RT27_BOVIN
ID RT27_BOVIN Reviewed; 415 AA.
AC Q32PI8; P82677;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=28S ribosomal protein S27, mitochondrial {ECO:0000305};
DE Short=MRP-S27;
DE Short=S27mt;
DE AltName: Full=Mitochondrial ribosomal protein S27 {ECO:0000250|UniProtKB:Q92552};
DE Flags: Precursor;
GN Name=MRPS27 {ECO:0000250|UniProtKB:Q92552};
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:AAI08101.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI08101.1};
RC TISSUE=Ileum {ECO:0000312|EMBL:AAI08101.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 46-59; 125-154; 193-214; 316-327 AND 348-362, SUBUNIT,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Liver {ECO:0000269|PubMed:11344316};
RX PubMed=11344316; DOI=10.1110/ps.35301;
RA Koc E.C., Burkhart W., Blackburn K., Koc H., Moseley A., Spremulli L.L.;
RT "Identification of four proteins from the small subunit of the mammalian
RT mitochondrial ribosome using a proteomics approach.";
RL Protein Sci. 10:471-481(2001).
CC -!- FUNCTION: RNA-binding component of the mitochondrial small ribosomal
CC subunit (mt-SSU) that plays a role in mitochondrial protein synthesis.
CC Stimulates mitochondrial mRNA translation of subunit components of the
CC mitochondrial electron transport chain. Binds to the mitochondrial 12S
CC rRNA (12S mt-rRNA) and tRNA(Glu). Overexpressed in hepatocellular
CC carcinoma tissues compared with adjacent non-tumoral liver tissues.
CC {ECO:0000250|UniProtKB:Q92552}.
CC -!- SUBUNIT: Component of the mitochondrial ribosome small subunit (28S)
CC which comprises a 12S rRNA and about 30 distinct proteins
CC (PubMed:11344316). Interacts with NOA1 (By similarity). Interacts with
CC MIEF1 upstream open reading frame protein (By similarity). Interacts
CC with METTL17 (By similarity). {ECO:0000250|UniProtKB:Q8BK72,
CC ECO:0000250|UniProtKB:Q92552, ECO:0000269|PubMed:11344316}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92552}.
CC Mitochondrion {ECO:0000269|PubMed:11344316}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mS27 family. {ECO:0000305}.
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DR EMBL; BC108100; AAI08101.1; -; mRNA.
DR RefSeq; NP_001033197.1; NM_001038108.2.
DR PDB; 3JD5; EM; 7.00 A; e=1-415.
DR PDB; 6NEQ; EM; 3.32 A; e=1-415.
DR PDB; 6NF8; EM; 3.48 A; e=1-415.
DR PDBsum; 3JD5; -.
DR PDBsum; 6NEQ; -.
DR PDBsum; 6NF8; -.
DR AlphaFoldDB; Q32PI8; -.
DR SMR; Q32PI8; -.
DR CORUM; Q32PI8; -.
DR IntAct; Q32PI8; 1.
DR STRING; 9913.ENSBTAP00000002549; -.
DR PaxDb; Q32PI8; -.
DR PRIDE; Q32PI8; -.
DR GeneID; 514740; -.
DR KEGG; bta:514740; -.
DR CTD; 23107; -.
DR eggNOG; KOG4570; Eukaryota.
DR InParanoid; Q32PI8; -.
DR OrthoDB; 793417at2759; -.
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:0097177; F:mitochondrial ribosome binding; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR019266; MRPS27.
DR InterPro; IPR034913; MRPS27/PTCD2.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR21393; PTHR21393; 1.
DR Pfam; PF10037; MRP-S27; 1.
DR PROSITE; PS51375; PPR; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Mitochondrion; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; Transit peptide;
KW Translation regulation; tRNA-binding.
FT TRANSIT 1..8
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 9..415
FT /note="28S ribosomal protein S27, mitochondrial"
FT /id="PRO_0000261585"
FT REPEAT 105..139
FT /note="PPR 1"
FT REPEAT 140..175
FT /note="PPR 2"
FT REGION 292..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 368..415
FT /evidence="ECO:0000255"
FT COMPBIAS 300..319
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 201..202
FT /note="ER -> RN (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:6NEQ"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 218..237
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 256..264
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 276..290
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6NEQ"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 328..344
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 353..363
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 365..405
FT /evidence="ECO:0007829|PDB:6NEQ"
SQ SEQUENCE 415 AA; 47955 MW; AC765A6DBE9A9296 CRC64;
MAAPMVRRAI FLARNVLLPQ LSLAGKRYLL SAAYEDSRKW EARAKEDCHL ADLASLMDKT
YERKLPVSSL TISRFVDNIS SREEIDHAEY YLYKFRHSPN CWYLRNWTIH TWIRQCLKYG
AQDKALYTLV NKVQYGIFPD NYTFNLLMDH FIKKENYKDA LSVVFEIMMQ EAFEVPSTQL
LSLYVLYQCL AKKTDFSWEE ERNFGASLLL PGLKQKNSVG LSSQLYGYAL LGKVELQQGL
RAVYHNMPLL WRPGYLDRAL QVMEKVASSP EDGKLCREAL GVLDRALKAL TAPAQESPEE
QPQEGEESPA SEELMEQLDV EETEQSKLPR YVERYEALHS KLQALGKVES ESLLTLTTQL
VKEQLPTCEA EDIATYEQKL QEWHLELVNL IEREKEMREK ARLKHEARRA AKAAA
