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RS3A_BOVIN
ID   RS3A_BOVIN              Reviewed;         264 AA.
AC   Q56JV9; A2V9E4; B0JYM2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=40S ribosomal protein S3a {ECO:0000255|HAMAP-Rule:MF_03122};
GN   Name=RPS3A {ECO:0000255|HAMAP-Rule:MF_03122};
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   TISSUE=Lymphoid epithelium;
RA   Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.;
RT   "Analysis of sequences obtained from constructed full-length bovine cDNA
RT   libraries.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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: May play a role during erythropoiesis through regulation of
CC       transcription factor DDIT3. {ECO:0000255|HAMAP-Rule:MF_03122}.
CC   -!- SUBUNIT: Component of the small ribosomal subunit. Mature ribosomes
CC       consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC       contains about 33 different proteins and 1 molecule of RNA (18S). The
CC       60S subunit contains about 49 different proteins and 3 molecules of RNA
CC       (28S, 5.8S and 5S). Identified in a IGF2BP1-dependent mRNP granule
CC       complex containing untranslated mRNAs. Binds with high affinity to
CC       IPO4. Interacts with DDIT3. {ECO:0000255|HAMAP-Rule:MF_03122}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122}.
CC       Nucleus {ECO:0000255|HAMAP-Rule:MF_03122}. Note=Localized in
CC       cytoplasmic mRNP granules containing untranslated mRNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_03122}.
CC   -!- PTM: ADP-ribosylated at Tyr-155 by PARP1 in presence of HPF1.
CC       {ECO:0000250|UniProtKB:P61247}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_03122}.
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DR   EMBL; AY911372; AAW82136.1; -; mRNA.
DR   EMBL; BC151408; AAI51409.1; -; mRNA.
DR   EMBL; BC102789; AAI02790.1; -; mRNA.
DR   RefSeq; NP_001029210.1; NM_001034038.1.
DR   AlphaFoldDB; Q56JV9; -.
DR   SMR; Q56JV9; -.
DR   STRING; 9913.ENSBTAP00000013079; -.
DR   PaxDb; Q56JV9; -.
DR   PeptideAtlas; Q56JV9; -.
DR   PRIDE; Q56JV9; -.
DR   Ensembl; ENSBTAT00000013079; ENSBTAP00000013079; ENSBTAG00000009908.
DR   GeneID; 282053; -.
DR   KEGG; bta:282053; -.
DR   CTD; 6189; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009908; -.
DR   VGNC; VGNC:55759; RPS3A.
DR   eggNOG; KOG1628; Eukaryota.
DR   GeneTree; ENSGT00390000018433; -.
DR   HOGENOM; CLU_062507_0_1_1; -.
DR   InParanoid; Q56JV9; -.
DR   OMA; GQNAYTK; -.
DR   OrthoDB; 1207239at2759; -.
DR   TreeFam; TF300037; -.
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 17.
DR   Bgee; ENSBTAG00000009908; Expressed in myometrium and 105 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:UniProtKB-UniRule.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:Ensembl.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03122; Ribosomal_S3Ae_euk; 1.
DR   InterPro; IPR027500; Ribosomal_S1/3_euk.
DR   InterPro; IPR001593; Ribosomal_S3Ae.
DR   InterPro; IPR018281; Ribosomal_S3Ae_CS.
DR   Pfam; PF01015; Ribosomal_S3Ae; 1.
DR   SMART; SM01397; Ribosomal_S3Ae; 1.
DR   PROSITE; PS01191; RIBOSOMAL_S3AE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ADP-ribosylation; Cytoplasm; Differentiation; Isopeptide bond;
KW   Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; Ubl conjugation.
FT   CHAIN           1..264
FT                   /note="40S ribosomal protein S3a"
FT                   /id="PRO_0000230763"
FT   REGION          232..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         34
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
FT   MOD_RES         56
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P97351"
FT   MOD_RES         155
FT                   /note="ADP-ribosyltyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
FT   MOD_RES         236
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
FT   MOD_RES         237
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97351"
FT   MOD_RES         249
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
FT   MOD_RES         256
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
FT   MOD_RES         263
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
FT   CROSSLNK        34
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
FT   CROSSLNK        249
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
SQ   SEQUENCE   264 AA;  29945 MW;  000037AE195F7A9D CRC64;
     MAVGKNKRLT KGGKKGAKKK VVDPFSKKDW YDVKAPAMFN IRNIGKTLVT RTQGTKIASD
     GLKGRVFEVS LADLQNDEVA FRKFKLITED VQGKNCLTNF HGMDLTRDKM CSMVKKWQTM
     IEAHVDVKTT DGYLLRLFCV GFTKKRNNQI RKTSYAQHQQ VRQIRKKMME IMTREVQTND
     LKEVVNKLIP DSIGKDIEKA CQSIYPLHDV FVRKVKMLKK PKFELGKLME LHGEGSSSGK
     ATGDETGAKV ERADGYEPPV QESV
 
 
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