CMKMT_ARATH
ID CMKMT_ARATH Reviewed; 304 AA.
AC F4JNX3; O65636;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Calmodulin-lysine N-methyltransferase {ECO:0000303|PubMed:24285794};
DE Short=CLNMT {ECO:0000303|PubMed:24285794};
DE Short=CaM KMT {ECO:0000303|PubMed:24285794};
DE EC=2.1.1.60 {ECO:0000250|UniProtKB:Q6GQ33};
GN Name=CaMKMT {ECO:0000303|PubMed:24285794};
GN OrderedLocusNames=At4g35987 {ECO:0000312|Araport:AT4G35987};
GN ORFNames=T19K4.120 {ECO:0000312|EMBL:CAA18493.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION BY AUXIN; SALT; KINETIN AND ABSCISIC ACID.
RC STRAIN=cv. Columbia;
RX PubMed=24285794; DOI=10.1105/tpc.113.119115;
RA Banerjee J., Magnani R., Nair M., Dirk L.M., DeBolt S., Maiti I.B.,
RA Houtz R.L.;
RT "Calmodulin-mediated signal transduction pathways in Arabidopsis are fine-
RT tuned by methylation.";
RL Plant Cell 25:4493-4511(2013).
RN [5]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY BIOTIC STRESS;
RP SALT STRESS AND MANNITOL.
RC STRAIN=cv. Columbia;
RX PubMed=24260266; DOI=10.1371/journal.pone.0079622;
RA Banerjee J., Sahoo D.K., Dey N., Houtz R.L., Maiti I.B.;
RT "An intergenic region shared by At4g35985 and At4g35987 in Arabidopsis
RT thaliana is a tissue specific and stress inducible bidirectional promoter
RT analyzed in transgenic arabidopsis and tobacco plants.";
RL PLoS ONE 8:E79622-E79622(2013).
CC -!- FUNCTION: Catalyzes the trimethylation of calmodulin (PubMed:24285794).
CC Regulates roots development probably by modulating auxin signaling
CC responses. May be involved in gravitropism. Involved in abscisic acid
CC (ABA)-mediated and abiotic stress responses, including salt (NaCl),
CC cold, drought and heat stresses (PubMed:24285794).
CC {ECO:0000269|PubMed:24285794}.
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:0000250|UniProtKB:Q6GQ33};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:B0K012}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7Z624}. Nucleus
CC {ECO:0000250|UniProtKB:Q7Z624}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4JNX3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4JNX3-2; Sequence=VSP_059985;
CC -!- TISSUE SPECIFICITY: Expressed in discreet spatial and tissue-specific
CC patterns including root tips, leaves-tips, floral buds, stamens,
CC hydathodes, stigma, anther, siliques, apical meristems and germinating
CC seeds (PubMed:24285794, PubMed:24260266). Also observed at high levels
CC in the root stele region (PubMed:24260266).
CC {ECO:0000269|PubMed:24260266, ECO:0000269|PubMed:24285794}.
CC -!- DEVELOPMENTAL STAGE: After seed stratification, first observed in the
CC micropylar end, later present in the endosperm region and in the testa,
CC and finally accumulates in the endosperm and emerging radicle. In
CC seedlings, first detected in the root and cotyledon tips, expression
CC level reaches a maximal at the cotyledonary leaf stage and is later
CC confined in the shoot apical meristem. In roots, expressed at the
CC primary root tip, at the basal side of root curvature, and at the
CC lateral root tip (PubMed:24285794). Also observed in very young
CC primordia, floral buds, and stamens (PubMed:24285794, PubMed:24260266).
CC In stamens, mostly present in the anther containing immature pollen
CC and, at low levels, in the filament. In siliques, highly expressed in
CC the abscission zone and, to a lower extent, in developing seeds
CC (PubMed:24285794). {ECO:0000269|PubMed:24260266,
CC ECO:0000269|PubMed:24285794}.
CC -!- INDUCTION: Induced by salt (NaCl) stress (PubMed:24285794,
CC PubMed:24260266). Accumulates in response to osmotic stress (e.g.
CC mannitol) and upon biotic stress, e.g. inoculation with the oomycete
CC P.tabacina (PubMed:24260266). Triggered by auxins indole-3-acetic acid
CC (IAA) and 2,4-dichlorophenoxyacetic acid (2,4-D). Repressed by kinetin
CC or abscisic acid (ABA) treatments (PubMed:24285794).
CC {ECO:0000269|PubMed:24260266, ECO:0000269|PubMed:24285794}.
CC -!- DISRUPTION PHENOTYPE: Suppressed calmodulin (CaM) methylation,
CC especially in roots. Longer roots with ectopic root hair cells in
CC atrichoblast cell files and the presence of nonhair cells in
CC trichoblast cell files. Increased number of epidermal cells in the root
CC elongation zone. Reduced root growth inhibition mediated by auxins
CC indole-3-acetic acid (IAA) and 2,4-dichlorophenoxyacetic acid (2,4-D).
CC Reduced sensitivity to abscisic acid (ABA)-mediated stress leading to
CC green cotyledons and normal germination in the presence of ABA.
CC Increased tolerance to abiotic stress such as salt (NaCl), cold,
CC drought and heat stresses. {ECO:0000269|PubMed:24285794}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. CLNMT methyltransferase family. {ECO:0000305}.
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DR EMBL; AL022373; CAA18493.1; -; Genomic_DNA.
DR EMBL; AL161588; CAB81508.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86599.1; -; Genomic_DNA.
DR EMBL; BT029304; ABK32118.1; -; mRNA.
DR PIR; T05491; T05491.
DR RefSeq; NP_680769.4; NM_148403.5. [F4JNX3-1]
DR AlphaFoldDB; F4JNX3; -.
DR SMR; F4JNX3; -.
DR STRING; 3702.AT4G35987.1; -.
DR PaxDb; F4JNX3; -.
DR PRIDE; F4JNX3; -.
DR ProteomicsDB; 241076; -. [F4JNX3-1]
DR EnsemblPlants; AT4G35987.1; AT4G35987.1; AT4G35987. [F4JNX3-1]
DR GeneID; 829754; -.
DR Gramene; AT4G35987.1; AT4G35987.1; AT4G35987. [F4JNX3-1]
DR KEGG; ath:AT4G35987; -.
DR Araport; AT4G35987; -.
DR TAIR; locus:504955358; AT4G35987.
DR eggNOG; KOG3201; Eukaryota.
DR HOGENOM; CLU_057006_2_0_1; -.
DR InParanoid; F4JNX3; -.
DR OMA; FQDECVA; -.
DR OrthoDB; 1161502at2759; -.
DR PhylomeDB; F4JNX3; -.
DR PRO; PR:F4JNX3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JNX3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0018025; F:calmodulin-lysine N-methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009630; P:gravitropism; IMP:UniProtKB.
DR GO; GO:0032259; P:methylation; IMP:UniProtKB.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0010928; P:regulation of auxin mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:1901000; P:regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:2000070; P:regulation of response to water deprivation; IMP:UniProtKB.
DR GO; GO:2000280; P:regulation of root development; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:0002239; P:response to oomycetes; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0080147; P:root hair cell development; IMP:UniProtKB.
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.
PE 2: Evidence at transcript level;
KW Abscisic acid signaling pathway; Alternative splicing;
KW Auxin signaling pathway; Cytoplasm; Developmental protein;
KW Methyltransferase; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..304
FT /note="Calmodulin-lysine N-methyltransferase"
FT /id="PRO_0000445938"
FT VAR_SEQ 1..175
FT /note="Missing (in isoform 2)"
FT /id="VSP_059985"
SQ SEQUENCE 304 AA; 34491 MW; B5A77C6FD0AA0484 CRC64;
MDPTSSSSSA LRWKILRQAL LRRSDSQSQT ETKRISRKAT QGFNLIPCQV VDSSPQSDKS
REASVCYTLP ITGSPKLYLT QRVDNCSDLN DFEISNRYNI DNTGLVCQWP SEEVLAYFCK
SQPERFRGKR VIELGSGYGL AGLVIAAATE ASEVVISDGN PQVVNYIKRN IETNSMAFGG
TSVKAMELHW NQHQLSELTN TFDIIVASDC TFFKEFHKDL ARTIKMLLKA KKASEALFFS
PKRGDSLEKF MKEIKDIGLH YILTENYDAQ VWKRHETLVK GDEAWPNYDK NHCYPLLIQI
TNQI
