383.1; NM_001035306.2.
DR AlphaFoldDB; Q58DW5; -.
DR SMR; Q58DW5; -.
DR STRING; 9913.ENSBTAP00000002626; -.
DR PaxDb; Q58DW5; -.
DR PeptideAtlas; Q58DW5; -.
DR PRIDE; Q58DW5; -.
DR Ensembl; ENSBTAT00000002626; ENSBTAP00000002626; ENSBTAG00000002026.
DR GeneID; 515238; -.
DR KEGG; bta:515238; -.
DR CTD; 6125; -.
DR VEuPathDB; HostDB:ENSBTAG00000002026; -.
DR eggNOG; KOG0875; Eukaryota.
DR GeneTree; ENSGT00950000183210; -.
DR HOGENOM; CLU_056222_1_0_1; -.
DR InParanoid; Q58DW5; -.
DR OMA; KSQFQGY; -.
DR OrthoDB; 999609at2759; -.
DR TreeFam; TF300044; -.
DR Reactome; R-BTA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-BTA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-BTA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-BTA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-BTA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000002026; Expressed in adenohypophysis and 104 other tissues.
DR ExpressionAtlas; Q58DW5; baseline.
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 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 Acetylation; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; Ubl conjugation.
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_0000236216"
FT REGION 252..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT MOD_RES 220
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P47962"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT CONFLICT 49
FT /note="Y -> N (in Ref. 2; AAI05199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 34345 MW; ECC7B07EC756814D CRC64;
MGFVKVVKNK AYFKRYQVKF RRRREGKTDY YARKRLVIQD KNKYNTPKYR MIVRVTNRDI
ICQIAYARIE GDMIVCAAYA HELPKYGVKV GLTNYAAAYC TGLLLARRLL NRFGMDKIYE
GQVEVTGDEY NVESIDGQPG AFTCYLDAGL ARTTTGNKVF GALKGAVDGG LSIPHSTKRF
PGYDSESKEF SAEVHRKHIM GQNVADYMRY LIEEDEDAYK KQFSQYIKNN VTPDMMEEMY
KKAHAAIREN PVYEKKPKKE VKKKRWNRPK MSLAQKKDRV AQKKASFLRA QERAAES
