MT21C_MOUSE
ID MT21C_MOUSE Reviewed; 248 AA.
AC Q8BLU2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein-lysine methyltransferase METTL21C;
DE EC=2.1.1.-;
DE AltName: Full=Methyltransferase-like protein 21C;
GN Name=Mettl21c;
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=Aorta, and Vein;
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).
CC -!- FUNCTION: Protein-lysine methyltransferase. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with members of the heat shock protein 70 families;
CC these proteins may possibly be methylation substrates for the enzyme.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL21
CC family. {ECO:0000305}.
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DR EMBL; AK041301; BAC30895.1; -; mRNA.
DR CCDS; CCDS14927.1; -.
DR RefSeq; NP_001013821.1; NM_001013799.1.
DR RefSeq; XP_006496189.1; XM_006496126.3.
DR RefSeq; XP_006496190.1; XM_006496127.2.
DR RefSeq; XP_006496191.1; XM_006496128.2.
DR AlphaFoldDB; Q8BLU2; -.
DR SMR; Q8BLU2; -.
DR STRING; 10090.ENSMUSP00000061229; -.
DR PhosphoSitePlus; Q8BLU2; -.
DR PaxDb; Q8BLU2; -.
DR PRIDE; Q8BLU2; -.
DR ProteomicsDB; 287513; -.
DR Antibodypedia; 25326; 123 antibodies from 15 providers.
DR Ensembl; ENSMUST00000061421; ENSMUSP00000061229; ENSMUSG00000047343.
DR GeneID; 433294; -.
DR KEGG; mmu:433294; -.
DR UCSC; uc007avv.1; mouse.
DR CTD; 196541; -.
DR MGI; MGI:3611450; Mettl21c.
DR VEuPathDB; HostDB:ENSMUSG00000047343; -.
DR eggNOG; KOG2793; Eukaryota.
DR GeneTree; ENSGT00940000156596; -.
DR HOGENOM; CLU_055721_0_0_1; -.
DR InParanoid; Q8BLU2; -.
DR OMA; AYLCQPG; -.
DR OrthoDB; 1494909at2759; -.
DR PhylomeDB; Q8BLU2; -.
DR TreeFam; TF354267; -.
DR BioGRID-ORCS; 433294; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Mettl21c; mouse.
DR PRO; PR:Q8BLU2; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BLU2; protein.
DR Bgee; ENSMUSG00000047343; Expressed in quadriceps femoris and 29 other tissues.
DR ExpressionAtlas; Q8BLU2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:MGI.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IMP:MGI.
DR GO; GO:0008628; P:hormone-mediated apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0018022; P:peptidyl-lysine methylation; ISO:MGI.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; IBA:GO_Central.
DR GO; GO:0006479; P:protein methylation; IDA:MGI.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IMP:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
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 Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..248
FT /note="Protein-lysine methyltransferase METTL21C"
FT /id="PRO_0000319591"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 104..106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 248 AA; 27892 MW; 67BA264E04FA0986 CRC64;
MDQHLHIAQQ PLLSGTPQED GFAGPSVEFD RIESSLRSIQ KFVPTDYASY TQEHYQFAGK
KIIIQESIEN YGTVVWPGAT ALCQYLEDHT EELNLQDAKI LEIGAGAGLV SIVSSLLGAQ
VTATDLPDVL GNLQYNILKN TLECTAHLPE VRELVWGEDL EQSFPKSTCC YDYVLASDVV
YHHYFLDKLL ATMVYLSQPG TVVLWANKFR FSADYEFLGK FKQAFDTTLL AEYSESSVKL
FKGILKWE
