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40S ribosomal protein S3 (EC 4.2.99.18)

 RS3_RAT                 Reviewed;         243 AA.
P62909; P17073; P47933;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
31-AUG-2004, sequence version 1.
12-SEP-2018, entry version 128.
RecName: Full=40S ribosomal protein S3;
EC=4.2.99.18 {ECO:0000250|UniProtKB:P23396};
Name=Rps3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 158-172.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=2275563; DOI=10.1016/0003-9861(90)90682-O;
Devi K.R.G., Chan Y.-L., Wool I.G.;
"The primary structure of rat ribosomal protein S3.";
Arch. Biochem. Biophys. 283:546-550(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION.
PubMed=7775413; DOI=10.1074/jbc.270.23.13620;
Kim J., Chubatsu L.S., Admon A., Stahl J., Fellous R., Linn S.;
"Implication of mammalian ribosomal protein S3 in the processing of
DNA damage.";
J. Biol. Chem. 270:13620-13629(1995).
-!- FUNCTION: Involved in translation as a component of the 40S small
ribosomal subunit (By similarity). Has endonuclease activity and
plays a role in repair of damaged DNA (PubMed:7775413). Cleaves
phosphodiester bonds of DNAs containing altered bases with broad
specificity and cleaves supercoiled DNA more efficiently than
relaxed DNA (By similarity). Displays high binding affinity for
7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by
reactive oxygen species (ROS) (By similarity). Has also been shown
to bind with similar affinity to intact and damaged DNA (By
similarity). Stimulates the N-glycosylase activity of the base
excision protein OGG1 (By similarity). Enhances the uracil
excision activity of UNG1 (By similarity). Also stimulates the
cleavage of the phosphodiester backbone by APEX1 (By similarity).
When located in the mitochondrion, reduces cellular ROS levels and
mitochondrial DNA damage. Has also been shown to negatively
regulate DNA repair in cells exposed to hydrogen peroxide (By
similarity). Plays a role in regulating transcription as part of
the NF-kappa-B p65-p50 complex where it binds to the RELA/p65
subunit, enhances binding of the complex to DNA and promotes
transcription of target genes (By similarity). Represses its own
translation by binding to its cognate mRNA (By similarity). Binds
to and protects TP53/p53 from MDM2-mediated ubiquitination (By
similarity). Involved in spindle formation and chromosome movement
during mitosis by regulating microtubule polymerization (By
similarity). Involved in induction of apoptosis through its role
in activation of CASP8 (By similarity). Induces neuronal apoptosis
by interacting with the E2F1 transcription factor and acting
synergistically with it to up-regulate pro-apoptotic proteins
BCL2L11/BIM and HRK/Dp5 (By similarity). Interacts with TRADD
following exposure to UV radiation and induces apoptosis by
caspase-dependent JNK activation (By similarity).
{ECO:0000250|UniProtKB:P23396, ECO:0000269|PubMed:7775413}.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate. {ECO:0000250|UniProtKB:P23396}.
-!- SUBUNIT: Component of the 40S small ribosomal subunit. Identified
in a IGF2BP1-dependent mRNP granule complex containing
untranslated mRNAs. Interacts with HNRPD. Interacts with PRMT1;
the interaction methylates RPS3. Interacts with SUMO1; the
interaction sumoylates RPS3. Interacts with UBC9. Interacts with
CDK1; the interaction phosphorylates RPS3. Interacts with PRKCD;
the interaction phosphorylates RPS3. Interacts with PKB/AKT; the
interaction phosphorylates RPS3. Interacts with E2F1; the
interaction occurs in the absence of nerve growth factor and
increases transcription of pro-apoptotic proteins BCL2L11/BIM and
HRK/Dp5. Interacts with the base excision repair proteins APEX1
and OGG1; interaction with OGG1 increases OGG1 N-glycosylase
activity. Interacts with UNG; the interaction increases the uracil
excision activity of UNG1. Interacts with HSP90; the interaction
prevents the ubiquitination and proteasome-dependent degradation
of RPS3 and is suppressed by increased ROS levels. Interacts with
TOM70; the interaction promotes translocation of RPS3 to the
mitochondrion. Interacts (via N-terminus) with RELA (via N-
terminus); the interaction enhances the DNA-binding activity of
the NF-kappa-B p65-p50 complex. Interacts with NFKBIA; the
interaction is direct and may bridge the interaction between RPS3
and RELA. Interacts with IKKB; the interaction phosphorylates RPS3
and enhances its translocation to the nucleus. Interacts (via KH
domain) with MDM2 and TP53. Interacts with TRADD. Interacts with
CRY1. {ECO:0000250|UniProtKB:P23396,
ECO:0000250|UniProtKB:P62908}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23396}.
Nucleus {ECO:0000250|UniProtKB:P23396}. Nucleus, nucleolus
{ECO:0000250|UniProtKB:P23396}. Mitochondrion inner membrane
{ECO:0000250|UniProtKB:P23396}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P23396}. Cytoplasm, cytoskeleton, spindle
{ECO:0000250|UniProtKB:P23396}. Note=In normal cells, located
mainly in the cytoplasm with small amounts in the nucleus but
translocates to the nucleus in cells undergoing apoptosis. Nuclear
translocation is induced by DNA damaging agents such as hydrogen
peroxide. Accumulates in the mitochondrion in response to
increased ROS levels. Localizes to the spindle during mitosis.
Localized in cytoplasmic mRNP granules containing untranslated
mRNAs. {ECO:0000250|UniProtKB:P23396,
ECO:0000250|UniProtKB:P62908}.
-!- PTM: Methylation by PRMT1 is required for import into the
nucleolus and for ribosome assembly.
{ECO:0000250|UniProtKB:P23396}.
-!- PTM: Sumoylation by SUMO1 enhances protein stability through
increased resistance to proteolysis. Sumoylation occurs at one or
more of the three consensus sites, Lys-18, Lys-214 and Lys-230.
{ECO:0000250|UniProtKB:P23396}.
-!- PTM: Phosphorylation at Thr-221 by CDK1 occurs mainly in G2/M
phase. Phosphorylation by PRKCD occurs on a non-ribosomal-
associated form which results in translocation of RPS3 to the
nucleus and enhances its endonuclease activity. Phosphorylated on
Ser-209 by IKKB in response to activation of the NF-kappa-B p65-
p50 complex which enhances the association of RPS3 with importin-
alpha and mediates the nuclear translocation of RPS3.
Phosphorylation by MAPK is required for translocation to the
nucleus following exposure of cells to DNA damaging agents such as
hydrogen peroxide. Phosphorylation by PKB/AKT mediates RPS3
nuclear translocation, enhances RPS3 endonuclease activity and
suppresses RPS3-induced neuronal apoptosis.
{ECO:0000250|UniProtKB:P23396}.
-!- PTM: Ubiquitinated. This is prevented by interaction with HSP90
which stabilizes the protein. Monoubiquitinated at Lys-214 by
ZNF598 when a ribosome has stalled during translation of poly(A)
sequences, leading to preclude synthesis of a long poly-lysine
tail and initiate the ribosome quality control (RQC) pathway to
degrade the potentially detrimental aberrant nascent polypeptide.
{ECO:0000250|UniProtKB:P23396}.
-!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X51536; CAA35916.1; -; mRNA.
EMBL; BC088450; AAH88450.1; -; mRNA.
PIR; S13882; R3RT3.
RefSeq; NP_001009239.1; NM_001009239.1.
UniGene; Rn.127805; -.
ProteinModelPortal; P62909; -.
SMR; P62909; -.
BioGrid; 250818; 5.
IntAct; P62909; 4.
MINT; P62909; -.
STRING; 10116.ENSRNOP00000023935; -.
iPTMnet; P62909; -.
PhosphoSitePlus; P62909; -.
PaxDb; P62909; -.
PRIDE; P62909; -.
Ensembl; ENSRNOT00000023935; ENSRNOP00000023935; ENSRNOG00000017418.
GeneID; 140654; -.
KEGG; rno:140654; -.
UCSC; RGD:619888; rat.
CTD; 6188; -.
RGD; 619888; Rps3.
eggNOG; KOG3181; Eukaryota.
eggNOG; COG0092; LUCA.
GeneTree; ENSGT00390000008610; -.
HOGENOM; HOG000210611; -.
HOVERGEN; HBG002195; -.
InParanoid; P62909; -.
KO; K02985; -.
OMA; AVRHVLM; -.
OrthoDB; EOG091G0I8D; -.
PhylomeDB; P62909; -.
TreeFam; TF300901; -.
PRO; PR:P62909; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000017418; Expressed in 10 organ(s), highest expression level in spleen.
Genevisible; P62909; RN.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0012505; C:endomembrane system; IDA:RGD.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:UniProtKB.
GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0031334; P:positive regulation of protein complex assembly; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006412; P:translation; IC:RGD.
Gene3D; 3.30.1140.32; -; 1.
Gene3D; 3.30.300.20; -; 1.
InterPro; IPR015946; KH_dom-like_a/b.
InterPro; IPR004044; KH_dom_type_2.
InterPro; IPR009019; KH_sf_prok-type.
InterPro; IPR001351; Ribosomal_S3_C.
InterPro; IPR036419; Ribosomal_S3_C_sf.
InterPro; IPR018280; Ribosomal_S3_CS.
InterPro; IPR005703; Ribosomal_S3_euk/arc.
Pfam; PF07650; KH_2; 1.
Pfam; PF00189; Ribosomal_S3_C; 1.
SUPFAM; SSF54814; SSF54814; 1.
SUPFAM; SSF54821; SSF54821; 1.
TIGRFAMs; TIGR01008; uS3_euk_arch; 1.
PROSITE; PS50823; KH_TYPE_2; 1.
PROSITE; PS00548; RIBOSOMAL_S3; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; Cell cycle; Cell division; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing; DNA damage;
DNA repair; DNA-binding; Isopeptide bond; Lyase; Membrane;
Methylation; Mitochondrion; Mitochondrion inner membrane; Mitosis;
Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
Ribosomal protein; RNA-binding; Transcription;
Transcription regulation; Translation regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P23396}.
CHAIN 2 243 40S ribosomal protein S3.
/FTId=PRO_0000130322.
DOMAIN 21 92 KH type-2. {ECO:0000255|PROSITE-
ProRule:PRU00118}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P23396}.
MOD_RES 6 6 Phosphoserine; by PKC/PRKCD.
{ECO:0000250|UniProtKB:P23396}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000250|UniProtKB:P23396}.
MOD_RES 42 42 Phosphothreonine; by MAPK.
{ECO:0000250|UniProtKB:P23396}.
MOD_RES 62 62 N6-acetyllysine.
{ECO:0000250|UniProtKB:P23396}.
MOD_RES 64 64 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000250|UniProtKB:P23396}.
MOD_RES 65 65 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000250|UniProtKB:P23396}.
MOD_RES 67 67 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000250|UniProtKB:P23396}.
MOD_RES 70 70 Phosphothreonine; by PKB.
{ECO:0000250|UniProtKB:P23396}.
MOD_RES 104 104 Phosphoserine.
{ECO:0000250|UniProtKB:P23396}.
MOD_RES 132 132 N6-succinyllysine.
{ECO:0000250|UniProtKB:P62908}.
MOD_RES 209 209 Phosphoserine; by IKKB.
{ECO:0000250|UniProtKB:P23396}.
MOD_RES 220 220 Phosphothreonine.
{ECO:0000250|UniProtKB:P23396}.
MOD_RES 221 221 Phosphothreonine; by CDK1 and PKC/PRKCD.
{ECO:0000250|UniProtKB:P23396}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000250|UniProtKB:P23396}.
MOD_RES 242 242 Phosphothreonine.
{ECO:0000250|UniProtKB:P23396}.
CROSSLNK 90 90 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P23396}.
CROSSLNK 202 202 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P23396}.
CROSSLNK 214 214 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P23396}.
CROSSLNK 214 214 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P23396}.
CROSSLNK 230 230 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P23396}.
SEQUENCE 243 AA; 26674 MW; 6B9BB34FDEE04AAF CRC64;
MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII LATRTQNVLG
EKGRRIRELT AVVQKRFGFP EGSVELYAEK VATRGLCAIA QAESLRYKLL GGLAVRRACY
GVLRFIMESG AKGCEVVVSG KLRGQRAKSM KFVDGLMIHS GDPVNYYVDT AVRHVLLRQG
VLGIKVKIML PWDPSGKIGP KKPLPDHVSI VEPKDEILPT TPISEQKGGK PEPPAMPQPV
PTA


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