ID   RS3A_FELCA              Reviewed;         260 AA.
AC   P61246; P33443; P49241;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=40S ribosomal protein S3a {ECO:0000255|HAMAP-Rule:MF_03122};
DE   Flags: Fragment;
GN   Name=RPS3A {ECO:0000255|HAMAP-Rule:MF_03122};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thymic lymphoma;
RX   PubMed=8607819; DOI=10.1006/bbrc.1996.0458;
RA   Starkey C.R., Menon R.P., Prabhu S., Levy L.S.;
RT   "Primary sequence and evolutionary conservation of ribosomal protein genes
RT   from the domestic cat.";
RL   Biochem. Biophys. Res. Commun. 220:648-652(1996).
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-151 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; U22231; AAB01669.1; -; mRNA.
DR   PIR; PC4158; PC4158.
DR   AlphaFoldDB; P61246; -.
DR   SMR; P61246; -.
DR   STRING; 9685.ENSFCAP00000018613; -.
DR   eggNOG; KOG1628; Eukaryota.
DR   HOGENOM; CLU_062507_0_1_1; -.
DR   InParanoid; P61246; -.
DR   Proteomes; UP000011712; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
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..260
FT                   /note="40S ribosomal protein S3a"
FT                   /id="PRO_0000153523"
FT   REGION          228..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         30
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
FT   MOD_RES         52
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P97351"
FT   MOD_RES         151
FT                   /note="ADP-ribosyltyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
FT   MOD_RES         232
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
FT   MOD_RES         233
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97351"
FT   MOD_RES         245
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
FT   MOD_RES         252
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
FT   MOD_RES         259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
FT   CROSSLNK        30
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
FT   CROSSLNK        245
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P61247"
FT   NON_TER         1
SQ   SEQUENCE   260 AA;  29586 MW;  08F77EADFABE2012 CRC64;
     KNKRLTKGGK KGAKKKVVDP FSKKDWYDVK APAMFNIRNI GKTLVTRTQG TKIASDGLKG
     RVFEVSLADL QNDEVAFRKF KLITEDVQGK NCLTNFHGMD LTRDKMCSMV KKWQTMIEAH
     VDVKTTDGYL LRLFCVGFTK KRNNQIRKTS YAQHQQVRQI RKKMMEIMTR EVQTNDLKEV
     VNKLIPDSIG KDIEKACQSI YPLHDVFVRK VKMLKKPKFE LGKLMELHGE GSSSGKATGD
     ETGAKVERAD GYEPPVQESV