RT02_BOVIN
ID RT02_BOVIN Reviewed; 293 AA.
AC P82923; A6H6X0;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=28S ribosomal protein S2, mitochondrial;
DE Short=MRP-S2;
DE Short=S2mt;
GN Name=MRPS2;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 90-99, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=11279123; DOI=10.1074/jbc.m100727200;
RA Koc E.C., Burkhart W., Blackburn K., Moseley A., Spremulli L.L.;
RT "The small subunit of the mammalian mitochondrial ribosome: identification
RT of the full complement of ribosomal proteins present.";
RL J. Biol. Chem. 276:19363-19374(2001).
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 -!- FUNCTION: Required for mitoribosome formation and stability, and
CC mitochondrial translation. {ECO:0000250|UniProtKB:Q9Y399}.
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:11279123, ECO:0000269|PubMed:24799711}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11279123,
CC ECO:0000269|PubMed:24799711}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000305}.
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DR EMBL; BC146028; AAI46029.1; -; mRNA.
DR RefSeq; NP_001092347.1; NM_001098877.2.
DR PDB; 3JD5; EM; 7.00 A; B=1-293.
DR PDB; 6NEQ; EM; 3.32 A; B=1-293.
DR PDB; 6NF8; EM; 3.48 A; B=1-293.
DR PDBsum; 3JD5; -.
DR PDBsum; 6NEQ; -.
DR PDBsum; 6NF8; -.
DR AlphaFoldDB; P82923; -.
DR SMR; P82923; -.
DR CORUM; P82923; -.
DR IntAct; P82923; 2.
DR STRING; 9913.ENSBTAP00000007473; -.
DR PaxDb; P82923; -.
DR PRIDE; P82923; -.
DR Ensembl; ENSBTAT00000007473; ENSBTAP00000007473; ENSBTAG00000005688.
DR GeneID; 505681; -.
DR KEGG; bta:505681; -.
DR CTD; 51116; -.
DR VEuPathDB; HostDB:ENSBTAG00000005688; -.
DR VGNC; VGNC:31660; MRPS2.
DR eggNOG; KOG0832; Eukaryota.
DR GeneTree; ENSGT00390000017382; -.
DR HOGENOM; CLU_040318_3_0_1; -.
DR InParanoid; P82923; -.
DR OMA; SYIDRAY; -.
DR OrthoDB; 573006at2759; -.
DR TreeFam; TF313480; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000005688; Expressed in laryngeal cartilage and 105 other tissues.
DR ExpressionAtlas; P82923; baseline.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; HDA:UniProtKB.
DR GO; GO:0061668; P:mitochondrial ribosome assembly; ISS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; HDA:UniProtKB.
DR CDD; cd01425; RPS2; 1.
DR HAMAP; MF_00291_B; Ribosomal_S2_B; 1.
DR InterPro; IPR001865; Ribosomal_S2.
DR InterPro; IPR005706; Ribosomal_S2_bac/mit/plastid.
DR InterPro; IPR018130; Ribosomal_S2_CS.
DR InterPro; IPR023591; Ribosomal_S2_flav_dom_sf.
DR PANTHER; PTHR12534; PTHR12534; 1.
DR Pfam; PF00318; Ribosomal_S2; 2.
DR PRINTS; PR00395; RIBOSOMALS2.
DR SUPFAM; SSF52313; SSF52313; 1.
DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..293
FT /note="28S ribosomal protein S2, mitochondrial"
FT /id="PRO_0000134342"
FT REGION 21..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:6NEQ"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:6NF8"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6NEQ"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 107..126
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:6NEQ"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:6NF8"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:6NF8"
FT HELIX 232..260
FT /evidence="ECO:0007829|PDB:6NEQ"
SQ SEQUENCE 293 AA; 31729 MW; 99DF74A062564211 CRC64;
MATGAVLPRL LGAGVRAAPR GRAAQRGRTL GSAAAAAARE PERDSDRSAR ILSEPLKHSD
FFNVKELFSV RSLFNARVHL GHKAGCRHRF MEPYIFGSRL GQDIIDLEQT ATHLQLALNF
TAHVAFRGGI ILFVSRARQF SHLIESTARS CGEYAHTRYF KGGLLTNAPL LLGARVRLPD
LIIFLHTLNN VFEPHVAVRD AAKMSIPTVG VVDTNCNPCL ITYPVPGNDD SPPAVQLFCQ
LFQTAVTRAK EKRRQLEALY RLQGAPGPHP ANPAAPGAPS PGAQAQLGMG HSP
