EFMT3_MOUSE
ID EFMT3_MOUSE Reviewed; 232 AA.
AC D3YWP0;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=EEF1A lysine methyltransferase 3 {ECO:0000250|UniProtKB:Q96AZ1};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q96AZ1};
DE AltName: Full=Methyltransferase-like protein 21B {ECO:0000312|MGI:MGI:3645330};
DE AltName: Full=Protein-lysine methyltransferase METTL21B {ECO:0000250|UniProtKB:Q96AZ1};
GN Name=Eef1akmt3 {ECO:0000250|UniProtKB:Q96AZ1};
GN Synonyms=Fam119b {ECO:0000312|MGI:MGI:3645330},
GN Mettl21b {ECO:0000312|MGI:MGI:3645330};
GN ORFNames=mCG_5197 {ECO:0000312|EMBL:EDL24461.1};
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=28108655; DOI=10.1093/nar/gkx002;
RA Malecki J., Aileni V.K., Ho A.Y., Schwarz J., Moen A., Soerensen V.,
RA Nilges B.S., Jakobsson M.E., Leidel S.A., Falnes P.O.;
RT "The novel lysine specific methyltransferase METTL21B affects mRNA
RT translation through inducible and dynamic methylation of Lys-165 in human
RT eukaryotic elongation factor 1 alpha (eEF1A).";
RL Nucleic Acids Res. 45:4370-4389(2017).
CC -!- FUNCTION: Protein-lysine methyltransferase that selectively mono-,
CC di- and trimethylates 'Lys-165' of the translation elongation factors
CC EEF1A1 and EEF1A2 in an aminoacyl-tRNA and GTP-dependent manner (By
CC similarity). EEF1A1 methylation by EEF1AKMT3 is dynamic as well as
CC inducible by stress conditions, such as ER-stress, and plays a
CC regulatory role on mRNA translation (PubMed:28108655).
CC {ECO:0000250|UniProtKB:Q96AZ1, ECO:0000269|PubMed:28108655}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961;
CC Evidence={ECO:0000250|UniProtKB:Q96AZ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC Evidence={ECO:0000250|UniProtKB:Q96AZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000250|UniProtKB:Q96AZ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51737;
CC Evidence={ECO:0000250|UniProtKB:Q96AZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+)
CC + N(6),N(6)-dimethyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:54196, Rhea:RHEA-COMP:13053, Rhea:RHEA-COMP:13827,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000250|UniProtKB:Q96AZ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54197;
CC Evidence={ECO:0000250|UniProtKB:Q96AZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6)-dimethyl-L-lysyl-[protein] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54200, Rhea:RHEA-COMP:13826, Rhea:RHEA-
CC COMP:13827, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61961, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000250|UniProtKB:Q96AZ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54201;
CC Evidence={ECO:0000250|UniProtKB:Q96AZ1};
CC -!- SUBUNIT: Interacts with members of the heat shock protein 70 and 90
CC families and of the TCP-1 chaperonin family, as well as with HSPD1,
CC STIP1 and tubulin; at least some of these proteins may be methylation
CC substrates. {ECO:0000250|UniProtKB:Q96AZ1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96AZ1}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q96AZ1}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL21
CC family. {ECO:0000305}.
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DR EMBL; CH466578; EDL24461.1; -; Genomic_DNA.
DR EMBL; AC134329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS56752.1; -.
DR RefSeq; NP_001191965.1; NM_001205036.1.
DR AlphaFoldDB; D3YWP0; -.
DR SMR; D3YWP0; -.
DR STRING; 10090.ENSMUSP00000111939; -.
DR PhosphoSitePlus; D3YWP0; -.
DR PaxDb; D3YWP0; -.
DR PRIDE; D3YWP0; -.
DR ProteomicsDB; 277554; -.
DR Antibodypedia; 28949; 19 antibodies from 9 providers.
DR Ensembl; ENSMUST00000116231; ENSMUSP00000111939; ENSMUSG00000080115.
DR GeneID; 100504608; -.
DR KEGG; mmu:100504608; -.
DR UCSC; uc029rjq.1; mouse.
DR CTD; 25895; -.
DR MGI; MGI:3645330; Eef1akmt3.
DR VEuPathDB; HostDB:ENSMUSG00000080115; -.
DR eggNOG; KOG2793; Eukaryota.
DR GeneTree; ENSGT00940000161297; -.
DR HOGENOM; CLU_055721_4_0_1; -.
DR InParanoid; D3YWP0; -.
DR OMA; HRDDKQN; -.
DR OrthoDB; 1494909at2759; -.
DR PhylomeDB; D3YWP0; -.
DR TreeFam; TF313206; -.
DR BioGRID-ORCS; 100504608; 1 hit in 72 CRISPR screens.
DR PRO; PR:D3YWP0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; D3YWP0; protein.
DR Bgee; ENSMUSG00000080115; Expressed in pancreas and 29 other tissues.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0008168; F:methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0018022; P:peptidyl-lysine methylation; IMP:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
DR Pfam; PF10294; Methyltransf_16; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..232
FT /note="EEF1A lysine methyltransferase 3"
FT /id="PRO_0000439952"
FT BINDING 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96AZ1"
FT BINDING 83..85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96AZ1"
FT BINDING 104
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96AZ1"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96AZ1"
FT BINDING 150
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96AZ1"
SQ SEQUENCE 232 AA; 25675 MW; CA19DC02782DE8D3 CRC64;
MASSRTDPET EPESVFPREI RLFTDSYSES SRFCFCGHEL SITQNFGSRL GVAARVWDAA
LSLCDYFESQ NVDFRGKKVI ELGAGTGIVG ILAALQGGDV TITDLPVALE QIQDNVHANV
PPGGRARVCA LSWGIDQHVF PGNYDLVLGA DIVYLEPTFP LLLGTLRHLC GPHGTIYLAS
KMRAEHGAET FFRRLLPQHF HLELAQRDED VNVNIYRARH REVAPAGQHP FC
