MTRFR_DANRE
ID MTRFR_DANRE Reviewed; 156 AA.
AC A5WUX7; A5WUX8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Mitochondrial translation release factor in rescue {ECO:0000305};
DE Flags: Precursor;
GN Name=mtrfr; ORFNames=si:ch211-275j6.5;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Part of a mitoribosome-associated quality control pathway
CC that prevents aberrant translation by responding to interruptions
CC during elongation. As heterodimer with MTRES1, ejects the unfinished
CC nascent chain and peptidyl transfer RNA (tRNA), respectively, from
CC stalled ribosomes. Recruitment of mitoribosome biogenesis factors to
CC these quality control intermediates suggests additional roles for
CC MTRES1 and MTRF during mitoribosome rescue.
CC {ECO:0000250|UniProtKB:Q9H3J6}.
CC -!- SUBUNIT: Interacts (via C-terminus) with MTRES1 (via S4 domain).
CC Associates with mitoribosomal S39 large subunit, peptidyl tRNA and
CC nascent chain. {ECO:0000250|UniProtKB:Q9H3J6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9H3J6}.
CC -!- DOMAIN: The GGQ domain interactS with the peptidyltransferase center
CC (PTC) of the large ribosomal subunit to trigger nascent chain
CC hydrolysis. {ECO:0000250|UniProtKB:Q9H3J6}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family, lacks the regions
CC that come into close contact with the mRNA in the ribosomal A-site and
CC determine the STOP codon specificity, suggesting a loss of codon
CC specificity for translation release factor activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAN87843.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CR847941; CAN87842.1; -; Genomic_DNA.
DR EMBL; CR847941; CAN87843.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001119948.1; NM_001126476.1.
DR AlphaFoldDB; A5WUX7; -.
DR SMR; A5WUX7; -.
DR STRING; 7955.ENSDARP00000129767; -.
DR PaxDb; A5WUX7; -.
DR Ensembl; ENSDART00000154507; ENSDARP00000129767; ENSDARG00000097803.
DR GeneID; 100004874; -.
DR KEGG; dre:100004874; -.
DR CTD; 91574; -.
DR ZFIN; ZDB-GENE-130109-1; mtrfr.
DR eggNOG; KOG2726; Eukaryota.
DR GeneTree; ENSGT00390000012759; -.
DR InParanoid; A5WUX7; -.
DR OrthoDB; 1415962at2759; -.
DR PhylomeDB; A5WUX7; -.
DR PRO; PR:A5WUX7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000097803; Expressed in testis and 21 other tissues.
DR ExpressionAtlas; A5WUX7; baseline.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0043023; F:ribosomal large subunit binding; ISS:UniProtKB.
DR GO; GO:0003747; F:translation release factor activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR Pfam; PF00472; RF-1; 1.
DR SUPFAM; SSF75620; SSF75620; 1.
PE 3: Inferred from homology;
KW Coiled coil; Mitochondrion; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..156
FT /note="Mitochondrial translation release factor in rescue"
FT /id="PRO_0000311837"
FT REGION 44..108
FT /note="GGQ domain"
FT /evidence="ECO:0000250|UniProtKB:Q80VP5"
FT REGION 114..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 100..141
FT /evidence="ECO:0000255"
FT MOTIF 58..60
FT /note="GGQ"
FT /evidence="ECO:0000250|UniProtKB:Q9H3J6"
SQ SEQUENCE 156 AA; 18184 MW; 92E031246F9C94BA CRC64;
MTLFFSHRLF TVWRLKCGVM DIGWPSVLPA AGKKYQIELP VVHEEELEEQ FVRGSGPGGQ
ATNKTSNCVV LRHIPSGIVV KCHETRSVDL NRKRAREILR EKLEVAYKGE ESELLKMKKE
SMQKKQDKRR KVNENIEKKR RFKEMLNSKQ EDDKST
