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Database: UniProt
Entry: RL8_BOVIN
LinkDB: RL8_BOVIN
Original site: RL8_BOVIN 
ID   RL8_BOVIN               Reviewed;         257 AA.
AC   Q3T0S6; B0JYM1;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Large ribosomal subunit protein uL2 {ECO:0000305};
DE   AltName: Full=60S ribosomal protein L8;
GN   Name=RPL8;
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].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) 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:P62917}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit (By similarity).
CC       Interacts with CRY1 (By similarity). {ECO:0000250|UniProtKB:P62917,
CC       ECO:0000250|UniProtKB:P62918}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62917}.
CC   -!- PTM: Hydroxylated on His-216 by RIOX1. The modification is impaired by
CC       hypoxia. {ECO:0000250|UniProtKB:P62917}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC       {ECO:0000305}.
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DR   EMBL; BC102277; AAI02278.1; -; mRNA.
DR   EMBL; BC151407; AAI51408.1; -; mRNA.
DR   RefSeq; NP_001029797.1; NM_001034625.2.
DR   RefSeq; XP_005215277.1; XM_005215220.1.
DR   PDB; 7NWH; EM; 4.10 A; A=1-249.
DR   PDBsum; 7NWH; -.
DR   AlphaFoldDB; Q3T0S6; -.
DR   EMDB; EMD-12632; -.
DR   SMR; Q3T0S6; -.
DR   STRING; 9913.ENSBTAP00000037200; -.
DR   PaxDb; 9913-ENSBTAP00000037200; -.
DR   PeptideAtlas; Q3T0S6; -.
DR   Ensembl; ENSBTAT00000037367.4; ENSBTAP00000037200.3; ENSBTAG00000026327.4.
DR   GeneID; 535056; -.
DR   KEGG; bta:535056; -.
DR   CTD; 6132; -.
DR   VEuPathDB; HostDB:ENSBTAG00000026327; -.
DR   eggNOG; KOG2309; Eukaryota.
DR   GeneTree; ENSGT00940000153244; -.
DR   HOGENOM; CLU_036235_0_3_1; -.
DR   InParanoid; Q3T0S6; -.
DR   OMA; GGRHPCT; -.
DR   OrthoDB; 1086454at2759; -.
DR   TreeFam; TF300748; -.
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-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-BTA-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-BTA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-BTA-9629569; Protein hydroxylation.
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 14.
DR   Bgee; ENSBTAG00000026327; Expressed in ileocecal valve and 107 other cell types or tissues.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 4.10.950.10; Ribosomal protein L2, domain 3; 1.
DR   HAMAP; MF_01320_A; Ribosomal_uL2_A; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR002171; Ribosomal_uL2.
DR   InterPro; IPR023672; Ribosomal_uL2_arc.
DR   InterPro; IPR022669; Ribosomal_uL2_C.
DR   InterPro; IPR022671; Ribosomal_uL2_CS.
DR   InterPro; IPR014726; Ribosomal_uL2_dom3.
DR   InterPro; IPR022666; Ribosomal_uL2_RNA-bd_dom.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR13691:SF16; 60S RIBOSOMAL PROTEIN L8; 1.
DR   PANTHER; PTHR13691; RIBOSOMAL PROTEIN L2; 1.
DR   Pfam; PF00181; Ribosomal_L2; 1.
DR   Pfam; PF03947; Ribosomal_L2_C; 1.
DR   PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR   SMART; SM01383; Ribosomal_L2; 1.
DR   SMART; SM01382; Ribosomal_L2_C; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR   PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Hydroxylation; Isopeptide bond;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; Ubl conjugation.
FT   CHAIN           1..257
FT                   /note="Large ribosomal subunit protein uL2"
FT                   /id="PRO_0000239849"
FT   REGION          207..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         216
FT                   /note="(3S)-3-hydroxyhistidine"
FT                   /evidence="ECO:0000250|UniProtKB:P62917"
FT   CROSSLNK        42
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62917"
FT   CROSSLNK        149
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62917"
FT   CROSSLNK        234
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62917"
FT   CROSSLNK        250
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62917"
SQ   SEQUENCE   257 AA;  28025 MW;  CE1610449749318B CRC64;
     MGRVIRGQRK GAGSVFRAHV KHRKGAARLR AVDFAERHGY IKGIVKDIIH DPGRGAPLAK
     VVFRDPYRFK KRTELFIAAE GIHTGQFVYC GKKAQLNIGN VLPVGTMPEG TIVCCLEEKP
     GDRGKLARAS GNYATVISHN PETKKTRVKL PSGSKKVISS ANRAVVGVVA GGGRIDKPIL
     KAGRAYHKYK AKRNCWPRVR GVAMNPVEHP FGGGNHQHIG KPSTIRRDAP AGRKVGLIAA
     RRTGRLRGTK TVQEKEN
//
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