ID   RS10_BOVIN              Reviewed;         165 AA.
AC   Q3T0F4;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=40S ribosomal protein S10;
GN   Name=RPS10;
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 40S ribosomal subunit. {ECO:0000250}.
CC   -!- SUBUNIT: Component of the small ribosomal subunit. Interacts with
CC       PRMT5. The methylated form interacts with NPM1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus
CC       {ECO:0000250}. Note=Localized in the granular component (GC) region of
CC       the nucleolus. Methylation is required for its localization in the GC
CC       region. Colocalizes with NPS1 in the GC region of the nucleolus (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Methylated by PRMT5. Methylation is necessary for its interaction
CC       with NPS1, its localization in the granular component (GC) region of
CC       the nucleolus, for the proper assembly of ribosomes, protein synthesis
CC       and optimal cell proliferation (By similarity). {ECO:0000250}.
CC   -!- PTM: Monoubiquitinated by ZNF598 when a ribosome has stalled during
CC       translation of poly(A) sequences, leading to preclude synthesis of a
CC       long poly-lysine tail and initiate the ribosome quality control (RQC)
CC       pathway to degrade the potentially detrimental aberrant nascent
CC       polypeptide. {ECO:0000250|UniProtKB:P46783}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS10 family.
CC       {ECO:0000305}.
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DR   EMBL; BC102416; AAI02417.1; -; mRNA.
DR   RefSeq; NP_001029888.1; NM_001034716.2.
DR   AlphaFoldDB; Q3T0F4; -.
DR   SMR; Q3T0F4; -.
DR   IntAct; Q3T0F4; 1.
DR   STRING; 9913.ENSBTAP00000056371; -.
DR   PeptideAtlas; Q3T0F4; -.
DR   PRIDE; Q3T0F4; -.
DR   Ensembl; ENSBTAT00000020719; ENSBTAP00000020719; ENSBTAG00000015598.
DR   GeneID; 540965; -.
DR   KEGG; bta:540965; -.
DR   CTD; 6204; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015598; -.
DR   VGNC; VGNC:55922; RPS10.
DR   eggNOG; KOG3344; Eukaryota.
DR   GeneTree; ENSGT00440000034918; -.
DR   HOGENOM; CLU_089349_3_1_1; -.
DR   InParanoid; Q3T0F4; -.
DR   OMA; GFNPEFR; -.
DR   OrthoDB; 1588066at2759; -.
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 23.
DR   Bgee; ENSBTAG00000015598; Expressed in blood and 108 other tissues.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR037447; Rps10.
DR   InterPro; IPR005326; S10_plectin_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR12146; PTHR12146; 1.
DR   Pfam; PF03501; S10_plectin; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT   CHAIN           1..165
FT                   /note="40S ribosomal protein S10"
FT                   /id="PRO_0000240292"
FT   REGION          92..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         12
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P63325"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P63325"
FT   MOD_RES         153
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P63325"
FT   MOD_RES         158
FT                   /note="Symmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P46783"
FT   MOD_RES         160
FT                   /note="Symmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P46783"
FT   CROSSLNK        138
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P46783"
FT   CROSSLNK        139
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P46783"
SQ   SEQUENCE   165 AA;  18898 MW;  64106DFCD97AABA3 CRC64;
     MLMPKKNRIA IYELLFKEGV MVAKKDVHMP KHPELADKNV PNLHVMKAMQ SLKSRGYVKE
     QFAWRHFYWY LTNEGIQYLR DYLHLPPEIV PATLRRSRPE TGRPRPKGLE GERPARLTRG
     EADRDTYRRS AVPPGADKKA EAGAGSATEF QFRGGFGRGR GQPPQ