MTRFR_MOUSE
ID MTRFR_MOUSE Reviewed; 184 AA.
AC Q80VP5; Q3US94; Q8BYK3; Q9CSJ6;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Mitochondrial translation release factor in rescue {ECO:0000305};
DE Flags: Precursor;
GN Name=Mtrfr {ECO:0000312|MGI:MGI:1919900};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-152 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP STRUCTURE BY NMR OF 21-124.
RX PubMed=22821833; DOI=10.1002/prot.24152;
RA Kogure H., Hikawa Y., Hagihara M., Tochio N., Koshiba S., Inoue Y.,
RA Guntert P., Kigawa T., Yokoyama S., Nameki N.;
RT "Solution structure and siRNA-mediated knockdown analysis of the
RT mitochondrial disease-related protein C12orf65.";
RL Proteins 80:2629-2642(2012).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80VP5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80VP5-2; Sequence=VSP_029604, VSP_029605;
CC -!- DOMAIN: The GGQ domain interacts with the peptidyltransferase center
CC (PTC) of the large ribosomal subunit to trigger nascent chain
CC hydrolysis. {ECO:0000269|PubMed:22821833}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK012682; BAB28408.3; -; mRNA.
DR EMBL; AK039255; BAC30294.1; -; mRNA.
DR EMBL; AK140664; BAE24439.1; -; mRNA.
DR EMBL; BC046909; AAH46909.1; -; mRNA.
DR CCDS; CCDS51647.1; -. [Q80VP5-1]
DR CCDS; CCDS51648.1; -. [Q80VP5-2]
DR RefSeq; NP_001128189.1; NM_001134717.2. [Q80VP5-1]
DR RefSeq; NP_082586.1; NM_028310.3. [Q80VP5-2]
DR PDB; 2RSM; NMR; -; A=21-124.
DR PDBsum; 2RSM; -.
DR AlphaFoldDB; Q80VP5; -.
DR BMRB; Q80VP5; -.
DR SMR; Q80VP5; -.
DR STRING; 10090.ENSMUSP00000076594; -.
DR iPTMnet; Q80VP5; -.
DR PhosphoSitePlus; Q80VP5; -.
DR EPD; Q80VP5; -.
DR MaxQB; Q80VP5; -.
DR PaxDb; Q80VP5; -.
DR PeptideAtlas; Q80VP5; -.
DR PRIDE; Q80VP5; -.
DR Antibodypedia; 31771; 58 antibodies from 16 providers.
DR DNASU; 72650; -.
DR Ensembl; ENSMUST00000077376; ENSMUSP00000076594; ENSMUSG00000047635. [Q80VP5-1]
DR Ensembl; ENSMUST00000111477; ENSMUSP00000107102; ENSMUSG00000047635. [Q80VP5-2]
DR GeneID; 72650; -.
DR KEGG; mmu:72650; -.
DR UCSC; uc008zpm.1; mouse. [Q80VP5-2]
DR UCSC; uc008zpn.2; mouse. [Q80VP5-1]
DR CTD; 91574; -.
DR MGI; MGI:1919900; Mtrfr.
DR VEuPathDB; HostDB:ENSMUSG00000047635; -.
DR eggNOG; KOG2726; Eukaryota.
DR GeneTree; ENSGT00390000012759; -.
DR HOGENOM; CLU_2078403_0_0_1; -.
DR InParanoid; Q80VP5; -.
DR OMA; WESSKNI; -.
DR OrthoDB; 1415962at2759; -.
DR PhylomeDB; Q80VP5; -.
DR TreeFam; TF323274; -.
DR BioGRID-ORCS; 72650; 7 hits in 72 CRISPR screens.
DR PRO; PR:Q80VP5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q80VP5; protein.
DR Bgee; ENSMUSG00000047635; Expressed in embryonic post-anal tail and 61 other tissues.
DR Genevisible; Q80VP5; MM.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Mitochondrion;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..98
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 99..184
FT /note="Mitochondrial translation release factor in rescue"
FT /id="PRO_0000311836"
FT REGION 60..124
FT /note="GGQ domain"
FT /evidence="ECO:0000269|PubMed:22821833"
FT REGION 132..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 130..178
FT /evidence="ECO:0000255"
FT MOTIF 74..76
FT /note="GGQ"
FT /evidence="ECO:0000269|PubMed:22821833"
FT COMPBIAS 153..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 98..128
FT /note="CHQTRSVDQNRKIARKVLQEKVDVFYNGENS -> VETGGEPRSAATAGFSQ
FT WACPFWHGDTANSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029604"
FT VAR_SEQ 129..184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029605"
FT CONFLICT 35
FT /note="L -> F (in Ref. 1; BAB28408)"
FT /evidence="ECO:0000305"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2RSM"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:2RSM"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:2RSM"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:2RSM"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2RSM"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2RSM"
FT HELIX 104..124
FT /evidence="ECO:0007829|PDB:2RSM"
SQ SEQUENCE 184 AA; 20787 MW; 4337CB91AEFE8780 CRC64;
MSSRSTWALL RLPLPLIRIC SGKWGLRLQE KPALLFPGMA ASTVQVAGRK DYPALLPLNE
SELEEQFVKG HGPGGQATNK TSNCVVLKHV PSGIVVKCHQ TRSVDQNRKI ARKVLQEKVD
VFYNGENSPV HKEKLEAERR KRERKKRAKE TLEKKKLLKE LREASQNITE KKADADGIPR
GFQE
