ID   EFNMT_BOVIN             Reviewed;         699 AA.
AC   A5PK19;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=eEF1A lysine and N-terminal methyltransferase {ECO:0000250|UniProtKB:Q8N6R0};
DE            Short=eEF1A-KNMT {ECO:0000250|UniProtKB:Q8N6R0};
DE   AltName: Full=Methyltransferase-like protein 13 {ECO:0000250|UniProtKB:Q8N6R0};
DE   Includes:
DE     RecName: Full=eEF1A lysine methyltransferase {ECO:0000250|UniProtKB:Q8N6R0};
DE              EC=2.1.1.- {ECO:0000250|UniProtKB:Q8N6R0};
DE   Includes:
DE     RecName: Full=eEF1A N-terminal methyltransferase {ECO:0000250|UniProtKB:Q8N6R0};
DE              EC=2.1.1.- {ECO:0000250|UniProtKB:Q8N6R0};
GN   Name=METTL13;
GN   Synonyms=EEF1AKNMT {ECO:0000250|UniProtKB:Q8N6R0},
GN   FEAT {ECO:0000250|UniProtKB:Q91YR5};
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=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Dual methyltransferase that catalyzes methylation of
CC       elongation factor 1-alpha (EEF1A1 and EEF1A2) at two different
CC       positions, and is therefore involved in the regulation of mRNA
CC       translation (By similarity). Via its C-terminus, methylates EEF1A1 and
CC       EEF1A2 at the N-terminal residue 'Gly-2' (By similarity). Via its N-
CC       terminus dimethylates EEF1A1 and EEF1A2 at residue 'Lys-55' (By
CC       similarity). Has no activity towards core histones H2A, H2B, H3 and H4
CC       (By similarity). Negatively regulates cell proliferation at G1/S
CC       transition via transcriptional suppression of cell cycle regulatory
CC       genes such as CDK4 and CDK6 (By similarity).
CC       {ECO:0000250|UniProtKB:Q8N6R0}.
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:Q8N6R0};
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:Q8N6R0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal glycyl-L-lysyl-L-glutamyl-[protein] + 3 S-adenosyl-
CC         L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-glycyl-L-lysyl-L-
CC         glutamyl-[protein] + 3 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:58440, Rhea:RHEA-COMP:15140, Rhea:RHEA-COMP:15143,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:142597, ChEBI:CHEBI:142600;
CC         Evidence={ECO:0000250|UniProtKB:Q8N6R0};
CC   -!- SUBUNIT: Forms a tripartite complex containing GAB1, METTL13 and SPRY2
CC       (By similarity). Within the complex interacts with GAB1 and SPRY2 (By
CC       similarity). {ECO:0000250|UniProtKB:Q8N6R0}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q91YR5}. Nucleus
CC       {ECO:0000250|UniProtKB:Q91YR5}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q91YR5}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC142321; AAI42322.1; -; mRNA.
DR   RefSeq; NP_001092555.1; NM_001099085.2.
DR   AlphaFoldDB; A5PK19; -.
DR   SMR; A5PK19; -.
DR   STRING; 9913.ENSBTAP00000023571; -.
DR   PaxDb; A5PK19; -.
DR   PRIDE; A5PK19; -.
DR   Ensembl; ENSBTAT00000023571; ENSBTAP00000023571; ENSBTAG00000017721.
DR   GeneID; 538472; -.
DR   KEGG; bta:538472; -.
DR   CTD; 51603; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017721; -.
DR   VGNC; VGNC:31403; METTL13.
DR   eggNOG; KOG2352; Eukaryota.
DR   GeneTree; ENSGT00510000047399; -.
DR   HOGENOM; CLU_010025_1_0_1; -.
DR   InParanoid; A5PK19; -.
DR   OMA; GEYCVEN; -.
DR   OrthoDB; 912165at2759; -.
DR   TreeFam; TF105906; -.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000017721; Expressed in semen and 107 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 2.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; SSF53335; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Methyltransferase; Mitochondrion;
KW   Multifunctional enzyme; Nucleus; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..699
FT                   /note="eEF1A lysine and N-terminal methyltransferase"
FT                   /id="PRO_0000310761"
FT   REGION          433..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N6R0"
FT   MOD_RES         267
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N6R0"
SQ   SEQUENCE   699 AA;  78751 MW;  C0BDCBEF38515F6A CRC64;
     MNLLPKSSKE FGSVDYWEKF FQQRGKKAFE WYGTYLELCG VLHKYIKPRE KVLVVGCGNS
     ELSEQLYDVG YQDIVNIDIS EVVIKQMKER NASRRPRMSF LKMDMTQMEF PDASFQVVLD
     KGTLDAVLTD EEEKTLQQVD RMLAEVGRVL QVGGRYLCIS LAQAHVLKKA VGHFSREGWM
     VRVHQVASSQ DQLLEAEPRF SLPVFAFIMT KFRPVTGSAL QIFELCAQEQ GKPVRLESAE
     QLAEAVRERQ QYAWLCSQLY RKAGLGSVSL DLCNGDTGEP RYTLHVVDSP TVKPSRDNHF
     AIFIIPQGRE TEWLFGMEEG RKQLAASAGF RRLITVALHR GQQYEGMDSI QAELSARVME
     LAPAGMPAQL QVPFLSVGGD IGVRIVQHQA CSPLSGDYVI EDVQGDDKRY FRRLIFLSNR
     NVVQSEARLL QDVSHRAQKK RKKDRKKHRP ADTPEDLPAA QGQSIDKSYL CCEHHKAMIA
     GLALLKNPEL LLETPLALLV VGLGGGSLPL FIHDHFPKSC IHAVEIDPSM LEVATQWFGF
     SQSDRMKVHI ADGLDFITRL AEEEARPHYD VIMFDVDSKD PTLGMSCPPP AFVAQLFLQK
     VKSILTPEGV FILNLVCRDL GLKDSVLAGL KAVFPLLYVR RIEGEVNEIL FCQLHSECKL
     ATPELLEMAR ALEQTLRKPG KGWDDTYVLS DMLNTVKIV