CML9_ARATH
ID CML9_ARATH Reviewed; 151 AA.
AC Q9S744;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Calmodulin-like protein 9 {ECO:0000303|Ref.5};
DE Short=AtCaM-9 {ECO:0000303|PubMed:11855649};
GN Name=CML9 {ECO:0000303|Ref.5}; Synonyms=CAM9 {ECO:0000303|PubMed:11855649};
GN OrderedLocusNames=At3g51920 {ECO:0000312|Araport:AT3G51920};
GN ORFNames=F4F15.30 {ECO:0000312|EMBL:CAB41312.1};
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], FUNCTION, AND TISSUE SPECIFICITY.
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].
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 [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 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 [7]
RP INTERACTION WITH IQD1.
RC STRAIN=cv. Columbia;
RX PubMed=23204523; DOI=10.1074/jbc.m112.396200;
RA Buerstenbinder K., Savchenko T., Mueller J., Adamson A.W., Stamm G.,
RA Kwong R., Zipp B.J., Dinesh D.C., Abel S.;
RT "Arabidopsis calmodulin-binding protein IQ67-domain 1 localizes to
RT microtubules and interacts with kinesin light chain-related protein-1.";
RL J. Biol. Chem. 288:1871-1882(2013).
RN [8]
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).
RN [9]
RP INTERACTION WITH ILK1.
RX PubMed=27208244; DOI=10.1104/pp.16.00035;
RA Brauer E.K., Ahsan N., Dale R., Kato N., Coluccio A.E., Pineros M.A.,
RA Kochian L.V., Thelen J.J., Popescu S.C.;
RT "The Raf-like kinase ILK1 and the high affinity K+ transporter HAK5 are
RT required for innate immunity and abiotic stress response.";
RL Plant Physiol. 171:1470-1484(2016).
CC -!- FUNCTION: Potential calcium sensor. {ECO:0000269|PubMed:11855649}.
CC -!- SUBUNIT: Interacts with IQD1 (PubMed:23204523). Interacts with ILK1
CC (PubMed:27208244). Binds to ABCG36 (PubMed:26315018).
CC {ECO:0000269|PubMed:23204523, ECO:0000269|PubMed:26315018,
CC ECO:0000269|PubMed:27208244}.
CC -!- INTERACTION:
CC Q9S744; Q9LDI3: CIPK24; NbExp=2; IntAct=EBI-1236048, EBI-537551;
CC Q9S744; Q9SSF8: CPK30; NbExp=2; IntAct=EBI-1236048, EBI-1235738;
CC Q9S744; P55737: HSP90-2; NbExp=2; IntAct=EBI-1236048, EBI-1235834;
CC Q9S744; Q9SND6: MAPKKK20; NbExp=2; IntAct=EBI-1236048, EBI-1235872;
CC Q9S744; P83755: psbA; NbExp=2; IntAct=EBI-1236048, EBI-1236013;
CC Q9S744; Q2V359: SAUR70; NbExp=2; IntAct=EBI-1236048, EBI-1235819;
CC Q9S744; Q9SUP6: WRKY53; NbExp=2; IntAct=EBI-1236048, EBI-1235980;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers and siliques.
CC {ECO:0000269|PubMed:11855649}.
CC -!- INDUCTION: By touch and during darkness conditions.
CC {ECO:0000269|PubMed:15720654}.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; AF178075; AAD53315.1; -; mRNA.
DR EMBL; AL049711; CAB41312.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78863.1; -; Genomic_DNA.
DR EMBL; AF380635; AAK55716.1; -; mRNA.
DR EMBL; AY054133; AAL06794.1; -; mRNA.
DR PIR; T49071; T49071.
DR RefSeq; NP_190760.1; NM_115051.3.
DR AlphaFoldDB; Q9S744; -.
DR SMR; Q9S744; -.
DR BioGRID; 9673; 119.
DR IntAct; Q9S744; 115.
DR STRING; 3702.AT3G51920.1; -.
DR PaxDb; Q9S744; -.
DR PRIDE; Q9S744; -.
DR ProteomicsDB; 240910; -.
DR EnsemblPlants; AT3G51920.1; AT3G51920.1; AT3G51920.
DR GeneID; 824355; -.
DR Gramene; AT3G51920.1; AT3G51920.1; AT3G51920.
DR KEGG; ath:AT3G51920; -.
DR Araport; AT3G51920; -.
DR TAIR; locus:2083700; AT3G51920.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; Q9S744; -.
DR OMA; QQMMSDV; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; Q9S744; -.
DR PRO; PR:Q9S744; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S744; baseline and differential.
DR Genevisible; Q9S744; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0019722; P:calcium-mediated signaling; IGI:TAIR.
DR GO; GO:0005513; P:detection of calcium ion; ISS:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; 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; 2.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..151
FT /note="Calmodulin-like protein 9"
FT /id="PRO_0000073653"
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..151
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 151 AA; 17036 MW; D6DEF91B10D0E48A CRC64;
MADAFTDEQI QEFYEAFCLI DKDSDGFITK EKLTKVMKSM GKNPKAEQLQ QMMSDVDIFG
NGGITFDDFL YIMAQNTSQE SASDELIEVF RVFDRDGDGL ISQLELGEGM KDMGMKITAE
EAEHMVREAD LDGDGFLSFH EFSKMMIAAS Y
