MT21A_BOVIN
ID MT21A_BOVIN Reviewed; 218 AA.
AC A4FV42;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Protein N-lysine methyltransferase METTL21A;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q8WXB1};
DE AltName: Full=Methyltransferase-like protein 21A;
GN Name=METTL21A; Synonyms=FAM119A;
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=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein-lysine methyltransferase that selectively
CC trimethylates residues in heat shock protein 70 (HSP70) family members.
CC Contributes to the in vivo trimethylation of Lys residues in HSPA1 and
CC HSPA8. In vitro methylates 'Lys-561' in HSPA1, 'Lys-564' in HSPA2,
CC 'Lys-585' in HSPA5, 'Lys-563' in HSPA6 and 'Lys-561' in HSPA8.
CC {ECO:0000250|UniProtKB:Q8WXB1}.
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:Q8WXB1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC Evidence={ECO:0000250|UniProtKB:Q8WXB1};
CC -!- SUBUNIT: Interacts with heat shock 70 family members; at least some of
CC these proteins are methylation substrates.
CC {ECO:0000250|UniProtKB:Q8WXB1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WXB1}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL21
CC family. {ECO:0000305}.
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DR EMBL; BC123706; AAI23707.1; -; mRNA.
DR RefSeq; NP_001076987.1; NM_001083518.2.
DR RefSeq; XP_005202816.1; XM_005202759.3.
DR RefSeq; XP_005202817.1; XM_005202760.3.
DR RefSeq; XP_010800572.1; XM_010802270.2.
DR AlphaFoldDB; A4FV42; -.
DR SMR; A4FV42; -.
DR STRING; 9913.ENSBTAP00000007203; -.
DR PaxDb; A4FV42; -.
DR PRIDE; A4FV42; -.
DR GeneID; 615773; -.
DR KEGG; bta:615773; -.
DR CTD; 151194; -.
DR eggNOG; KOG2793; Eukaryota.
DR HOGENOM; CLU_055721_4_2_1; -.
DR InParanoid; A4FV42; -.
DR OrthoDB; 1588190at2759; -.
DR TreeFam; TF313206; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006479; P:protein 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; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..218
FT /note="Protein N-lysine methyltransferase METTL21A"
FT /id="PRO_0000292032"
FT BINDING 47
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8WXB1"
FT BINDING 73..75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8WXB1"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8WXB1"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8WXB1"
FT BINDING 143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8WXB1"
SQ SEQUENCE 218 AA; 24484 MW; 9D6ADA9C214CACA1 CRC64;
MALVPYTETA EMGLQRFHKP LATFSFANHT IQIRQDWKQL GVAAVVWDAA VVLATYLEMG
TVELRGCSAV ELGAGTGLVG IVAALLGAHV TITDRKVALE FLKSNVQANL PPHIQPKAVV
KELTWGQNLG RFSPGEFDLI LGADIIYLEE TFTDLLQTLE HLCSNHSVVL LACRIRYERD
YNFLAMLERQ FTVSKVHYDS EKDVHIYKAQ RRCLREDL
