ID CML12_ARATH Reviewed; 324 AA.
AC P25071; Q38972; Q39064; Q8H1A0;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 3.
DT 24-JAN-2024, entry version 174.
DE RecName: Full=Calmodulin-like protein 12 {ECO:0000303|Ref.7};
DE AltName: Full=Touch-induced calmodulin-related protein 3 {ECO:0000303|PubMed:2302732};
GN Name=CML12 {ECO:0000303|Ref.7};
GN Synonyms=CAL4, TCH3 {ECO:0000303|PubMed:2302732};
GN OrderedLocusNames=At2g41100 {ECO:0000312|Araport:AT2G41100};
GN ORFNames=T3K9.13 {ECO:0000312|EMBL:AAD12001.1};
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=2302732; DOI=10.1016/0092-8674(90)90587-5;
RA Braam J., Davis R.W.;
RT "Rain-, wind-, and touch-induced expression of calmodulin and calmodulin-
RT related genes in Arabidopsis.";
RL Cell 60:357-364(1990).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=7827491; DOI=10.1105/tpc.6.11.1553;
RA Sistrunk M.L., Antosiewicz D.M., Purugganan M.M., Braam J.;
RT "Arabidopsis TCH3 encodes a novel Ca2+ binding protein and shows
RT environmentally induced and tissue-specific regulation.";
RL Plant Cell 6:1553-1565(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8564305;
RA Ito T., Hirano M., Akama K., Shimura Y., Okada K.;
RT "Touch-inducible genes for calmodulin and a calmodulin-related protein are
RT located in tandem on a chromosome of Arabidopsis thaliana.";
RL Plant Cell Physiol. 36:1369-1373(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX DOI=10.1046/j.1469-8137.2003.00845.x;
RA McCormack E., Braam J.;
RT "Calmodulins and related potential calcium sensors of Arabidopsis.";
RL New Phytol. 159:585-598(2003).
RN [8]
RP INTERACTION WITH PID, AND INDUCTION BY AUXIN.
RX PubMed=12857841; DOI=10.1104/pp.103.019943;
RA Benjamins R., Ampudia C.S., Hooykaas P.J., Offringa R.;
RT "PINOID-mediated signaling involves calcium-binding proteins.";
RL Plant Physiol. 132:1623-1630(2003).
RN [9]
RP INDUCTION.
RX PubMed=15720654; DOI=10.1111/j.1469-8137.2004.01238.x;
RA Lee D., Polisensky D.H., Braam J.;
RT "Genome-wide identification of touch- and darkness-regulated Arabidopsis
RT genes: a focus on calmodulin-like and XTH genes.";
RL New Phytol. 165:429-444(2005).
RN [10]
RP INTERACTION WITH ABCG36.
RC STRAIN=cv. Columbia;
RX PubMed=26315018; DOI=10.1111/nph.13582;
RA Campe R., Langenbach C., Leissing F., Popescu G.V., Popescu S.C.,
RA Goellner K., Beckers G.J., Conrath U.;
RT "ABC transporter PEN3/PDR8/ABCG36 interacts with calmodulin that, like
RT PEN3, is required for Arabidopsis nonhost resistance.";
RL New Phytol. 209:294-306(2016).
CC -!- FUNCTION: Potential calcium sensor that binds calcium in vitro.
CC -!- SUBUNIT: Interacts with PID (PubMed:12857841). Binds to ABCG36
CC (PubMed:26315018). {ECO:0000269|PubMed:12857841,
CC ECO:0000269|PubMed:26315018}.
CC -!- INTERACTION:
CC P25071; O64682: PID; NbExp=4; IntAct=EBI-1238781, EBI-1393382;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P25071-1; Sequence=Displayed;
CC -!- INDUCTION: By auxin, rain-, wind-, and touch (thigmomorphogenesis) and
CC during darkness conditions. {ECO:0000269|PubMed:12857841,
CC ECO:0000269|PubMed:15720654}.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; L34546; AAC37419.1; -; Genomic_DNA.
DR EMBL; D45848; BAA08282.1; -; Genomic_DNA.
DR EMBL; AC004261; AAD12001.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09928.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09931.1; -; Genomic_DNA.
DR EMBL; AF424577; AAL11571.1; -; mRNA.
DR EMBL; AY120719; AAM53277.1; -; mRNA.
DR EMBL; BT000036; AAN15355.1; -; mRNA.
DR PIR; B34669; B34669.
DR PIR; T02109; T02109.
DR RefSeq; NP_001189723.1; NM_001202794.1. [P25071-1]
DR RefSeq; NP_181643.1; NM_129675.5. [P25071-1]
DR AlphaFoldDB; P25071; -.
DR SMR; P25071; -.
DR BioGRID; 4046; 7.
DR IntAct; P25071; 89.
DR STRING; 3702.P25071; -.
DR iPTMnet; P25071; -.
DR PaxDb; 3702-AT2G41100-4; -.
DR ProteomicsDB; 240987; -. [P25071-1]
DR DNASU; 818709; -.
DR EnsemblPlants; AT2G41100.1; AT2G41100.1; AT2G41100. [P25071-1]
DR EnsemblPlants; AT2G41100.4; AT2G41100.4; AT2G41100. [P25071-1]
DR GeneID; 818709; -.
DR Gramene; AT2G41100.1; AT2G41100.1; AT2G41100. [P25071-1]
DR Gramene; AT2G41100.4; AT2G41100.4; AT2G41100. [P25071-1]
DR KEGG; ath:AT2G41100; -.
DR Araport; AT2G41100; -.
DR TAIR; AT2G41100; TCH3.
DR eggNOG; KOG0027; Eukaryota.
DR InParanoid; P25071; -.
DR OrthoDB; 213738at2759; -.
DR PhylomeDB; P25071; -.
DR PRO; PR:P25071; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P25071; baseline and differential.
DR Genevisible; P25071; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0009646; P:response to absence of light; IEP:TAIR.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:TAIR.
DR GO; GO:0009652; P:thigmotropism; IEP:TAIR.
DR CDD; cd00051; EFh; 3.
DR Gene3D; 1.10.238.10; EF-hand; 3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23050; CALCIUM BINDING PROTEIN; 1.
DR PANTHER; PTHR23050:SF483; CALMODULIN-LIKE PROTEIN 12; 1.
DR Pfam; PF13499; EF-hand_7; 3.
DR SMART; SM00054; EFh; 6.
DR SUPFAM; SSF47473; EF-hand; 2.
DR PROSITE; PS00018; EF_HAND_1; 6.
DR PROSITE; PS50222; EF_HAND_2; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..324
FT /note="Calmodulin-like protein 12"
FT /id="PRO_0000073657"
FT DOMAIN 8..43
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 44..79
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 97..132
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 133..168
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 187..222
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 223..258
FT /note="EF-hand 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 112
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CONFLICT 223..226
FT /note="QTKA -> KQKL (in Ref. 1; AAC37419)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 36807 MW; 94277BFBC2D2C5CE CRC64;
MADKLTDDQI TEYRESFRLF DKNGDGSITK KELGTMMRSI GEKPTKADLQ DLMNEADLDG
DGTIDFPEFL CVMAKNQGHD QAPRHTKKTM ADKLTDDQIT EYRESFRLFD KNGDGSITKK
ELRTVMFSLG KNRTKADLQD MMNEVDLDGD GTIDFPEFLY LMAKNQGHDQ APRHTKKTMV
DYQLTDDQIL EFREAFRVFD KNGDGYITVN ELRTTMRSLG ETQTKAELQD MINEADADGD
GTISFSEFVC VMTGKMIDTQ SKKETYRVVN QGQGQVQRHT RNDRAGGTNW ERDIAVGVAS
NIIASPISDF MKDRFKDLFE ALLS
//
