RT22_BOVIN
ID RT22_BOVIN Reviewed; 359 AA.
AC P82649; Q2NL06;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=28S ribosomal protein S22, mitochondrial;
DE Short=MRP-S22;
DE Short=S22mt;
GN Name=MRPS22;
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 (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 104-115; 125-145; 279-290 AND 329-337, IDENTIFICATION
RP IN THE 28S MITOCHONDRIAL RIBOSOME, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
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 mS22 family. {ECO:0000305}.
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DR EMBL; BC111265; AAI11266.1; -; mRNA.
DR RefSeq; NP_001039784.1; NM_001046319.2.
DR PDB; 3JD5; EM; 7.00 A; a=1-359.
DR PDB; 6NEQ; EM; 3.32 A; a=1-359.
DR PDB; 6NF8; EM; 3.48 A; a=1-359.
DR PDBsum; 3JD5; -.
DR PDBsum; 6NEQ; -.
DR PDBsum; 6NF8; -.
DR AlphaFoldDB; P82649; -.
DR SMR; P82649; -.
DR CORUM; P82649; -.
DR IntAct; P82649; 1.
DR STRING; 9913.ENSBTAP00000056612; -.
DR PaxDb; P82649; -.
DR PRIDE; P82649; -.
DR GeneID; 532044; -.
DR KEGG; bta:532044; -.
DR CTD; 56945; -.
DR eggNOG; KOG3890; Eukaryota.
DR InParanoid; P82649; -.
DR OrthoDB; 845271at2759; -.
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:0003735; F:structural constituent of ribosome; HDA:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; HDA:UniProtKB.
DR InterPro; IPR019374; Ribosomal_S22_mit.
DR PANTHER; PTHR13071; PTHR13071; 1.
DR Pfam; PF10245; MRP-S22; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..359
FT /note="28S ribosomal protein S22, mitochondrial"
FT /id="PRO_0000087702"
FT CONFLICT 135
FT /note="T -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 107..124
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6NF8"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:6NEQ"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:6NF8"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 223..233
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 239..255
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 281..289
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 293..305
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 311..318
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:6NF8"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 338..352
FT /evidence="ECO:0007829|PDB:6NEQ"
SQ SEQUENCE 359 AA; 40665 MW; BB5D8424A5DA354D CRC64;
MATLRVSLSL WNLHAGSRGA GRVYFRARAR PRPGDLFQPL PGVCGAGTPC RGLCSEAESG
SPKIKKPTFM DEEVQSILIK MTGLDLLKIF KPAVQETKPP TYKLMTQAQL EEATRQAIEA
AKVRLKMPPV LEERTPINDV LAEDKILEGT ETGKYVFTDI SYSIPHRERF IVVREPSGTL
RKASWEERDR MIQIYFPKEG RRVLTPVIFR EENLQTMYSQ DRHVDVLNLC VAQFEPDSAD
YIKVHHQTYE DIDKYGKYDL LRSTRHFGGM AWYFVNKKKI DGLLIDQIQR DLVDDAASLV
QLYHILHPDG QSAQEAKEQA AEGLQLIKVF AKTEAQKGAY IELTLQAYQE AFISSSAAS
