RS3A_RAT
ID RS3A_RAT Reviewed; 264 AA.
AC P49242; P33443;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=40S ribosomal protein S3a {ECO:0000255|HAMAP-Rule:MF_03122};
DE AltName: Full=V-fos transformation effector protein;
DE Contains:
DE RecName: Full=40S ribosomal protein S3b;
GN Name=Rps3a; Synonyms=Fte-1, Fte1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1549582; DOI=10.1073/pnas.89.6.2200;
RA Kho C.J., Zarbl H.;
RT "Fte-1, a v-fos transformation effector gene, encodes the mammalian
RT homologue of a yeast gene involved in protein import into mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2200-2204(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 24-50.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8912649; DOI=10.1006/bbrc.1996.1629;
RA Chan Y.-L., Olvera J., Paz V., Wool I.G.;
RT "The primary structures of rat ribosomal proteins S3a (the V-Fos
RT transformation effector) and of S3b.";
RL Biochem. Biophys. Res. Commun. 228:141-147(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION IN SMALL RIBOSOMAL SUBUNIT.
RX PubMed=925037; DOI=10.1016/s0021-9258(17)38346-1;
RA Collatz E., Ulbrich N., Tsurugi K., Lightfoot H.N., MacKinlay W., Lin A.,
RA Wool I.G.;
RT "Isolation of eukaryotic ribosomal proteins. Purification and
RT characterization of the 40 S ribosomal subunit proteins Sa, Sc, S3a, S3b,
RT S5', S9, S10, S11, S12, S14, S15, S15', S16, S17, S18, S19, S20, S21, S26,
RT S27', and S29.";
RL J. Biol. Chem. 252:9071-9080(1977).
RN [5]
RP MASS SPECTROMETRY.
RX PubMed=8910435; DOI=10.1074/jbc.271.45.28189;
RA Louie D.F., Resing K.A., Lewis T.S., Ahn N.G.;
RT "Mass spectrometric analysis of 40 S ribosomal proteins from Rat-1
RT fibroblasts.";
RL J. Biol. Chem. 271:28189-28198(1996).
RN [6]
RP GENE NAME.
RX PubMed=9074506; DOI=10.1016/s0378-1119(96)00719-6;
RA Lecomte F., Szpirer J., Szpirer C.;
RT "The S3a ribosomal protein gene is identical to the Fte-1 (v-fos
RT transformation effector) gene and the TNF-alpha-induced TU-11 gene, and its
RT transcript level is altered in transformed and tumor cells.";
RL Gene 186:271-277(1997).
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: The protein designated S3b has the same amino acid sequence as S3a
CC except that it lacks the C-terminal 12 residues. It is probable that
CC S3a is converted by proteolysis, either physiologically or
CC fortuitously, to S3b.
CC -!- PTM: ADP-ribosylated at Tyr-155 by PARP1 in presence of HPF1.
CC {ECO:0000250|UniProtKB:P61247}.
CC -!- MASS SPECTROMETRY: [40S ribosomal protein S3a]: Mass=29815.3;
CC Mass_error=1.4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8910435};
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03122}.
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DR EMBL; M84716; AAA42335.1; -; mRNA.
DR EMBL; X75161; CAA53004.1; -; mRNA.
DR EMBL; BC058483; AAH58483.1; -; mRNA.
DR PIR; JC5250; JC5250.
DR RefSeq; NP_058849.1; NM_017153.1.
DR AlphaFoldDB; P49242; -.
DR SMR; P49242; -.
DR BioGRID; 247958; 5.
DR IntAct; P49242; 9.
DR MINT; P49242; -.
DR STRING; 10116.ENSRNOP00000016329; -.
DR iPTMnet; P49242; -.
DR PhosphoSitePlus; P49242; -.
DR jPOST; P49242; -.
DR PaxDb; P49242; -.
DR PRIDE; P49242; -.
DR Ensembl; ENSRNOT00000016329; ENSRNOP00000016329; ENSRNOG00000011893.
DR GeneID; 29288; -.
DR KEGG; rno:29288; -.
DR UCSC; RGD:62078; rat.
DR CTD; 6189; -.
DR RGD; 62078; Rps3a.
DR eggNOG; KOG1628; Eukaryota.
DR GeneTree; ENSGT00390000018433; -.
DR HOGENOM; CLU_062507_0_1_1; -.
DR InParanoid; P49242; -.
DR OMA; GQNAYTK; -.
DR OrthoDB; 1207239at2759; -.
DR PhylomeDB; P49242; -.
DR TreeFam; TF300037; -.
DR Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-RNO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-RNO-72649; Translation initiation complex formation.
DR Reactome; R-RNO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-RNO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-RNO-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-RNO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P49242; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011893; Expressed in thymus and 19 other tissues.
DR Genevisible; P49242; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0015935; C:small ribosomal subunit; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; IDA:RGD.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
DR GO; GO:0031369; F:translation initiation factor binding; IPI:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:RGD.
DR GO; GO:0045727; P:positive regulation of translation; IDA:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0006412; P:translation; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; ADP-ribosylation; Cytoplasm; Differentiation;
KW Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..264
FT /note="40S ribosomal protein S3a"
FT /id="PRO_0000030637"
FT CHAIN 1..252
FT /note="40S ribosomal protein S3b"
FT /id="PRO_0000030638"
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 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; 014537AE0C1E2E86 CRC64;
MAVGKNKRLT KGGKKGAKKK VVDPFSKKDW YDVKAPAMFN IRNIGKTLVT RTQGTKIASD
GLKGRVFEVS LADLQNDEVA FRKFKLITED VQGKNCLTNF HGMDLTRDKM CSMVKKWQTM
IEAHVDVKTT DGYLLRLFCV GFTKKRNNQI RKTSYAQHQQ VRQIRKKMME IMTREVQTND
LKEVVNKLIP DSIGKDIEKA CQSIYPLHDV FVRKVKMLKK PKFELGKLME LHGEGGSSGK
TTGDETGAKV ERADGYEPPV QESV
