RL4_RAT
ID RL4_RAT Reviewed; 421 AA.
AC P50878;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=60S ribosomal protein L4;
DE AltName: Full=60S ribosomal protein L1;
GN Name=Rpl4; Synonyms=Rpl1;
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=7575549; DOI=10.1006/bbrc.1995.2359;
RA Chan Y.-L., Olvera J., Wool I.G.;
RT "The primary structures of rat ribosomal proteins L4 and L41.";
RL Biochem. Biophys. Res. Commun. 214:810-818(1995).
RN [2]
RP INTERACTION WITH RBM3.
RX PubMed=15684048; DOI=10.1073/pnas.0409764102;
RA Dresios J., Aschrafi A., Owens G.C., Vanderklish P.W., Edelman G.M.,
RA Mauro V.P.;
RT "Cold stress-induced protein Rbm3 binds 60S ribosomal subunits, alters
RT microRNA levels, and enhances global protein synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1865-1870(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND SER-295, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (PubMed:15684048).
CC {ECO:0000250|UniProtKB:P36578, ECO:0000269|PubMed:15684048}.
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; X82180; CAA57671.1; -; mRNA.
DR PIR; JC4277; JC4277.
DR RefSeq; NP_071955.1; NM_022510.1.
DR AlphaFoldDB; P50878; -.
DR SMR; P50878; -.
DR BioGRID; 249017; 6.
DR IntAct; P50878; 4.
DR MINT; P50878; -.
DR STRING; 10116.ENSRNOP00000013462; -.
DR iPTMnet; P50878; -.
DR PhosphoSitePlus; P50878; -.
DR jPOST; P50878; -.
DR PaxDb; P50878; -.
DR PRIDE; P50878; -.
DR GeneID; 64302; -.
DR KEGG; rno:64302; -.
DR UCSC; RGD:619824; rat.
DR CTD; 6124; -.
DR RGD; 619824; Rpl4.
DR eggNOG; KOG1475; Eukaryota.
DR InParanoid; P50878; -.
DR OrthoDB; 878848at2759; -.
DR PhylomeDB; P50878; -.
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:P50878; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031672; C:A band; IDA:RGD.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:RGD.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR GO; GO:0015934; C:large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:RGD.
DR GO; GO:0008097; F:5S 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:0007420; P:brain development; IEP:RGD.
DR GO; GO:0003360; P:brainstem development; IEP:RGD.
DR GO; GO:0030154; P:cell differentiation; IEP:RGD.
DR GO; GO:0071417; P:cellular response to organonitrogen compound; IEP:RGD.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:RGD.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IMP:RGD.
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 Acetylation; Citrullination; Cytoplasm; Isopeptide bond; Methylation;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW 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_0000129353"
FT REGION 365..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..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:0007744|PubMed:22673903"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 364
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D8E6"
FT MOD_RES 365
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 364
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; 47257 MW; 08C82C1D7A49AAC5 CRC64;
MACARPLISV YSEKGESSGK NVTLPAVFKA PIRPDIVNFV HTNLRKNNRQ PYAVSELAGH
QTSAESWGTG RAVARIPRVR GGGTHRSGQG AFGNMCRGGR MFAPTKTWRR WHRRVNTTQK
RYAICSALAA SALPALVMSK GHCVEEVPEL PLVVEDKVES YKKTKEAVQL LKKLKAWNDI
KKVYASQRMR AGKGKMRNRR RIQRRGPCII YNEDNGIIKA FRNIPGITLL NVSKLNILKL
APGGHVGRFC IWTESAFRKL DELYGTWRKA ASLKSNYNLP MHKMMNTDLS RILKSPEIQR
ALRAPRKKIH RRVLKKNPLK NLRIMLKLNP YAKTMRRNTI LRQARNHKLR VKKLEAAAAA
LAAKSEKIVP EKGAGDKKPA VGKKGKKPVD AKKLKKPAGK KVVTKKPAEK KPTTEEKKSA
A
