TFB2M_MOUSE
ID TFB2M_MOUSE Reviewed; 396 AA.
AC Q3TL26; Q61669; Q8BTJ2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Dimethyladenosine transferase 2, mitochondrial {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9H5Q4};
DE AltName: Full=Mitochondrial 12S rRNA dimethylase 2;
DE AltName: Full=Mitochondrial transcription factor B2;
DE Short=mTFB2M;
DE Short=mtTFB2;
DE AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2;
DE Flags: Precursor;
GN Name=Tfb2m {ECO:0000312|MGI:MGI:107937};
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 [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lymphoma;
RA Wang B., Hunsperger J.P., Laib J., Fan D.;
RL Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Heart;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=12532263; DOI=10.1007/s00335-002-2218-z;
RA Rantanen A., Gaspari M., Falkenberg M., Gustafsson C.M., Larsson N.-G.;
RT "Characterization of the mouse genes for mitochondrial transcription
RT factors B1 and B2.";
RL Mamm. Genome 14:1-6(2003).
RN [4]
RP FUNCTION.
RX PubMed=15526033; DOI=10.1038/sj.emboj.7600465;
RA Gaspari M., Falkenberg M., Larsson N.-G., Gustafsson C.M.;
RT "The mitochondrial RNA polymerase contributes critically to promoter
RT specificity in mammalian cells.";
RL EMBO J. 23:4606-4614(2004).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent rRNA methyltransferase
CC which may methylate two specific adjacent adenosines in the loop of a
CC conserved hairpin near the 3'-end of 12S mitochondrial rRNA (By
CC similarity). Component of the mitochondrial transcription initiation
CC complex, composed at least of TFB2M, TFAM and POLRMT that is required
CC for basal transcription of mitochondrial DNA (PubMed:15526033). In this
CC complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M
CC induces structural changes in POLRMT to enable promoter opening and
CC trapping of the DNA non-template strand (PubMed:15526033). Stimulates
CC transcription independently of the methyltransferase activity (By
CC similarity). {ECO:0000250|UniProtKB:Q9H5Q4,
CC ECO:0000269|PubMed:15526033}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine in rRNA + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyladenosine in rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:58728, Rhea:RHEA-COMP:15198, Rhea:RHEA-COMP:15199,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449;
CC Evidence={ECO:0000250|UniProtKB:Q9H5Q4};
CC -!- SUBUNIT: Homodimer. Component of the mitochondrial transcription
CC initiation complex, composed at least of TFB2M, TFAM and POLRMT. In
CC this complex TFAM recruits POLRMT to the promoter whereas TFB2M induces
CC structural changes in POLRMT to enable promoter opening and trapping of
CC the DNA non-template strand. Interacts with mitochondrial RNA
CC polymerase POLRMT. Interacts with TFAM. {ECO:0000250|UniProtKB:Q9H5Q4}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12532263}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family. KsgA
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01026}.
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DR EMBL; M74555; AAA37817.1; -; mRNA.
DR EMBL; AK090106; BAC41095.1; -; mRNA.
DR EMBL; AK146563; BAE27262.1; -; mRNA.
DR EMBL; AK166717; BAE38967.1; -; mRNA.
DR EMBL; AK167930; BAE39934.1; -; mRNA.
DR EMBL; AK168970; BAE40774.1; -; mRNA.
DR EMBL; AK169138; BAE40917.1; -; mRNA.
DR CCDS; CCDS15561.1; -.
DR PIR; S27870; S27870.
DR RefSeq; NP_001317984.1; NM_001331055.1.
DR RefSeq; NP_032275.2; NM_008249.5.
DR AlphaFoldDB; Q3TL26; -.
DR SMR; Q3TL26; -.
DR BioGRID; 200317; 4.
DR STRING; 10090.ENSMUSP00000027769; -.
DR iPTMnet; Q3TL26; -.
DR PhosphoSitePlus; Q3TL26; -.
DR EPD; Q3TL26; -.
DR MaxQB; Q3TL26; -.
DR PaxDb; Q3TL26; -.
DR PeptideAtlas; Q3TL26; -.
DR PRIDE; Q3TL26; -.
DR ProteomicsDB; 259375; -.
DR Antibodypedia; 34721; 262 antibodies from 29 providers.
DR DNASU; 15278; -.
DR Ensembl; ENSMUST00000027769; ENSMUSP00000027769; ENSMUSG00000026492.
DR GeneID; 15278; -.
DR KEGG; mmu:15278; -.
DR UCSC; uc007dvl.1; mouse.
DR CTD; 64216; -.
DR MGI; MGI:107937; Tfb2m.
DR VEuPathDB; HostDB:ENSMUSG00000026492; -.
DR eggNOG; KOG0820; Eukaryota.
DR GeneTree; ENSGT00950000183142; -.
DR HOGENOM; CLU_051778_1_0_1; -.
DR InParanoid; Q3TL26; -.
DR OMA; RAQACKK; -.
DR OrthoDB; 1169941at2759; -.
DR PhylomeDB; Q3TL26; -.
DR TreeFam; TF325100; -.
DR Reactome; R-MMU-163282; Mitochondrial transcription initiation.
DR BioGRID-ORCS; 15278; 14 hits in 73 CRISPR screens.
DR ChiTaRS; Tfb2m; mouse.
DR PRO; PR:Q3TL26; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3TL26; protein.
DR Bgee; ENSMUSG00000026492; Expressed in hindlimb stylopod muscle and 67 other tissues.
DR ExpressionAtlas; Q3TL26; baseline and differential.
DR Genevisible; Q3TL26; MM.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0034246; F:mitochondrial transcription factor activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0006390; P:mitochondrial transcription; ISO:MGI.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR GO; GO:0006391; P:transcription initiation from mitochondrial promoter; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016861; TFB2M.
DR PANTHER; PTHR11727; PTHR11727; 1.
DR PANTHER; PTHR11727:SF13; PTHR11727:SF13; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SMART; SM00650; rADc; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Mitochondrion; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Transit peptide.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 44..396
FT /note="Dimethyladenosine transferase 2, mitochondrial"
FT /id="PRO_0000273180"
FT REGION 43..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..329
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9H5Q4"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 149
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT CONFLICT 12
FT /note="I -> L (in Ref. 1; AAA37817)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="R -> G (in Ref. 1; AAA37817)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="T -> M (in Ref. 1; AAA37817)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="Q -> P (in Ref. 2; BAC41095)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="E -> G (in Ref. 2; BAC41095)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="H -> P (in Ref. 2; BAC41095)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="N -> H (in Ref. 2; BAC41095)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="R -> P (in Ref. 2; BAC41095)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="Q -> P (in Ref. 2; BAC41095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 45864 MW; D276BD58D595F111 CRC64;
MRGPAMRLPP RIALSALARG PSCILGSGAA TRKDWQTRNR RGFSDFNIEP LPDSDLEESS
PWTSRNRSEP TRHIACKKAA RNLVRDLLEH QNPSRQIILE CNPGPGILTG ALLKAGARVV
AFESEKTFIP HLEPLQRNMD GELQVVHCDF FKMDPRYQEV VRPDVSSQAI FQNLGIKAVP
WSAGVPIKVF GILPYKHERR ILWKILFDLY SCESIYRYGR VELNMFVSEK EFRKLIATPK
RPDLYQVMAV LWQVACDVKF LHMEPWSSFS VHTENGHLEK SKHGESVNLL KQNLYLVRMT
PRRTLFTENL SPLNYDIFFH LVKHCFGKRN APIIRHLRSL STVDPINILR QIRKNPGDTA
ARMYPHDFKK LFETIEQSED SVFKWIYDYC PEDMEF
