EFM4_YEAST
ID EFM4_YEAST Reviewed; 257 AA.
AC P40516; D6VVM0; Q6B2R5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein-lysine N-methyltransferase EFM4 {ECO:0000255|HAMAP-Rule:MF_03188, ECO:0000305|PubMed:25231983};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03188, ECO:0000269|PubMed:20510667, ECO:0000269|PubMed:22522802, ECO:0000269|PubMed:24517342};
DE AltName: Full=Elongation factor methyltransferase 4 {ECO:0000255|HAMAP-Rule:MF_03188, ECO:0000303|PubMed:25231983};
DE AltName: Full=Secretion and early endocytosis protein 1 {ECO:0000303|PubMed:19160456};
GN Name=EFM4 {ECO:0000255|HAMAP-Rule:MF_03188, ECO:0000303|PubMed:25231983};
GN Synonyms=SEE1 {ECO:0000303|PubMed:19160456};
GN OrderedLocusNames=YIL064W {ECO:0000312|SGD:S000001326};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=19160456; DOI=10.1002/yea.1641;
RA Martin-Granados C., Riechers S.P., Stahl U., Lang C.;
RT "Absence of See1p, a widely conserved Saccharomyces cerevisiae protein,
RT confers both deficient heterologous protein production and endocytosis.";
RL Yeast 25:871-877(2008).
RN [7]
RP FUNCTION.
RX PubMed=20510667; DOI=10.1016/j.abb.2010.05.023;
RA Lipson R.S., Webb K.J., Clarke S.G.;
RT "Two novel methyltransferases acting upon eukaryotic elongation factor 1A
RT in Saccharomyces cerevisiae.";
RL Arch. Biochem. Biophys. 500:137-143(2010).
RN [8]
RP FUNCTION.
RX PubMed=22522802; DOI=10.1002/pmic.201100570;
RA Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.;
RT "Methylation of translation-associated proteins in Saccharomyces
RT cerevisiae: Identification of methylated lysines and their
RT methyltransferases.";
RL Proteomics 12:960-972(2012).
RN [9]
RP GENE NAME.
RX PubMed=25231983; DOI=10.1074/jbc.m114.605527;
RA Dzialo M.C., Travaglini K.J., Shen S., Roy K., Chanfreau G.F., Loo J.A.,
RA Clarke S.G.;
RT "Translational roles of elongation factor 2 protein lysine methylation.";
RL J. Biol. Chem. 289:30511-30524(2014).
RN [10]
RP FUNCTION.
RX PubMed=24517342; DOI=10.1021/pr401251k;
RA Hart-Smith G., Chia S.Z., Low J.K., McKay M.J., Molloy M.P., Wilkins M.R.;
RT "Stoichiometry of Saccharomyces cerevisiae lysine methylation: insights
RT into non-histone protein lysine methyltransferase activity.";
RL J. Proteome Res. 13:1744-1756(2014).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC methyltransferase that mono- and dimethylates elongation factor 1-alpha
CC (TEF1 and TEF2) at 'Lys-316'. May play a role in intracellular
CC transport. {ECO:0000255|HAMAP-Rule:MF_03188,
CC ECO:0000269|PubMed:20510667, ECO:0000269|PubMed:22522802,
CC ECO:0000269|PubMed:24517342}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03188,
CC ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Defects at both very early and later stages of
CC endocytic transport in cells. {ECO:0000269|PubMed:19160456}.
CC -!- MISCELLANEOUS: Present with 1620 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. EFM4 family. {ECO:0000255|HAMAP-Rule:MF_03188,
CC ECO:0000305}.
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DR EMBL; Z38060; CAA86159.1; -; Genomic_DNA.
DR EMBL; AY692665; AAT92684.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08486.1; -; Genomic_DNA.
DR PIR; S48415; S48415.
DR RefSeq; NP_012200.1; NM_001179414.1.
DR AlphaFoldDB; P40516; -.
DR SMR; P40516; -.
DR BioGRID; 34928; 105.
DR DIP; DIP-5648N; -.
DR STRING; 4932.YIL064W; -.
DR iPTMnet; P40516; -.
DR MaxQB; P40516; -.
DR PaxDb; P40516; -.
DR PRIDE; P40516; -.
DR EnsemblFungi; YIL064W_mRNA; YIL064W; YIL064W.
DR GeneID; 854746; -.
DR KEGG; sce:YIL064W; -.
DR SGD; S000001326; EFM4.
DR VEuPathDB; FungiDB:YIL064W; -.
DR eggNOG; KOG1271; Eukaryota.
DR GeneTree; ENSGT00390000013399; -.
DR HOGENOM; CLU_044783_1_0_1; -.
DR InParanoid; P40516; -.
DR OMA; LGTKQYW; -.
DR BioCyc; YEAST:G3O-31332-MON; -.
DR Reactome; R-SCE-8876725; Protein methylation.
DR PRO; PR:P40516; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40516; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:SGD.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; IBA:GO_Central.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03188; Methyltr_EFM4; 1.
DR InterPro; IPR026635; Efm4/METTL10.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Transport.
FT CHAIN 1..257
FT /note="Protein-lysine N-methyltransferase EFM4"
FT /id="PRO_0000202983"
FT CONFLICT 104
FT /note="N -> S (in Ref. 3; AAT92684)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 257 AA; 28690 MW; DB617B79C9A711FC CRC64;
MKRSEKKSMS SALKNGIMER TQPEKVVQMQ GTADLSTSKL GTKKYWDELY ALELENFRRN
PQDTGDCWFS DSDAEQKMID FLVDNIGAYR ISENASVVDL GTGNGHMLFE LHQTEFQGKL
VGIDYSEESV KLASNIAEAT GVDNFISFQQ ADIFSGDWKP GKYDIVLDKG TLDAISLSGM
KINGKLDVVD VYAGVVERIL KKDGIFLITS CNFTQDELVK IIETDNLKMW KTIKYPVFQF
GGVQGATICS VAFVKQN
