RL4_CANLF
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 03-AUG-2022, entry version 101.
DE RecName: Full=60S ribosomal protein L4;
DE AltName: Full=60S ribosomal protein L1;
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}.
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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; 9612.ENSCAFP00000036039; -.
DR PaxDb; Q28346; -.
DR eggNOG; KOG1475; Eukaryota.
DR InParanoid; Q28346; -.
DR EvolutionaryTrace; Q28346; -.
DR Proteomes; UP000002254; 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_L4_C_dom.
DR InterPro; IPR002136; Ribosomal_L4/L1e.
DR InterPro; IPR013000; Ribosomal_L4/L1e_euk/arc_CS.
DR InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR InterPro; IPR045240; Ribosomal_L4_euk/arch.
DR PANTHER; PTHR19431; PTHR19431; 1.
DR Pfam; PF14374; Ribos_L4_asso_C; 1.
DR Pfam; PF00573; Ribosomal_L4; 1.
DR SUPFAM; SSF52166; SSF52166; 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="60S ribosomal protein L4"
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
