RL4_PIG
ID RL4_PIG Reviewed; 101 AA.
AC Q29187;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=60S ribosomal protein L4;
DE AltName: Full=60S ribosomal protein L1;
DE Flags: Fragment;
GN Name=RPL4; Synonyms=RPL1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
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; F14498; CAA23090.1; -; mRNA.
DR STRING; 9823.ENSSSCP00000005322; -.
DR PeptideAtlas; Q29187; -.
DR eggNOG; KOG1475; Eukaryota.
DR InParanoid; Q29187; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR InterPro; IPR045240; Ribosomal_L4_euk/arch.
DR PANTHER; PTHR19431; PTHR19431; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Citrullination; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN <1..101
FT /note="60S ribosomal protein L4"
FT /id="PRO_0000129352"
FT REGION 34..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P36578"
FT MOD_RES 28
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D8E6"
FT MOD_RES 35
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D8E6"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36578"
FT CROSSLNK 2
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P36578"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P36578"
FT NON_TER 1
SQ SEQUENCE 101 AA; 11109 MW; A9097C9780CB15CE CRC64;
LKLNPYAKTM RRNTILRQXR XHKIRMDKAA ALKAKSGEKG VPDKKPVVEK KGKKAIGKKA
VGVKKQKKPL VGKKAVVTKK PAAEKKPAXK KPTTEEKKAV A