RL8_RAT
ID RL8_RAT Reviewed; 257 AA.
AC P62919; A0JMZ6; P25120;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=60S ribosomal protein L8;
GN Name=Rpl8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=1610349; DOI=10.1016/0006-291x(92)91658-d;
RA Chan Y.-L., Wool I.G.;
RT "The primary structure of rat ribosomal protein L8.";
RL Biochem. Biophys. Res. Commun. 185:539-547(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; X62145; CAA44071.1; -; mRNA.
DR EMBL; BC126063; AAI26064.1; -; mRNA.
DR PIR; JU0177; R5RTL8.
DR RefSeq; NP_001030088.2; NM_001034916.2.
DR RefSeq; XP_002729189.1; XM_002729143.5.
DR RefSeq; XP_017450875.1; XM_017595386.1.
DR AlphaFoldDB; P62919; -.
DR SMR; P62919; -.
DR BioGRID; 247805; 3.
DR IntAct; P62919; 7.
DR STRING; 10116.ENSRNOP00000046553; -.
DR iPTMnet; P62919; -.
DR PhosphoSitePlus; P62919; -.
DR SwissPalm; P62919; -.
DR jPOST; P62919; -.
DR PaxDb; P62919; -.
DR PRIDE; P62919; -.
DR Ensembl; ENSRNOT00000100252; ENSRNOP00000077291; ENSRNOG00000068956.
DR GeneID; 100360117; -.
DR GeneID; 26962; -.
DR KEGG; rno:100360117; -.
DR KEGG; rno:26962; -.
DR UCSC; RGD:619827; rat.
DR CTD; 6132; -.
DR RGD; 619827; Rpl8.
DR eggNOG; KOG2309; Eukaryota.
DR GeneTree; ENSGT00940000153244; -.
DR HOGENOM; CLU_036235_0_3_1; -.
DR InParanoid; P62919; -.
DR OMA; SCIELRP; -.
DR OrthoDB; 1156335at2759; -.
DR PhylomeDB; P62919; -.
DR TreeFam; TF300748; -.
DR Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-RNO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-RNO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-RNO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P62919; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000032635; Expressed in thymus and 19 other tissues.
DR Genevisible; P62919; RN.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:RGD.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR GO; GO:0042788; C:polysomal ribosome; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:1990932; F:5.8S rRNA binding; IDA:RGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0002181; P:cytoplasmic translation; ISO:RGD.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR HAMAP; MF_01320_A; Ribosomal_L2_A; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR023672; Ribosomal_L2_arc.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR022671; Ribosomal_L2_CS.
DR InterPro; IPR014726; Ribosomal_L2_dom3.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR13691; PTHR13691; 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; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydroxylation; Isopeptide bond; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Ubl conjugation.
FT CHAIN 1..257
FT /note="60S ribosomal protein L8"
FT /id="PRO_0000129746"
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
