ID   RS3A_MACFA              Reviewed;         264 AA.
AC   Q4R4Z6;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=40S ribosomal protein S3a {ECO:0000255|HAMAP-Rule:MF_03122};
GN   Name=RPS3A {ECO:0000255|HAMAP-Rule:MF_03122}; ORFNames=QnpA-15704;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Parietal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB169748; BAE01829.1; -; mRNA.
DR   RefSeq; NP_001270826.1; NM_001283897.1.
DR   AlphaFoldDB; Q4R4Z6; -.
DR   SMR; Q4R4Z6; -.
DR   STRING; 9541.XP_005556120.1; -.
DR   GeneID; 101866348; -.
DR   CTD; 6189; -.
DR   eggNOG; KOG1628; Eukaryota.
DR   OrthoDB; 1207239at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:UniProtKB-UniRule.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
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: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   Pfam; PF01015; Ribosomal_S3Ae; 1.
DR   SMART; SM01397; 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_0000230764"
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;  29926 MW;  049E0F184DCD6666 CRC64;
     MAVGKNKRLT KGGKKGAKKK VVDPFSKKDW YDVKAPAMFN IRNIGKTLVT RTQGTKIASD
     GLKGHVFEVS LADLQNDEVA FRKFKLITED VQGKNCLTNF HGMDLTRDKM CSMVKKWQTM
     IEAHVDVKTT DGYLLRLFCV GFTKKRNNQI RKTSYAQHQQ VRQIRKKMME IMTREVQTND
     LKEVVNKLIP DSIGKDIEKA CQSIYPLHDV FVRKVKMLKK PKFELGKLME LHGEGSSSGK
     ATGDETGAKV ERADGYEPPV QESV