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RL4_BOVIN
ID   RL4_BOVIN               Reviewed;         422 AA.
AC   Q58DW0; Q3T088;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=60S ribosomal protein L4;
GN   Name=RPL4;
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].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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: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; BT021487; AAX46334.1; -; mRNA.
DR   EMBL; BC102521; AAI02522.1; -; mRNA.
DR   RefSeq; NP_001014894.1; NM_001014894.1.
DR   AlphaFoldDB; Q58DW0; -.
DR   SMR; Q58DW0; -.
DR   STRING; 9913.ENSBTAP00000006866; -.
DR   iPTMnet; Q58DW0; -.
DR   PaxDb; Q58DW0; -.
DR   PeptideAtlas; Q58DW0; -.
DR   PRIDE; Q58DW0; -.
DR   Ensembl; ENSBTAT00000006866; ENSBTAP00000006866; ENSBTAG00000005211.
DR   GeneID; 510547; -.
DR   KEGG; bta:510547; -.
DR   CTD; 6124; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005211; -.
DR   eggNOG; KOG1475; Eukaryota.
DR   GeneTree; ENSGT00390000018145; -.
DR   HOGENOM; CLU_026535_4_0_1; -.
DR   InParanoid; Q58DW0; -.
DR   OMA; WHQKVNV; -.
DR   OrthoDB; 878848at2759; -.
DR   TreeFam; TF300593; -.
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-72689; Formation of a pool of free 40S subunits.
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 10.
DR   Bgee; ENSBTAG00000005211; Expressed in adenohypophysis and 106 other tissues.
DR   ExpressionAtlas; Q58DW0; baseline.
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   2: Evidence at transcript 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..422
FT                   /note="60S ribosomal protein L4"
FT                   /id="PRO_0000129348"
FT   REGION          359..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..422
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         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P36578"
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   422 AA;  47412 MW;  ADC3F06A6EA3F8E3 CRC64;
     MACARPLISV YSEKGESSGK NVTLPAVFKA PIRPDIVNFV HTNLRKNNRQ PYAVSELAGH
     QTSAESWGTG RAVARIPRVR GGGTHRSGQG AFGNMCRGGR MFAPTKTWRR WHRRVNTTQK
     RYAICSALAA SALPALVMSK GHRIEEVPEL PLVVEDKVEG YKKTKEAVLL LKKLKAWNDI
     KKVYASQRMR AGKGKMRNRR RIQRRGPCII YNEDNGIIKA FRNIPGITLL NVSKLNILKL
     APGGHVGRFC IWTESAFRKL DELYGTWRKA ASLKSNYNLP MHKMLNTDLS RILKSPEIQR
     ALRAPRKKIH RRVLKKNPLK NLRIMLKLNP YAKTMRRNTI LRQARNHKIR MDKAAAALEA
     KSDQKGVQGK KPVVGNKEKK AVGDKKLKKP VVGKKAAGTK KPAAEKKPTE KKPTSEEKKA
     AA
 
 
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