ID   RT03_ARATH              Reviewed;         556 AA.
AC   Q95749; A7KNJ9;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 3.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Ribosomal protein S3, mitochondrial;
GN   Name=RPS3; OrderedLocusNames=AtMg00090;
OS   Arabidopsis thaliana (Mouse-ear cress).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. C24;
RX   PubMed=8988169; DOI=10.1038/ng0197-57;
RA   Unseld M., Marienfeld J.R., Brandt P., Brennicke A.;
RT   "The mitochondrial genome of Arabidopsis thaliana contains 57 genes in
RT   366,924 nucleotides.";
RL   Nat. Genet. 15:57-61(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RX   PubMed=10611383; DOI=10.1073/pnas.96.26.15324;
RA   Giege P., Brennicke A.;
RT   "RNA editing in Arabidopsis mitochondria effects 441 C to U changes in
RT   ORFs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:15324-15329(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-556.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=8776901; DOI=10.2307/3870308;
RA   Sakamoto W., Kondo H., Murata M., Motoyoshi F.;
RT   "Altered mitochondrial gene expression in a maternal distorted leaf mutant
RT   of Arabidopsis induced by chloroplast mutator.";
RL   Plant Cell 8:1377-1390(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-539, AND RNA EDITING.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta; TISSUE=Rosette leaf;
RX   PubMed=17565941; DOI=10.1534/genetics.107.073585;
RA   Bentolila S., Elliott L.E., Hanson M.R.;
RT   "Genetic architecture of mitochondrial editing in Arabidopsis thaliana.";
RL   Genetics 178:1693-1708(2008).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- RNA EDITING: Modified_positions=22 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941}, 172 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941}, 296 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941}, 451 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941}, 512 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941}, 524 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941}, 527 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941}, 533 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941};
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC       {ECO:0000305}.
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; Y08501; CAA69755.3; ALT_SEQ; Genomic_DNA.
DR   EMBL; D84192; BAA12250.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; EF488942; ABS50654.1; -; mRNA.
DR   EMBL; EF488943; ABS50655.1; -; mRNA.
DR   RefSeq; NP_085481.1; NC_001284.2.
DR   PDB; 6XYW; EM; 3.86 A; Bb=1-556.
DR   PDBsum; 6XYW; -.
DR   AlphaFoldDB; Q95749; -.
DR   SMR; Q95749; -.
DR   BioGRID; 4; 1.
DR   IntAct; Q95749; 2.
DR   STRING; 3702.ATMG00090.1; -.
DR   PaxDb; Q95749; -.
DR   PeptideAtlas; Q95749; -.
DR   PRIDE; Q95749; -.
DR   Araport; ATMG00090; -.
DR   eggNOG; ENOG502QSWK; Eukaryota.
DR   InParanoid; Q95749; -.
DR   OrthoDB; 486424at2759; -.
DR   PRO; PR:Q95749; -.
DR   Proteomes; UP000006548; Mitochondrion (cv. C24).
DR   ExpressionAtlas; Q95749; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 3.30.1140.32; -; 1.
DR   InterPro; IPR009019; KH_sf_prok-type.
DR   InterPro; IPR001351; Ribosomal_S3_C.
DR   InterPro; IPR036419; Ribosomal_S3_C_sf.
DR   InterPro; IPR044954; RPS3_plant.
DR   PANTHER; PTHR35928; PTHR35928; 1.
DR   Pfam; PF00189; Ribosomal_S3_C; 1.
DR   SUPFAM; SSF54814; SSF54814; 1.
DR   SUPFAM; SSF54821; SSF54821; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA editing.
FT   CHAIN           1..556
FT                   /note="Ribosomal protein S3, mitochondrial"
FT                   /id="PRO_0000130310"
FT   CONFLICT        25
FT                   /note="E -> D (in Ref. 4; ABS50655/ABS50654)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   556 AA;  64876 MW;  86B367DB5648D1C0 CRC64;
     MARKGNPISV RLGKNRSSDS SWFSEYYYGK FVYQDVNLRS YFGSIRPPTR LTFGFRLGRC
     IILHFPKRTF IHFFLPRRPR RLKRREKTRP GKEKGRWWTT FGKAGPIECL HSSDDTEEER
     NEVRGRGARK RVESIRLDDR KKQNEIRGWP KKKQRYGYHD RLPSIKKNLS KLLRISGAFK
     HPKYAGVVND IAFLIENDDS FKKTKLFKLF FQNKSRSDGP TSYLRTLPAV RPSLNFLVMQ
     YFFNTKNQIN FDPVVVLNHF VAPGAAEPST MGRANAQGRS LQKRIRSRIA FFVESLTSEK
     KCLAEAKNRL THFIRLANDL RFAGTTKTTI SLFPFFGATF FFLRDGVGVY NNLDAREQLL
     NQLRVKCWNL VGKDKIMELI EKLKNLGGIE ELIKVIDMMI EIILRKRGIP YRYNSYFYEV
     KKMRSFLSNR TNTKTLIESV KIKSVYQSAS LIAQDISFQL KNKRRSFHSI FAKIVKEIPK
     GVEGIRICFS GRLKDAAEKA QTKCYKHRKT SCNVFNHKID YAPVEVFTRY GILGVKVWIS
     YSQKKGRRAI SETYEI