RS23_PIG
ID RS23_PIG Reviewed; 143 AA.
AC Q6SA96;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=40S ribosomal protein S23;
GN Name=RPS23;
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 [MRNA].
RC TISSUE=Longissimus muscle;
RA Tian X., Li J., Chen Y.;
RT "Cloning and expression of ribosomal protein S23 in pig.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH ASFV UBCV1 (MICROBIAL INFECTION).
RX PubMed=33384682; DOI=10.3389/fmicb.2020.622907;
RA Barrado-Gil L., Del Puerto A., Munoz-Moreno R., Galindo I.,
RA Cuesta-Geijo M.A., Urquiza J., Nistal-Villan E., Maluquer de Motes C.,
RA Alonso C.;
RT "African Swine Fever Virus Ubiquitin-Conjugating Enzyme Interacts With Host
RT Translation Machinery to Regulate the Host Protein Synthesis.";
RL Front. Microbiol. 11:622907-622907(2020).
RN [3] {ECO:0007744|PDB:3J7P, ECO:0007744|PDB:3J7R}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=24930395; DOI=10.1016/j.cell.2014.05.024;
RA Voorhees R.M., Fernandez I.S., Scheres S.H., Hegde R.S.;
RT "Structure of the mammalian ribosome-Sec61 complex to 3.4 A resolution.";
RL Cell 157:1632-1643(2014).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell
CC (PubMed:24930395). The small ribosomal subunit (SSU) binds messenger
CC RNAs (mRNAs) and translates the encoded message by selecting cognate
CC aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU)
CC contains the ribosomal catalytic site termed the peptidyl transferase
CC center (PTC), which catalyzes the formation of peptide bonds, thereby
CC polymerizing the amino acids delivered by tRNAs into a polypeptide
CC chain. The nascent polypeptides leave the ribosome through a tunnel in
CC the LSU and interact with protein factors that function in enzymatic
CC processing, targeting, and the membrane insertion of nascent chains at
CC the exit of the ribosomal tunnel. Plays an important role in
CC translational accuracy (By similarity). {ECO:0000250|UniProtKB:P62266,
CC ECO:0000269|PubMed:24930395}.
CC -!- SUBUNIT: Component of the 40S small ribosomal subunit.
CC {ECO:0000269|PubMed:24930395}.
CC -!- SUBUNIT: (Microbial infection) Interacts with the African swine fever
CC virus (ASFV) ubiquitin-conjugating enzyme UBCv1; this interaction
CC probably plays a role in the viral regulation of host protein
CC synthesis. {ECO:0000269|PubMed:33384682}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P62266}. Cytoplasm
CC {ECO:0000269|PubMed:24930395}. Rough endoplasmic reticulum
CC {ECO:0000269|PubMed:24930395}. Note=Detected on cytosolic polysomes (By
CC similarity). Detected in ribosomes that are associated with the rough
CC endoplasmic reticulum (PubMed:24930395). {ECO:0000250|UniProtKB:P62266,
CC ECO:0000269|PubMed:24930395}.
CC -!- PTM: Hydroxylation at Pro-62 affects translation termination
CC efficiency. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC {ECO:0000305}.
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DR EMBL; AY461380; AAR22386.1; -; mRNA.
DR RefSeq; NP_998929.1; NM_213764.1.
DR PDB; 3J7P; EM; 3.50 A; SX=1-143.
DR PDB; 3J7R; EM; 3.90 A; SX=1-143.
DR PDBsum; 3J7P; -.
DR PDBsum; 3J7R; -.
DR AlphaFoldDB; Q6SA96; -.
DR SMR; Q6SA96; -.
DR STRING; 9823.ENSSSCP00000015028; -.
DR PaxDb; Q6SA96; -.
DR PeptideAtlas; Q6SA96; -.
DR PRIDE; Q6SA96; -.
DR GeneID; 396638; -.
DR KEGG; ssc:396638; -.
DR CTD; 6228; -.
DR eggNOG; KOG1749; Eukaryota.
DR InParanoid; Q6SA96; -.
DR OrthoDB; 1402984at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0098556; C:cytoplasmic side of rough endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; ISS:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:1990145; P:maintenance of translational fidelity; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; ISS:UniProtKB.
DR CDD; cd03367; Ribosomal_S23; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006032; Ribosomal_S12/S23.
DR InterPro; IPR005680; Ribosomal_S23_euk/arc.
DR PANTHER; PTHR11652; PTHR11652; 1.
DR Pfam; PF00164; Ribosom_S12_S23; 1.
DR PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00982; uS12_E_A; 1.
DR PROSITE; PS00055; RIBOSOMAL_S12; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Endoplasmic reticulum; Hydroxylation;
KW Isopeptide bond; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..143
FT /note="40S ribosomal protein S23"
FT /id="PRO_0000146459"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62267"
FT MOD_RES 62
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 135
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62266"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62266"
SQ SEQUENCE 143 AA; 15817 MW; 84009485BCE9A8E5 CRC64;
MGKCRGLRTA RKLRSHRRDH KWHDKQYKKA HLGTALKANP FGGASHAKGI VLEKVGVEAK
QPNSAIRKCV RVQLIKNGKK ITAFVPNDGC LNFIEENDEV LVAGFGRKGH AVGDIPGVRF
KVVKVANVSL LALYKGKKER PRS
