ID RL4_CANLF Reviewed; 421 AA. AC Q28346; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 108. DE RecName: Full=Large ribosomal subunit protein uL4 {ECO:0000305}; DE AltName: Full=60S ribosomal protein L1; DE AltName: Full=60S ribosomal protein L4; GN Name=RPL4; Synonyms=RPL1; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-421. RC STRAIN=Mongrel; RA Sandholzer U.; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP STRUCTURE BY ELECTRON MICROSCOPY (8.7 ANGSTROMS). RX PubMed=18400176; DOI=10.1016/j.str.2008.01.007; RA Chandramouli P., Topf M., Menetret J.F., Eswar N., Cannone J.J., RA Gutell R.R., Sali A., Akey C.W.; RT "Structure of the mammalian 80S ribosome at 8.7 A resolution."; RL Structure 16:535-548(2008). 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:P36578}. CC -!- SUBUNIT: Component of the large ribosomal subunit. May bind IPO9 with CC low affinity (By similarity). Interacts with RBM3 (By similarity). CC {ECO:0000250|UniProtKB:P36578, ECO:0000250|UniProtKB:P50878}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P36578}. CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q9D8E6}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X99909; CAA68182.1; -; mRNA. DR PDB; 4V5Z; EM; 8.70 A; c=1-421. DR PDBsum; 4V5Z; -. DR AlphaFoldDB; Q28346; -. DR SMR; Q28346; -. DR STRING; 9615.ENSCAFP00000047295; -. DR PaxDb; 9612-ENSCAFP00000036039; -. DR eggNOG; KOG1475; Eukaryota. DR InParanoid; Q28346; -. DR EvolutionaryTrace; Q28346; -. DR Proteomes; UP000002254; Unplaced. DR Proteomes; UP000694429; Unplaced. DR Proteomes; UP000694542; Unplaced. DR Proteomes; UP000805418; Unplaced. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. 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; IEA:InterPro. DR Gene3D; 3.40.1370.10; -; 1. DR InterPro; IPR025755; Ribos_uL4_C_dom. DR InterPro; IPR002136; Ribosomal_uL4. DR InterPro; IPR023574; Ribosomal_uL4_dom_sf. DR InterPro; IPR013000; Ribosomal_uL4_euk/arc_CS. DR InterPro; IPR045240; Ribosomal_uL4_euk/arch. DR PANTHER; PTHR19431; 60S RIBOSOMAL PROTEIN L4; 1. DR PANTHER; PTHR19431:SF0; 60S RIBOSOMAL PROTEIN L4; 1. DR Pfam; PF14374; Ribos_L4_asso_C; 1. DR Pfam; PF00573; Ribosomal_L4; 1. DR SUPFAM; SSF52166; Ribosomal protein L4; 1. DR PROSITE; PS00939; RIBOSOMAL_L1E; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Citrullination; Cytoplasm; Isopeptide bond; KW Methylation; Phosphoprotein; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P36578" FT CHAIN 2..421 FT /note="Large ribosomal subunit protein uL4" FT /id="PRO_0000129349" FT REGION 359..421 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 371..394 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 398..421 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P36578" FT MOD_RES 14 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P36578" FT MOD_RES 97 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9D8E6" FT MOD_RES 106 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P36578" FT MOD_RES 259 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D8E6" FT MOD_RES 266 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P36578" FT MOD_RES 290 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P50878" FT MOD_RES 300 FT /note="Citrulline" FT /evidence="ECO:0000250|UniProtKB:Q9D8E6" FT MOD_RES 333 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P36578" FT MOD_RES 353 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D8E6" FT MOD_RES 361 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9D8E6" FT MOD_RES 362 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P36578" FT CROSSLNK 239 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P36578" FT CROSSLNK 327 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P36578" FT CROSSLNK 361 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P36578" SQ SEQUENCE 421 AA; 47515 MW; AF08C4DDA50A435B CRC64; MACARPLISV YSEKGESSGK NVTLPAVFKA PIRPDIVNFV HTNLRKNNRQ PYAVSELAGH QTSAESWGTG RAVARIPRVR GGGTHRSGQG AFGNMCRGGR MFAPTKTWRR WHRRVNTTQK RYAICSALAC LSLPALVMSK GHRIEEVPEL PLVVEDKVEG YKKTKEAVLL LKKLKAWNDI KKVYASQRMR AGKGKMRNRR RIQRRGPCII YNEDNGIIKA FRKHPGITLL NVSKLNILKL APGGHVGRFC IWTESAFRKL DDLYGTWRKA ASLKSNYNLP MHKMLNTDLS RILKMPRDPR ALRAPRKKIH RRVLKKNPLK NLRIMLKLNP YAKTMRRNTI LRQAKNHKLR MDKAAAALEA KSEEKGVPGK KPRRKKGKKT VGVKKPKKPV VGKKAAATKK PAADKKPAEK KPTTEEKKPA A //