CML24_ARATH
ID CML24_ARATH Reviewed; 161 AA.
AC P25070; O22592; Q1ECM5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Calcium-binding protein CML24;
DE AltName: Full=Calmodulin-like protein 24;
DE AltName: Full=Touch-induced calmodulin-related protein 2;
GN Name=CML24; Synonyms=TCH2; OrderedLocusNames=At5g37770; ORFNames=K22F20.1;
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;
RA Johnson K.A., Braam J.;
RT "Regulation and characterization of the calmodulin-related TCH2 gene of
RT Arabidopsis thaliana.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-70.
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 [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16113225; DOI=10.1104/pp.105.062612;
RA Delk N.A., Johnson K.A., Chowdhury N.I., Braam J.;
RT "CML24, regulated in expression by diverse stimuli, encodes a potential
RT Ca2+ sensor that functions in responses to abscisic acid, daylength, and
RT ion stress.";
RL Plant Physiol. 139:240-253(2005).
RN [9]
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 [10]
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 [11]
RP 3D-STRUCTURE MODELING OF 7-158.
RX PubMed=9037719;
RX DOI=10.1002/(sici)1097-0134(199701)27:1<144::aid-prot14>3.0.co;2-n;
RA Khan A.R., Johnson K.A., Braam J., James M.N.G.;
RT "Comparative modeling of the three-dimensional structure of the calmodulin-
RT related TCH2 protein from Arabidopsis.";
RL Proteins 27:144-153(1997).
CC -!- FUNCTION: Calcium-binding protein that may positively regulate abscisic
CC acid (ABA) inhibition of germination and seedling development. May be
CC required for photoperiod-induced flowering and function in ion
CC homeostasis. {ECO:0000269|PubMed:16113225}.
CC -!- TISSUE SPECIFICITY: Expressed in seed coat, seedling radical,
CC cotyledons, hypocotyl, shoot apex and elongating root. Expressed in the
CC vasculature of cotyledons, leaves and roots. Highly expressed in guard
CC cells, trichomes and hydathodes. Expressed in inflorescence stem branch
CC points, silique abscission zone, young and mature styles and stigmatic
CC papillae, mature anthers and developing seed.
CC {ECO:0000269|PubMed:16113225}.
CC -!- INDUCTION: By rain-, wind-, and touch (thigmomorphogenesis), dark, heat
CC and cold treatments, hydrogen peroxide, ABA and auxin.
CC {ECO:0000269|PubMed:15720654, ECO:0000269|PubMed:16113225}.
CC -!- CAUTION: Although assigned as a calmodulin family member by Ref.9, it
CC only contains EF-hand domains. {ECO:0000305}.
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DR EMBL; AF026473; AAB82713.1; -; Genomic_DNA.
DR EMBL; AB016873; BAB10353.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94229.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71016.1; -; Genomic_DNA.
DR EMBL; BT025709; ABF82612.1; -; mRNA.
DR EMBL; AK227202; BAE99241.1; -; mRNA.
DR EMBL; AY086500; AAM63501.1; -; mRNA.
DR PIR; C34669; C34669.
DR RefSeq; NP_001318691.1; NM_001344218.1.
DR RefSeq; NP_198593.1; NM_123136.3.
DR AlphaFoldDB; P25070; -.
DR SMR; P25070; -.
DR BioGRID; 19006; 1.
DR STRING; 3702.AT5G37770.1; -.
DR iPTMnet; P25070; -.
DR PaxDb; P25070; -.
DR PRIDE; P25070; -.
DR ProteomicsDB; 240998; -.
DR EnsemblPlants; AT5G37770.1; AT5G37770.1; AT5G37770.
DR EnsemblPlants; AT5G37770.2; AT5G37770.2; AT5G37770.
DR GeneID; 833755; -.
DR Gramene; AT5G37770.1; AT5G37770.1; AT5G37770.
DR Gramene; AT5G37770.2; AT5G37770.2; AT5G37770.
DR KEGG; ath:AT5G37770; -.
DR Araport; AT5G37770; -.
DR TAIR; locus:2156040; AT5G37770.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_061288_20_7_1; -.
DR InParanoid; P25070; -.
DR OMA; KKMMSNG; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; P25070; -.
DR PRO; PR:P25070; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P25070; baseline and differential.
DR Genevisible; P25070; AT.
DR GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR GO; GO:0048574; P:long-day photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0009909; P:regulation of flower development; IGI:TAIR.
DR GO; GO:0080164; P:regulation of nitric oxide metabolic process; IGI:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009646; P:response to absence of light; IEP:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0051592; P:response to calcium ion; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:TAIR.
DR GO; GO:0010038; P:response to metal ion; IMP:TAIR.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 2: Evidence at transcript level;
KW Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..161
FT /note="Calcium-binding protein CML24"
FT /id="PRO_0000073656"
FT DOMAIN 13..48
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 49..84
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 90..125
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 126..161
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 30
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 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 109
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 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 145
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 CONFLICT 54
FT /note="T -> Y (in Ref. 7; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 17546 MW; A7324A5C0E0CBDB9 CRC64;
MSSKNGVVRS CLGSMDDIKK VFQRFDKNGD GKISVDELKE VIRALSPTAS PEETVTMMKQ
FDLDGNGFID LDEFVALFQI GIGGGGNNRN DVSDLKEAFE LYDLDGNGRI SAKELHSVMK
NLGEKCSVQD CKKMISKVDI DGDGCVNFDE FKKMMSNGGG A
