RL3_BOVIN
ID RL3_BOVIN Reviewed; 403 AA.
AC P39872; Q5E9A8; Q9N0L7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=60S ribosomal protein L3;
GN Name=RPL3;
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 [MRNA].
RX PubMed=7948030; DOI=10.1016/0167-4781(94)90232-1;
RA Simonic T., Gaudi S., Giussani F., Ronchi S., Tenchini M.L.;
RT "cDNA sequence for bovine ribosomal protein L3 carrying a bipartite nuclear
RT targeting motif, identified also in many other ribosomal proteins.";
RL Biochim. Biophys. Acta 1219:706-710(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10684968; DOI=10.1016/s0167-4781(99)00237-7;
RA Duga S., Asselta R., Malcovati M., Tenchini M.L., Ronchi S., Simonic T.;
RT "The intron-containing L3 ribosomal protein gene (RPL3): sequence analysis
RT and identification of U43 and of two novel intronic small nucleolar RNAs.";
RL Biochim. Biophys. Acta 1490:225-236(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. {ECO:0000250|UniProtKB:P39023}.
CC -!- SUBUNIT: Component of the large ribosomal subunit. Interacts with
CC DHX33. {ECO:0000250|UniProtKB:P39023}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P39023}. Cytoplasm
CC {ECO:0000250|UniProtKB:P39023}.
CC -!- PTM: Constitutively monomethylated at His-245 by METTL18. Regulates the
CC function of RPL3 in the dynamics of pre-rRNA processing, ribosome
CC biogenesis, and translation. It is not required for incorporation of
CC RPL3 into ribosomes. {ECO:0000250|UniProtKB:P39023}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC {ECO:0000305}.
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DR EMBL; Z29555; CAA82654.1; -; mRNA.
DR EMBL; AJ238851; CAB76199.1; -; Genomic_DNA.
DR EMBL; BT021012; AAX09029.1; -; mRNA.
DR EMBL; BC102253; AAI02254.1; -; mRNA.
DR PIR; S50221; S50221.
DR RefSeq; NP_777140.1; NM_174715.1.
DR AlphaFoldDB; P39872; -.
DR SMR; P39872; -.
DR IntAct; P39872; 1.
DR STRING; 9913.ENSBTAP00000004188; -.
DR PaxDb; P39872; -.
DR PeptideAtlas; P39872; -.
DR PRIDE; P39872; -.
DR Ensembl; ENSBTAT00000004188; ENSBTAP00000004188; ENSBTAG00000003228.
DR GeneID; 282688; -.
DR KEGG; bta:282688; -.
DR CTD; 6122; -.
DR VEuPathDB; HostDB:ENSBTAG00000003228; -.
DR VGNC; VGNC:101451; RPL3.
DR eggNOG; KOG0746; Eukaryota.
DR GeneTree; ENSGT00390000017606; -.
DR HOGENOM; CLU_033361_2_1_1; -.
DR InParanoid; P39872; -.
DR OMA; HQRTEYN; -.
DR OrthoDB; 793191at2759; -.
DR TreeFam; TF300555; -.
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 5.
DR Bgee; ENSBTAG00000003228; Expressed in digestive system secreted substance and 106 other tissues.
DR ExpressionAtlas; P39872; baseline.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 4.10.960.10; -; 1.
DR InterPro; IPR045077; L3_arc_euk.
DR InterPro; IPR000597; Ribosomal_L3.
DR InterPro; IPR019926; Ribosomal_L3_CS.
DR InterPro; IPR044892; Ribosomal_L3_dom_3_arc_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR11363; PTHR11363; 1.
DR Pfam; PF00297; Ribosomal_L3; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..403
FT /note="60S ribosomal protein L3"
FT /id="PRO_0000077226"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT MOD_RES 136
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27659"
FT MOD_RES 245
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT MOD_RES 286
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P27659"
FT MOD_RES 294
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT MOD_RES 366
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT MOD_RES 373
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27659"
FT CROSSLNK 39
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 224
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 366
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 386
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 393
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 399
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CONFLICT 362
FT /note="K -> E (in Ref. 2; CAB76199)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="I -> V (in Ref. 2; CAB76199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 46024 MW; BB1FD71F932D224E CRC64;
MSHRKFSAPR HGSLGFLPRK RSSRHRGKVK SFPKDDSSKP VHLTAFLGYK AGMTHIVREV
DRPGSKVNKK EVVEAVTIVE TPPMVIVGIV GYVETPRGLR TFKTIFAEHI SDECKRRFYK
NWHKSKKKAF TKYCKKWQDA DGKKQLERDF SSMKKYCQVI RVIAHTQMRL LPLRQKKAHL
MEVQVNGGTV AEKLDWARER LEQQVPVSQV FGQDEMIDVI GVTKGKGYKG VTSRWHTKKL
PRKTHRGLRK VACIGAWHPA RVAFSVARAG QKGYHHRTEI NKKIYKIGQG YLIKDGKLIK
NNASTDYDLS DKSINPLGGF VHYGEVTNDF VMLKGCVVGT KKRVLTLRKS LLVQTKRRAL
EKIDLKFIDT TSKFGHGRFQ TVEEKKAFMG PLKKDRIAKE EGA
