ETKMT_MOUSE
ID ETKMT_MOUSE Reviewed; 255 AA.
AC Q80ZM3; B8JKU7; Q3V219; Q8VEL3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Electron transfer flavoprotein beta subunit lysine methyltransferase;
DE EC=2.1.1.- {ECO:0000269|PubMed:25023281};
DE AltName: Full=ETFB lysine methyltransferase;
DE Short=ETFB-KMT;
DE AltName: Full=Protein N-lysine methyltransferase METTL20;
DE Flags: Precursor;
GN Name=Mettl20 {ECO:0000312|MGI:MGI:2443575};
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=Head;
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].
RC STRAIN=FVB/N; TISSUE=Embryo, Mammary gland, and Mammary tumor;
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 [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25023281; DOI=10.1074/jbc.m114.580464;
RA Rhein V.F., Carroll J., He J., Ding S., Fearnley I.M., Walker J.E.;
RT "Human METTL20 methylates lysine residues adjacent to the recognition loop
RT of the electron transfer flavoprotein in mitochondria.";
RL J. Biol. Chem. 289:24640-24651(2014).
CC -!- FUNCTION: Protein-lysine methyltransferase that selectively
CC trimethylates the flavoprotein ETFB in mitochondria. Thereby, may
CC negatively regulate the function of ETFB in electron transfer from
CC Acyl-CoA dehydrogenases. {ECO:0000269|PubMed:25023281}.
CC -!- SUBUNIT: Interacts with HSPD1; this protein may possibly be a
CC methylation substrate. {ECO:0000250|UniProtKB:Q8IXQ9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IXQ9}.
CC Mitochondrion matrix {ECO:0000250|UniProtKB:Q8IXQ9}. Note=Concentrated
CC in cytoplasmic granular foci. {ECO:0000250|UniProtKB:Q8IXQ9}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. ETFBKMT
CC family. {ECO:0000305}.
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DR EMBL; AK132096; BAE20980.1; -; mRNA.
DR EMBL; CU207334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018279; AAH18279.1; -; mRNA.
DR EMBL; BC048711; AAH48711.1; -; mRNA.
DR EMBL; BC065807; AAH65807.1; -; mRNA.
DR CCDS; CCDS20715.1; -.
DR RefSeq; NP_001239023.1; NM_001252094.1.
DR RefSeq; NP_001239024.1; NM_001252095.1.
DR RefSeq; NP_001239025.1; NM_001252096.1.
DR RefSeq; NP_796075.2; NM_177101.5.
DR RefSeq; XP_017177126.1; XM_017321637.1.
DR AlphaFoldDB; Q80ZM3; -.
DR SMR; Q80ZM3; -.
DR STRING; 10090.ENSMUSP00000042102; -.
DR PhosphoSitePlus; Q80ZM3; -.
DR MaxQB; Q80ZM3; -.
DR PaxDb; Q80ZM3; -.
DR PRIDE; Q80ZM3; -.
DR Antibodypedia; 24685; 35 antibodies from 14 providers.
DR DNASU; 320204; -.
DR Ensembl; ENSMUST00000047531; ENSMUSP00000042102; ENSMUSG00000039958.
DR Ensembl; ENSMUST00000111551; ENSMUSP00000107176; ENSMUSG00000039958.
DR Ensembl; ENSMUST00000179873; ENSMUSP00000136167; ENSMUSG00000039958.
DR GeneID; 320204; -.
DR KEGG; mmu:320204; -.
DR UCSC; uc009etx.2; mouse.
DR CTD; 254013; -.
DR MGI; MGI:2443575; Mettl20.
DR VEuPathDB; HostDB:ENSMUSG00000039958; -.
DR eggNOG; ENOG502QUSY; Eukaryota.
DR GeneTree; ENSGT00940000162982; -.
DR InParanoid; Q80ZM3; -.
DR OMA; ILNCELN; -.
DR OrthoDB; 1585716at2759; -.
DR PhylomeDB; Q80ZM3; -.
DR TreeFam; TF314934; -.
DR Reactome; R-MMU-8876725; Protein methylation.
DR BioGRID-ORCS; 320204; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Etfbkmt; mouse.
DR PRO; PR:Q80ZM3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q80ZM3; protein.
DR Bgee; ENSMUSG00000039958; Expressed in left lobe of liver and 221 other tissues.
DR ExpressionAtlas; Q80ZM3; baseline and differential.
DR Genevisible; Q80ZM3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0008276; F:protein methyltransferase activity; IBA:GO_Central.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IMP:UniProtKB.
DR GO; GO:1904733; P:negative regulation of electron transfer activity; ISS:UniProtKB.
DR GO; GO:1904736; P:negative regulation of fatty acid beta-oxidation using acyl-CoA dehydrogenase; IMP:UniProtKB.
DR GO; GO:0018022; P:peptidyl-lysine methylation; ISO:MGI.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; IMP:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Mitochondrion; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q8IXQ9"
FT CHAIN 33..255
FT /note="Electron transfer flavoprotein beta subunit lysine
FT methyltransferase"
FT /id="PRO_0000318710"
FT CONFLICT 72
FT /note="W -> R (in Ref. 1; BAE20980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 28639 MW; 03007491AF6AEC4E CRC64;
MAFSLCWKAP RSPWSFLQAV NNGSPLFLWR TVGSCLDPKM KAYLEENTEV TSSGSLTPEI
QLRLLTPRCK FWWERADLWP YSDPYWAIYW PGGQALSRYL LDNPAVVRGK SVLDLGSGCG
ATAIAAKMSG ASKILANDID PIAGMAITLN CKLNGLNPFP VLTKNILNTQ QGKFDLIVLG
DMFYDEDLAD SLHLWLQNYF WTHGTRVLIG DPGRPQFSGH SIRHQLYQLV EYTLPEPTQQ
ENNGLTTSAV WDFHP
