EFMT3_BOVIN
ID EFMT3_BOVIN Reviewed; 226 AA.
AC A4FV98;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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;
DE AltName: Full=Protein-lysine methyltransferase METTL21B {ECO:0000250|UniProtKB:Q96AZ1};
GN Name=EEF1AKMT3 {ECO:0000250|UniProtKB:Q96AZ1};
GN Synonyms=FAM119B, METTL21B {ECO:0000250|UniProtKB:Q96AZ1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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. EEF1A1
CC methylation by EEF1AKMT3 is dynamic as well as inducible by stress
CC conditions, such as ER-stress, and plays a regulatory role on mRNA
CC translation. {ECO:0000250|UniProtKB:Q96AZ1}.
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}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC123899; AAI23900.1; -; mRNA.
DR RefSeq; NP_001096810.1; NM_001103340.1.
DR AlphaFoldDB; A4FV98; -.
DR SMR; A4FV98; -.
DR STRING; 9913.ENSBTAP00000022493; -.
DR PaxDb; A4FV98; -.
DR PRIDE; A4FV98; -.
DR Ensembl; ENSBTAT00000022493; ENSBTAP00000022493; ENSBTAG00000016910.
DR GeneID; 100125307; -.
DR KEGG; bta:100125307; -.
DR CTD; 25895; -.
DR VEuPathDB; HostDB:ENSBTAG00000016910; -.
DR VGNC; VGNC:50099; EEF1AKMT3.
DR eggNOG; KOG2793; Eukaryota.
DR GeneTree; ENSGT00940000161297; -.
DR HOGENOM; CLU_055721_4_0_1; -.
DR InParanoid; A4FV98; -.
DR OMA; HRDDKQN; -.
DR OrthoDB; 1494909at2759; -.
DR TreeFam; TF313206; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000016910; Expressed in semen and 99 other tissues.
DR ExpressionAtlas; A4FV98; baseline.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018022; P:peptidyl-lysine methylation; ISS: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 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..226
FT /note="EEF1A lysine methyltransferase 3"
FT /id="PRO_0000291849"
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"
SQ SEQUENCE 226 AA; 24972 MW; AB328D2D934F1992 CRC64;
MADSRPDPES EPDSVFPREV GLFADCYSEK SRFCFCGHVL NITENFGSRL GVAARVWDAA
LSLCNYFESQ NVDFRGKKVI ELGAGTGIVG ILAALQGGDV TITDLPLVLE QIQGNVQANV
PPGGRAQVRA LSWGIDQHVF PGDYDLVLGA DIVYLEPTFP LLLGTLRHLC GPHGTIYLAS
KMREEHGTES FFQHLLPQHF QLELAQRDED ENVNIYRARH RGPRPA
