MT21A_MOUSE
ID MT21A_MOUSE Reviewed; 218 AA.
AC Q9CQL0; Q8R2Y7;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 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=Cecum, and Tongue;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 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; AK009673; BAB26430.1; -; mRNA.
DR EMBL; AK009675; BAB26431.1; -; mRNA.
DR EMBL; AK009678; BAB26434.1; -; mRNA.
DR EMBL; AK009679; BAB26435.1; -; mRNA.
DR EMBL; AK009680; BAB26436.1; -; mRNA.
DR EMBL; AK009682; BAB26437.1; -; mRNA.
DR EMBL; AK011433; BAB27618.1; -; mRNA.
DR EMBL; AK033578; BAC28371.1; -; mRNA.
DR EMBL; BC026952; AAH26952.1; -; mRNA.
DR CCDS; CCDS15006.1; -.
DR RefSeq; NP_080240.1; NM_025964.3.
DR RefSeq; XP_006496266.1; XM_006496203.3.
DR RefSeq; XP_006496267.1; XM_006496204.3.
DR AlphaFoldDB; Q9CQL0; -.
DR SMR; Q9CQL0; -.
DR STRING; 10090.ENSMUSP00000050424; -.
DR PhosphoSitePlus; Q9CQL0; -.
DR EPD; Q9CQL0; -.
DR MaxQB; Q9CQL0; -.
DR PaxDb; Q9CQL0; -.
DR PeptideAtlas; Q9CQL0; -.
DR PRIDE; Q9CQL0; -.
DR ProteomicsDB; 287512; -.
DR Antibodypedia; 34188; 181 antibodies from 21 providers.
DR DNASU; 67099; -.
DR Ensembl; ENSMUST00000053469; ENSMUSP00000050424; ENSMUSG00000025956.
DR Ensembl; ENSMUST00000114079; ENSMUSP00000109713; ENSMUSG00000025956.
DR GeneID; 67099; -.
DR KEGG; mmu:67099; -.
DR UCSC; uc007bgu.1; mouse.
DR CTD; 151194; -.
DR MGI; MGI:1914349; Mettl21a.
DR VEuPathDB; HostDB:ENSMUSG00000025956; -.
DR eggNOG; KOG2793; Eukaryota.
DR GeneTree; ENSGT00940000157249; -.
DR HOGENOM; CLU_055721_4_2_1; -.
DR InParanoid; Q9CQL0; -.
DR OMA; AQDWKKL; -.
DR OrthoDB; 1588190at2759; -.
DR PhylomeDB; Q9CQL0; -.
DR TreeFam; TF313206; -.
DR Reactome; R-MMU-8876725; Protein methylation.
DR BioGRID-ORCS; 67099; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Mettl21a; mouse.
DR PRO; PR:Q9CQL0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CQL0; protein.
DR Bgee; ENSMUSG00000025956; Expressed in motor neuron and 248 other tissues.
DR Genevisible; Q9CQL0; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0008276; F:protein methyltransferase activity; ISO:MGI.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018022; P:peptidyl-lysine methylation; ISO:MGI.
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_0000292034"
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"
FT CONFLICT 86
FT /note="L -> P (in Ref. 2; AAH26952)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 24286 MW; 7CAFEA691B90195A CRC64;
MALVPYEESA AIGLQKFHKP LATFSFANHT IQIRQDWRQL GVAAVVWDAA VVLSMYLEMG
AVELRGCSAV ELGAGTGLVG IVAALLGAQV TITDRKVALE FLKSNVEANL PPHIQPKAVV
KELTWGQNLE SFSPGEFDLI LGADVIYLED TFTDLLQTLG HLCSNNSVIL LACRIRYERD
SNFLTMLERQ FTVSKVHYDP EKDVHIYKAQ KRNQREDL
