CMKMT_MOUSE
ID CMKMT_MOUSE Reviewed; 323 AA.
AC Q3U2J5; Q9D9C5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Calmodulin-lysine N-methyltransferase;
DE Short=CLNMT;
DE Short=CaM KMT;
DE EC=2.1.1.60;
GN Name=Camkmt; Synonyms=Clnmt;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Testis;
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 TISSUE SPECIFICITY.
RX PubMed=23285036; DOI=10.1371/journal.pone.0052425;
RA Magen S., Magnani R., Haziza S., Hershkovitz E., Houtz R., Cambi F.,
RA Parvari R.;
RT "Human calmodulin methyltransferase: expression, activity on calmodulin,
RT and Hsp90 dependence.";
RL PLoS ONE 7:E52425-E52425(2012).
CC -!- FUNCTION: Catalyzes the trimethylation of 'Lys-116' in calmodulin.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[calmodulin]-L-lysine + S-adenosyl-L-methionine =
CC [calmodulin]-N(6)-methyl-L-lysine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:21556, Rhea:RHEA-COMP:11360, Rhea:RHEA-COMP:11361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.60;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00942};
CC -!- SUBUNIT: Monomer. Interacts with HSP90, probably as a client (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000250|UniProtKB:Q7Z624}. Nucleus {ECO:0000250|UniProtKB:Q7Z624}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus
CC {ECO:0000250|UniProtKB:Q7Z624}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3U2J5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U2J5-2; Sequence=VSP_027786, VSP_027787;
CC -!- TISSUE SPECIFICITY: Detected in most of the tissues examined, with the
CC highest expression in the brain and muscle (at protein level).
CC {ECO:0000269|PubMed:23285036}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. CLNMT methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00942}.
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DR EMBL; AK007130; BAB24867.1; -; mRNA.
DR EMBL; AK155246; BAE33145.1; -; mRNA.
DR CCDS; CCDS37712.1; -. [Q3U2J5-1]
DR RefSeq; NP_082852.1; NM_028576.2. [Q3U2J5-1]
DR AlphaFoldDB; Q3U2J5; -.
DR SMR; Q3U2J5; -.
DR BioGRID; 216118; 1.
DR STRING; 10090.ENSMUSP00000092811; -.
DR iPTMnet; Q3U2J5; -.
DR PhosphoSitePlus; Q3U2J5; -.
DR MaxQB; Q3U2J5; -.
DR PaxDb; Q3U2J5; -.
DR PRIDE; Q3U2J5; -.
DR ProteomicsDB; 285500; -. [Q3U2J5-1]
DR ProteomicsDB; 285501; -. [Q3U2J5-2]
DR Antibodypedia; 53862; 21 antibodies from 13 providers.
DR Ensembl; ENSMUST00000095188; ENSMUSP00000092811; ENSMUSG00000071037. [Q3U2J5-1]
DR GeneID; 73582; -.
DR KEGG; mmu:73582; -.
DR UCSC; uc008dtt.1; mouse. [Q3U2J5-1]
DR CTD; 79823; -.
DR MGI; MGI:1920832; Camkmt.
DR VEuPathDB; HostDB:ENSMUSG00000071037; -.
DR eggNOG; KOG3201; Eukaryota.
DR GeneTree; ENSGT00390000002168; -.
DR HOGENOM; CLU_057006_0_0_1; -.
DR InParanoid; Q3U2J5; -.
DR OMA; FQDECVA; -.
DR PhylomeDB; Q3U2J5; -.
DR TreeFam; TF316589; -.
DR BRENDA; 2.1.1.60; 3474.
DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-MMU-8876725; Protein methylation.
DR BioGRID-ORCS; 73582; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Camkmt; mouse.
DR PRO; PR:Q3U2J5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3U2J5; protein.
DR Bgee; ENSMUSG00000071037; Expressed in animal zygote and 169 other tissues.
DR ExpressionAtlas; Q3U2J5; baseline and differential.
DR Genevisible; Q3U2J5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0018025; F:calmodulin-lysine N-methyltransferase activity; IMP:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0018022; P:peptidyl-lysine methylation; IMP:MGI.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025800; CaM-Lys-N-MeTrfase.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13539; PTHR13539; 1.
DR Pfam; PF10294; Methyltransf_16; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51610; SAM_CLNMT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Golgi apparatus; Methyltransferase;
KW Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..323
FT /note="Calmodulin-lysine N-methyltransferase"
FT /id="PRO_0000300116"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 127..145
FT /note="IWPSEEVLAHYCLKHSHIF -> DPPPAPHTGGVDGDVFLTT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027786"
FT VAR_SEQ 146..323
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027787"
SQ SEQUENCE 323 AA; 35887 MW; 26EF97905B6790CD CRC64;
MESQVAAAGA AETEAEAGKR PAMGSASQGS LVSAPKGAVR WQLLRQVLKQ KQLDDHLRHV
SVRRFESFNL FSVTEATKKG TEKEAGVWVQ YTSIFYPKYS ISVRHNSGSL NVEDVLTSFD
NTGNVCIWPS EEVLAHYCLK HSHIFRDLAV CELGGGMTCL AGLMVAISAD VKEVLLTDGN
EKAIRNVDSI IACNKKTGVF KTPKISSRVL RWDNETDVSQ LEGHFDIVMC ADCLFLDQYR
ASLVDAIKRL LQPTGKAVVF APRRGNTFNQ FCNLAEKAGF SLQRHENYDE PISNFHSKLK
KEGSDIYEEN LHYPLLLILT KTG
