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   24-JAN-2024, entry version 154.
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=(6R)-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:78530,
CC         ChEBI:CHEBI:78844, ChEBI:CHEBI:195366; 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; 10090-ENSMUSP00000074347; -.
DR   ProteomicsDB; 267386; -.
DR   Pumba; Q9D799; -.
DR   Antibodypedia; 25895; 202 antibodies from 15 providers.
DR   DNASU; 69606; -.
DR   Ensembl; ENSMUST00000074792.7; ENSMUSP00000074347.7; ENSMUSG00000059183.13.
DR   GeneID; 69606; -.
DR   KEGG; mmu:69606; -.
DR   UCSC; uc009qdh.2; mouse.
DR   AGR; MGI:1916856; -.
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; RKVWQNV; -.
DR   OrthoDB; 179280at2759; -.
DR   PhylomeDB; Q9D799; -.
DR   TreeFam; TF323405; -.
DR   BioGRID-ORCS; 69606; 14 hits in 78 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 246 other cell types or tissues.
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   Gene3D; 3.40.50.12230; -; 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   NCBIfam; TIGR00460; fmt; 1.
DR   PANTHER; PTHR11138; METHIONYL-TRNA FORMYLTRANSFERASE; 1.
DR   PANTHER; PTHR11138:SF5; METHIONYL-TRNA FORMYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
DR   Genevisible; Q9D799; MM.
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
//