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RS23_BOVIN
ID   RS23_BOVIN              Reviewed;         143 AA.
AC   Q3T199;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=40S ribosomal protein S23;
GN   Name=RPS23;
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].
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 ribosome, a large ribonucleoprotein complex
CC       responsible for the synthesis of proteins in the cell. The small
CC       ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC       encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC       molecules. The large subunit (LSU) contains the ribosomal catalytic
CC       site termed the peptidyl transferase center (PTC), which catalyzes the
CC       formation of peptide bonds, thereby polymerizing the amino acids
CC       delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC       leave the ribosome through a tunnel in the LSU and interact with
CC       protein factors that function in enzymatic processing, targeting, and
CC       the membrane insertion of nascent chains at the exit of the ribosomal
CC       tunnel. Plays an important role in translational accuracy.
CC       {ECO:0000250|UniProtKB:P62266}.
CC   -!- SUBUNIT: Component of the 40S small ribosomal subunit.
CC       {ECO:0000250|UniProtKB:P62266}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P62266}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P62266}. Rough endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q6SA96}. Note=Detected on cytosolic polysomes
CC       (By similarity). Detected in ribosomes that are associated with the
CC       rough endoplasmic reticulum (By similarity).
CC       {ECO:0000250|UniProtKB:P62266, ECO:0000250|UniProtKB:Q6SA96}.
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; BC102049; AAI02050.1; -; mRNA.
DR   RefSeq; NP_001029862.1; NM_001034690.2.
DR   AlphaFoldDB; Q3T199; -.
DR   SMR; Q3T199; -.
DR   STRING; 9913.ENSBTAP00000017770; -.
DR   PaxDb; Q3T199; -.
DR   PeptideAtlas; Q3T199; -.
DR   PRIDE; Q3T199; -.
DR   Ensembl; ENSBTAT00000017770; ENSBTAP00000017770; ENSBTAG00000013358.
DR   GeneID; 540129; -.
DR   KEGG; bta:540129; -.
DR   CTD; 6228; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013358; -.
DR   eggNOG; KOG1749; Eukaryota.
DR   GeneTree; ENSGT00550000074784; -.
DR   HOGENOM; CLU_115574_0_1_1; -.
DR   InParanoid; Q3T199; -.
DR   OMA; KFRWSQR; -.
DR   OrthoDB; 1402984at2759; -.
DR   TreeFam; TF300871; -.
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-72695; Formation of the ternary complex, and subsequently, the 43S complex.
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 7.
DR   Bgee; ENSBTAG00000013358; Expressed in adenohypophysis and 103 other tissues.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; ISS:UniProtKB.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR   GO; GO:0042788; C:polysomal ribosome; ISS:UniProtKB.
DR   GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
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:0034063; P:stress granule assembly; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   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_0000240295"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
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;  15808 MW;  8417A48B8CF0A8E5 CRC64;
     MGKCRGLRTA RKLRSHRRDQ KWHDKQYKKA HLGTALKANP FGGASHAKGI VLEKVGVEAK
     QPNSAIRKCV RVQLIKNGKK ITAFVPNDGC LNFIEENDEV LVAGFGRKGH AVGDIPGVRF
     KVVKVANVSL LALYKGKKER PRS
 
 
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