RL4_PONAB
ID RL4_PONAB Reviewed; 427 AA.
AC Q5RCR3;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=60S ribosomal protein L4;
GN Name=RPL4;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR858206; CAH90444.1; -; mRNA.
DR RefSeq; NP_001125225.1; NM_001131753.1.
DR AlphaFoldDB; Q5RCR3; -.
DR SMR; Q5RCR3; -.
DR STRING; 9601.ENSPPYP00000015792; -.
DR GeneID; 100172118; -.
DR KEGG; pon:100172118; -.
DR CTD; 6124; -.
DR eggNOG; KOG1475; Eukaryota.
DR InParanoid; Q5RCR3; -.
DR OrthoDB; 878848at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
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..427
FT /note="60S ribosomal protein L4"
FT /id="PRO_0000290001"
FT REGION 369..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..400
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..427
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 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 427 AA; 47667 MW; 4785EC60699CD5E2 CRC64;
MACARPLISV YSEKGESSGK NVTLPAVFKA PIRPDIVNFV HTNLRKNNRQ PYAVSELAGH
QTSAESWGTG RAVARIPRVR GGGTHRSGQG AFGNMCRGGR MFAPTKTWRR WHRRVNTTQK
RYAICSALAA SALPALVMSK GHRIEEVPEL PLVVEDKVEG YKKTKEAVLL LKKLKARNDI
KKVYASQRMR AGKGKMRNRR RIQRRGPCII YNEDNGIIKA FRNIPGITLL NVSKLNILKL
APGGHVGRFC IWTESAFRKL DELYGTWRKA ASLKSNYNLP MHKMINTDLS RILKSPEIQR
ALRAPRKKIH RRVLKKNPLK NLRIMLKLNP YAKTMRRNTI LRQARNHKLR VDKAAAAAAA
LQAKSDEKAA VAGKKPVVGK KGKKAAVGVK KQKKPLVGKK AAATKKPAPE KKPAEKKPTT
EEKKPAA
