FMT_MOUSE
ID FMT_MOUSE Reviewed; 386 AA.
AC Q9D799; E9QKZ0; Q8VE89;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Methionyl-tRNA formyltransferase, mitochondrial;
DE Short=MtFMT;
DE EC=2.1.2.9 {ECO:0000250|UniProtKB:Q96DP5};
DE Flags: Precursor;
GN Name=Mtfmt; Synonyms=Fmt;
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].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Methionyl-tRNA formyltransferase that formylates methionyl-
CC tRNA in mitochondria and is crucial for translation initiation.
CC {ECO:0000250|UniProtKB:Q96DP5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) =
CC (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-
CC tRNA(fMet); Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952, Rhea:RHEA-
CC COMP:9953, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:78530, ChEBI:CHEBI:78844; EC=2.1.2.9;
CC Evidence={ECO:0000250|UniProtKB:Q96DP5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24381;
CC Evidence={ECO:0000250|UniProtKB:Q96DP5};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O77480}.
CC -!- DOMAIN: Composed of an N- and a C-terminal domain. The N-terminal
CC domain carries the tetrahydrofolate (THF)-binding site and the C-
CC terminal domain is presumably involved in positioning the Met-tRNA
CC substrate for the formylation reaction.
CC -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000305}.
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DR EMBL; AK009430; BAB26282.1; -; mRNA.
DR EMBL; AC114645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019509; AAH19509.1; -; mRNA.
DR CCDS; CCDS23292.1; -.
DR RefSeq; NP_081410.2; NM_027134.3.
DR AlphaFoldDB; Q9D799; -.
DR SMR; Q9D799; -.
DR STRING; 10090.ENSMUSP00000074347; -.
DR iPTMnet; Q9D799; -.
DR PhosphoSitePlus; Q9D799; -.
DR EPD; Q9D799; -.
DR MaxQB; Q9D799; -.
DR PaxDb; Q9D799; -.
DR PRIDE; Q9D799; -.
DR ProteomicsDB; 267386; -.
DR Antibodypedia; 25895; 169 antibodies from 14 providers.
DR DNASU; 69606; -.
DR Ensembl; ENSMUST00000074792; ENSMUSP00000074347; ENSMUSG00000059183.
DR GeneID; 69606; -.
DR KEGG; mmu:69606; -.
DR UCSC; uc009qdh.2; mouse.
DR CTD; 123263; -.
DR MGI; MGI:1916856; Mtfmt.
DR VEuPathDB; HostDB:ENSMUSG00000059183; -.
DR eggNOG; KOG3082; Eukaryota.
DR GeneTree; ENSGT00390000017828; -.
DR HOGENOM; CLU_033347_0_0_1; -.
DR InParanoid; Q9D799; -.
DR OMA; FMPELHA; -.
DR OrthoDB; 963177at2759; -.
DR PhylomeDB; Q9D799; -.
DR TreeFam; TF323405; -.
DR BioGRID-ORCS; 69606; 14 hits in 73 CRISPR screens.
DR PRO; PR:Q9D799; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D799; protein.
DR Bgee; ENSMUSG00000059183; Expressed in renal medulla collecting duct and 243 other tissues.
DR Genevisible; Q9D799; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; ISS:UniProtKB.
DR GO; GO:0071951; P:conversion of methionyl-tRNA to N-formyl-methionyl-tRNA; ISS:UniProtKB.
DR CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR InterPro; IPR005794; Fmt.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR041711; Met-tRNA-FMT_N.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
DR TIGRFAMs; TIGR00460; fmt; 1.
PE 2: Evidence at transcript level;
KW Mitochondrion; Protein biosynthesis; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..386
FT /note="Methionyl-tRNA formyltransferase, mitochondrial"
FT /id="PRO_0000010094"
FT CONFLICT 40
FT /note="K -> M (in Ref. 1; BAB26282)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="F -> S (in Ref. 3; AAH19509)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 386 AA; 43092 MW; 74B0542C0ECA4D9D CRC64;
MLLPRCCWGR WLMGRRPRCS CQAPAGFDGK DGRGSRVREK PPWRVLFLGT DHFARETLRA
LHAARDGKEE KLIEKLEVVT VPSLSPKGLP VKQYAIQSQL PVYEWPDVGS GEYDVGVVAS
FGRLLSEALI LKFPYGILNV HPSCLPRWRG PAPIIHTVLH GDTVTGVTIM QIRPKRFDIG
PILQQETIPV PPKSTSKELE AVLSKLGANM LISVLKNLPE SLNNGRPQPA EGVTYAPKVS
AGTSCVKWEE QTSEQVLRLH LAIGDIVPLQ TLWMENTVKL LDLVEVNNSI LADPKLTGQT
VTPGFVVYHR PSQMLLVRCK DGWIGVRSVM LKKTLTATDF YNGYLHAWYQ KNSHAHPSQC
RFQTLRLPTK MQQKTKLLLC NSALSS
