MT21A_PONAB
ID MT21A_PONAB Reviewed; 236 AA.
AC Q5RE14;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR857725; CAH89993.1; -; mRNA.
DR RefSeq; NP_001124945.1; NM_001131473.1.
DR RefSeq; XP_009236295.1; XM_009238020.1.
DR RefSeq; XP_009236296.1; XM_009238021.1.
DR RefSeq; XP_009236297.1; XM_009238022.1.
DR RefSeq; XP_009236298.1; XM_009238023.1.
DR RefSeq; XP_009236299.1; XM_009238024.1.
DR AlphaFoldDB; Q5RE14; -.
DR SMR; Q5RE14; -.
DR STRING; 9601.ENSPPYP00000014659; -.
DR Ensembl; ENSPPYT00000054598; ENSPPYP00000030457; ENSPPYG00000013116.
DR GeneID; 100171817; -.
DR KEGG; pon:100171817; -.
DR CTD; 151194; -.
DR eggNOG; KOG2793; Eukaryota.
DR GeneTree; ENSGT00940000157249; -.
DR HOGENOM; CLU_055721_4_2_1; -.
DR InParanoid; Q5RE14; -.
DR OrthoDB; 1588190at2759; -.
DR Proteomes; UP000001595; Chromosome 2B.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018022; P:peptidyl-lysine methylation; IEA:Ensembl.
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..236
FT /note="Protein N-lysine methyltransferase METTL21A"
FT /id="PRO_0000292035"
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 112
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"
FT BINDING 161
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8WXB1"
SQ SEQUENCE 236 AA; 26670 MW; D6B598AFB31BB01F CRC64;
MALVPYEETT EFGLQKFHKP LKTFSFANHT IQIRQDWRHL GVAAVVWDAA IVLSTYLEMG
AVELRGRSAV ELGAGTGLVG IVAALLALKS SMKPLLVHCL LFFSGAHVTI TDRKVALEFL
KSNVQANLPP HIQPKTVVKE LTWGQNLGSF SPGEFDLILG ADIIYLEETF TDLLQTLEHL
CSNHSVILLA CRIRYERDNN FLAMLERQFT VRKVHYDPEK DVHIYEAQKR NQKEDL
