ID   RT23_BOVIN              Reviewed;         190 AA.
AC   Q2NL27; P82666;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=28S ribosomal protein S23, mitochondrial;
DE            Short=MRP-S23;
DE            Short=S23mt;
GN   Name=MRPS23 {ECO:0000312|EMBL:AAI11165.1};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1] {ECO:0000312|EMBL:AAI11165.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI11165.1};
RC   TISSUE=Liver {ECO:0000312|EMBL:AAI11165.1};
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 84-93 AND 124-133, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Liver {ECO:0000269|PubMed:10938081};
RX   PubMed=10938081; DOI=10.1074/jbc.m003596200;
RA   Koc E.C., Burkhart W., Blackburn K., Moseley A., Koc H., Spremulli L.L.;
RT   "A proteomics approach to the identification of mammalian mitochondrial
RT   small subunit ribosomal proteins.";
RL   J. Biol. Chem. 275:32585-32591(2000).
RN   [3] {ECO:0007744|PDB:3JD5}
RP   STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), SUBCELLULAR LOCATION,
RP   AND SUBUNIT.
RX   PubMed=24799711; DOI=10.1073/pnas.1401657111;
RA   Kaushal P.S., Sharma M.R., Booth T.M., Haque E.M., Tung C.S.,
RA   Sanbonmatsu K.Y., Spremulli L.L., Agrawal R.K.;
RT   "Cryo-EM structure of the small subunit of the mammalian mitochondrial
RT   ribosome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:7284-7289(2014).
CC   -!- SUBUNIT: Component of the mitochondrial ribosome small subunit (28S)
CC       which comprises a 12S rRNA and about 30 distinct proteins.
CC       {ECO:0000269|PubMed:10938081, ECO:0000269|PubMed:24799711}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10938081,
CC       ECO:0000269|PubMed:24799711}.
CC   -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC       mS23 family. {ECO:0000305}.
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DR   EMBL; BC111164; AAI11165.1; -; mRNA.
DR   RefSeq; NP_001039657.1; NM_001046192.2.
DR   PDB; 3JD5; EM; 7.00 A; b=1-190.
DR   PDB; 6NEQ; EM; 3.32 A; b=1-190.
DR   PDB; 6NF8; EM; 3.48 A; b=1-190.
DR   PDBsum; 3JD5; -.
DR   PDBsum; 6NEQ; -.
DR   PDBsum; 6NF8; -.
DR   AlphaFoldDB; Q2NL27; -.
DR   SMR; Q2NL27; -.
DR   CORUM; Q2NL27; -.
DR   IntAct; Q2NL27; 1.
DR   STRING; 9913.ENSBTAP00000016409; -.
DR   iPTMnet; Q2NL27; -.
DR   PaxDb; Q2NL27; -.
DR   PRIDE; Q2NL27; -.
DR   GeneID; 515228; -.
DR   KEGG; bta:515228; -.
DR   CTD; 51649; -.
DR   eggNOG; ENOG502RZIC; Eukaryota.
DR   InParanoid; Q2NL27; -.
DR   OrthoDB; 1115569at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; HDA:UniProtKB.
DR   GO; GO:0032543; P:mitochondrial translation; HDA:UniProtKB.
DR   InterPro; IPR019520; Ribosomal_S23.
DR   InterPro; IPR023611; Ribosomal_S23/S25_mit.
DR   PANTHER; PTHR15925; PTHR15925; 1.
DR   Pfam; PF10484; MRP-S23; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Mitochondrion;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y3D9"
FT   CHAIN           2..190
FT                   /note="28S ribosomal protein S23, mitochondrial"
FT                   /id="PRO_0000278129"
FT   REGION          137..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y3D9"
FT   MOD_RES         83
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VE22"
FT   MOD_RES         102
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y3D9"
FT   CONFLICT        131..132
FT                   /note="IL -> LI (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:6NEQ"
FT   HELIX           12..21
FT                   /evidence="ECO:0007829|PDB:6NEQ"
FT   HELIX           31..37
FT                   /evidence="ECO:0007829|PDB:6NEQ"
FT   HELIX           67..78
FT                   /evidence="ECO:0007829|PDB:6NEQ"
FT   HELIX           95..109
FT                   /evidence="ECO:0007829|PDB:6NEQ"
FT   HELIX           114..126
FT                   /evidence="ECO:0007829|PDB:6NEQ"
SQ   SEQUENCE   190 AA;  21594 MW;  FF4491AE6D03455B CRC64;
     MAGSRLETVG SIFTRTRDLI RAGVLKEKPL WFDVYNAFPP LREPVFRRPR LRYGKAKSPT
     QDIYYHEDQI RAKFYAAYGS GPKAFDLFNP NFKSTCQRFV EKYIELQKLG ETDEEKLFVE
     AGKALLAEGV ILRRVEKART QQEGSQVSRK SESMGVESQT ALEENPPLKE VPQAQHLESP
     GEESKGLSPP