EFMT4_MOUSE
ID EFMT4_MOUSE Reviewed; 255 AA.
AC P0DPE0; Q14BY3; Q80Z59; Q80Z60; Q9D8Q9; Q9D928;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=EEF1A lysine methyltransferase 4 {ECO:0000250|UniProtKB:P0DPD7};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P0DPD7};
GN Name=Eef1akmt4 {ECO:0000250|UniProtKB:P0DPD7};
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=Pancreas;
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: Protein-lysine methyltransferase that efficiently catalyzes
CC three successive methylations on 'Lys-36' in eukaryotic translation
CC elongation factor 1 alpha (EEF1A1 or EEF1A2).
CC {ECO:0000250|UniProtKB:P0DPD7}.
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:P0DPD7};
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:P0DPD7};
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:P0DPD7};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Eef1akmt4-1;
CC IsoId=P0DPE0-1, Q80Z60-3;
CC Sequence=Displayed;
CC Name=Eef1akmt4-Ece2-1; Synonyms=ECE-2a-1;
CC IsoId=P0DPD9-1, Q80Z60-1;
CC Sequence=External;
CC Name=Eef1akmt4-Ece2-2; Synonyms=ECE-2a-2;
CC IsoId=P0DPD9-2, Q80Z60-2;
CC Sequence=External;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB25257.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK007407; BAB25019.1; -; mRNA.
DR EMBL; AK007791; BAB25257.1; ALT_FRAME; mRNA.
DR EMBL; AC087898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115541; AAI15542.1; -; mRNA.
DR CCDS; CCDS37290.1; -.
DR RefSeq; NP_079738.2; NM_025462.2. [P0DPE0-1]
DR RefSeq; NP_808809.1; NM_177940.1.
DR RefSeq; NP_808810.1; NM_177941.1.
DR AlphaFoldDB; P0DPE0; -.
DR SMR; P0DPE0; -.
DR PhosphoSitePlus; P0DPE0; -.
DR MaxQB; P0DPE0; -.
DR PRIDE; P0DPE0; -.
DR ProteomicsDB; 277766; -.
DR Ensembl; ENSMUST00000115522; ENSMUSP00000111184; ENSMUSG00000115219. [P0DPE0-1]
DR GeneID; 110599566; -.
DR GeneID; 110599584; -.
DR KEGG; mmu:110599566; -.
DR KEGG; mmu:110599584; -.
DR CTD; 110599564; -.
DR MGI; MGI:5903914; Eef1akmt4.
DR VEuPathDB; HostDB:ENSMUSG00000115219; -.
DR GeneTree; ENSGT00940000164140; -.
DR OMA; INMFHEE; -.
DR OrthoDB; 282463at2759; -.
DR PRO; PR:P0DPE0; -.
DR Proteomes; UP000000589; Chromosome 16.
DR Bgee; ENSMUSG00000115219; Expressed in humerus cartilage element and 204 other tissues.
DR ExpressionAtlas; P0DPE0; baseline and differential.
DR Genevisible; Q80Z60; MM.
DR GO; GO:0008168; F:methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Methyltransferase; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..255
FT /note="EEF1A lysine methyltransferase 4"
FT /id="PRO_0000443291"
FT MOTIF 129..134
FT /note="Required for methyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 26
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 30
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 41
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 88..89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 113..114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT MOD_RES 39
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT CONFLICT 160
FT /note="E -> V (in Ref. 1; BAB25257)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 28531 MW; 250B2EF4520D7E47 CRC64;
MASPRTPVSP PELPEKNFQY RQVQYWDQRY KDAADSGPYE WFGDFASFRA LLEPELCPED
RILVLGCGNS ALSYELFLGG FPNVTSVDYS PVVVAAMQVR YAHVPSLRWE TMDVRALDFP
SGSFDVVLEK GTLDAMLAGE PDPWNVSSEG VHTVDQVLSE VSRLLVPGGR FISMTSAGPH
FRIRHYAQSR YDWSLRHTTY SSGFHFHFYI MHKGRALSVS QLALGAQILS SPSPPASPCF
LQDSDNEDFL SAIQL
