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-MAY-2023, entry version 143. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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; 312751at2759; -. 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:0030234; F:enzyme regulator activity; 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 Gene3D; 1.10.238.10; EF-hand; 2. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR PANTHER; PTHR23049; MYOSIN REGULATORY LIGHT CHAIN 2; 1. DR PANTHER; PTHR23049:SF34; MYOSIN REGULATORY LIGHT CHAIN SQH; 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; 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 //