ID   CALM7_ARATH             Reviewed;         149 AA.
AC   P59220;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   04-NOV-2026, entry version 186.
DE   RecName: Full=Calmodulin-7 {ECO:0000303|PubMed:11855649};
DE            Short=CaM-7 {ECO:0000303|PubMed:11855649};
GN   Name=CAM7 {ECO:0000303|PubMed:11855649};
GN   OrderedLocusNames=At3g43810 {ECO:0000312|Araport:AT3G43810};
GN   ORFNames=T28A8.100 {ECO:0000312|EMBL:CAB83153.1};
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 [MRNA], AND CHARACTERIZATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=11855649; DOI=10.1007/s004250100636;
RA   Zielinski R.E.;
RT   "Characterization of three new members of the Arabidopsis thaliana
RT   calmodulin gene family: conserved and highly diverged members of the gene
RT   family functionally complement a yeast calmodulin null.";
RL   Planta 214:446-455(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
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   [7]
RP   INTERACTION WITH MPK8, AND FUNCTION.
RX   PubMed=21419340; DOI=10.1016/j.molcel.2011.02.029;
RA   Takahashi F., Mizoguchi T., Yoshida R., Ichimura K., Shinozaki K.;
RT   "Calmodulin-dependent activation of MAP kinase for ROS homeostasis in
RT   Arabidopsis.";
RL   Mol. Cell 41:649-660(2011).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ABCG36, AND SUBCELLULAR
RP   LOCATION.
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: Calmodulin mediates the control of a large number of enzymes,
CC       ion channels and other proteins by Ca(2+) (PubMed:21419340). Among the
CC       enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number
CC       of protein kinases and phosphatases (PubMed:21419340). Activates MPK8
CC       in vitro (PubMed:21419340). Required during nonhost resistance (NHR) to
CC       the nonadapted fungal pathogens Phakopsora pachyrhizi and Blumeria
CC       graminis f.sp. hordei, probably via its Ca(2+)-dependent interaction
CC       with ABCG36 (PubMed:26315018). {ECO:0000269|PubMed:21419340,
CC       ECO:0000269|PubMed:26315018}.
CC   -!- SUBUNIT: Interacts with MPK8 (PubMed:21419340). Binds to ABCG36 in a
CC       Ca(2+)-dependent manner (PubMed:26315018).
CC       {ECO:0000269|PubMed:21419340, ECO:0000269|PubMed:26315018}.
CC   -!- INTERACTION:
CC       P59220; Q9ZVM9: At1g54610; NbExp=2; IntAct=EBI-1236031, EBI-1235713;
CC       P59220; O48788: At2g26730; NbExp=2; IntAct=EBI-1236031, EBI-1239029;
CC       P59220; Q9M8T0: At3g02880; NbExp=2; IntAct=EBI-1236031, EBI-1238677;
CC       P59220; Q9LD45: BI-1; NbExp=2; IntAct=EBI-1236031, EBI-1644586;
CC       P59220; Q9LDI3: CIPK24; NbExp=2; IntAct=EBI-1236031, EBI-537551;
CC       P59220; Q42479: CPK3; NbExp=2; IntAct=EBI-1236031, EBI-1235782;
CC       P59220; Q9SSF8: CPK30; NbExp=2; IntAct=EBI-1236031, EBI-1235738;
CC       P59220; Q9LTM4: CYP71B19; NbExp=2; IntAct=EBI-1236031, EBI-1239070;
CC       P59220; Q9SLP1: CYP78A9; NbExp=2; IntAct=EBI-1236031, EBI-1238437;
CC       P59220; P55737: HSP90-2; NbExp=2; IntAct=EBI-1236031, EBI-1235834;
CC       P59220; P83755: psbA; NbExp=2; IntAct=EBI-1236031, EBI-1236013;
CC       P59220; Q2V359: SAUR70; NbExp=2; IntAct=EBI-1236031, EBI-1235819;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26315018};
CC       Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC       {ECO:0000305}. Nucleus {ECO:0000269|PubMed:26315018}. Note=Co-localizes
CC       with ABCG36 at the cytoplasm/plasma membrane interface.
CC       {ECO:0000269|PubMed:26315018}.
CC   -!- DISRUPTION PHENOTYPE: Compromised nonhost resistance (NHR) to the
CC       nonadapted fungal pathogens Phakopsora pachyrhizi and Blumeria graminis
CC       f.sp. hordei. {ECO:0000269|PubMed:26315018}.
CC   -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC   -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR   EMBL; AF178073; AAD53313.1; -; mRNA.
DR   EMBL; AL162691; CAB83153.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77831.1; -; Genomic_DNA.
DR   EMBL; OZ408685; CAO7043147.1; -; Genomic_DNA.
DR   EMBL; AY088477; AAM66013.1; -; mRNA.
DR   PIR; T47417; T47417.
DR   RefSeq; NP_189967.1; NM_114249.4.
DR   PDB; 4AQR; X-ray; 1.95 A; A/B=1-149.
DR   PDB; 5A2H; X-ray; 2.27 A; A=1-149.
DR   AlphaFoldDB; P59220; -.
DR   SASBDB; P59220; -.
DR   SMR; P59220; -.
DR   BioGRID; 8812; 128.
DR   FunCoup; P59220; 3494.
DR   IntAct; P59220; 122.
DR   STRING; 3702.P59220; -.
DR   iPTMnet; P59220; -.
DR   PaxDb; 3702-P59220; -.
DR   ProteomicsDB; 239187; -.
DR   GeneID; 823492; -.
DR   KEGG; ath:AT3G43810; -.
DR   Araport; AT3G43810; -.
DR   TAIR; AT3G43810; CAM7.
DR   eggNOG; KOG0027; Eukaryota.
DR   HOGENOM; CLU_061288_2_0_1; -.
DR   InParanoid; P59220; -.
DR   OMA; ADGEXPF; -.
DR   PhylomeDB; P59220; -.
DR   SABIO-RK; P59220; -.
DR   EvolutionaryTrace; P59220; -.
DR   PRO; PR:P59220; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   Proteomes; UP001984100; Chromosome 3.
DR   ExpressionAtlas; P59220; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISM:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR   GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR   GO; GO:0005513; P:detection of calcium ion; ISS:TAIR.
DR   GO; GO:0010099; P:regulation of photomorphogenesis; IMP:TAIR.
DR   CDD; cd00051; EFh; 2.
DR   FunFam; 1.10.238.10:FF:000034; Calmodulin; 1.
DR   FunFam; 1.10.238.10:FF:000042; Calmodulin; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 3.
DR   InterPro; IPR050230; CALM/Myosin/TropC-like.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR23048:SF53; CALMODULIN; 1.
DR   PANTHER; PTHR23048; MYOSIN LIGHT CHAIN 1, 3; 1.
DR   Pfam; PF13499; EF-hand_7; 2.
DR   SMART; SM00054; EFh; 4.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell membrane; Membrane; Metal-binding; Nucleus;
KW   Reference proteome; Repeat.
FT   CHAIN           1..149
FT                   /note="Calmodulin-7"
FT                   /id="PRO_0000198283"
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          81..116
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          117..149
FT                   /note="EF-hand 4"
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         94
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         96
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         98
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         130
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         132
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         134
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         136
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   HELIX           7..20
FT                   /evidence="ECO:0007829|PDB:4AQR"
FT   STRAND          25..28
FT                   /evidence="ECO:0007829|PDB:5A2H"
FT   HELIX           30..39
FT                   /evidence="ECO:0007829|PDB:4AQR"
FT   HELIX           46..56
FT                   /evidence="ECO:0007829|PDB:4AQR"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:4AQR"
FT   HELIX           66..74
FT                   /evidence="ECO:0007829|PDB:4AQR"
FT   HELIX           82..93
FT                   /evidence="ECO:0007829|PDB:4AQR"
FT   HELIX           103..112
FT                   /evidence="ECO:0007829|PDB:4AQR"
FT   HELIX           119..129
FT                   /evidence="ECO:0007829|PDB:4AQR"
FT   STRAND          131..137
FT                   /evidence="ECO:0007829|PDB:4AQR"
FT   HELIX           139..146
FT                   /evidence="ECO:0007829|PDB:4AQR"
SQ   SEQUENCE   149 AA;  16848 MW;  EB2B188A90AD508D CRC64;
     MADQLTDDQI SEFKEAFSLF DKDGDGCITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
     NGTIDFPEFL NLMARKMKDT DSEEELKEAF RVFDKDQNGF ISAAELRHVM TNLGEKLTDE
     EVDEMIREAD VDGDGQINYE EFVKVMMAK
//