CALM7_ARATH
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 03-AUG-2022, entry version 167.
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 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 [5]
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 [6]
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 [7]
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; 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 PDBsum; 4AQR; -.
DR PDBsum; 5A2H; -.
DR AlphaFoldDB; P59220; -.
DR SASBDB; P59220; -.
DR SMR; P59220; -.
DR BioGRID; 8812; 127.
DR IntAct; P59220; 122.
DR STRING; 3702.AT3G43810.1; -.
DR iPTMnet; P59220; -.
DR PaxDb; P59220; -.
DR PRIDE; P59220; -.
DR ProteomicsDB; 239187; -.
DR EnsemblPlants; AT3G43810.1; AT3G43810.1; AT3G43810.
DR GeneID; 823492; -.
DR Gramene; AT3G43810.1; AT3G43810.1; AT3G43810.
DR KEGG; ath:AT3G43810; -.
DR Araport; AT3G43810; -.
DR TAIR; locus:2101049; AT3G43810.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; P59220; -.
DR OMA; SCDRHPP; -.
DR PhylomeDB; P59220; -.
DR PRO; PR:P59220; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P59220; baseline and differential.
DR Genevisible; P59220; AT.
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: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 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 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
