CALM2_ARATH
ID CALM2_ARATH Reviewed; 149 AA.
AC P0DH97; P25069;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Calmodulin-2;
DE Short=CaM-2;
GN Name=CAM2; Synonyms=ATCAL5, CAL1;
GN OrderedLocusNames=At2g41110 {ECO:0000312|Araport:AT2G41110};
GN ORFNames=T3K9.12 {ECO:0000312|EMBL:AAD12000.1};
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. C24; TISSUE=Seedling;
RX PubMed=8173593;
RA Chandra A., Upadhyaya K.C.;
RT "Structure and organization of a novel calmodulin gene of Arabidopsis
RT thaliana.";
RL Cell. Mol. Biol. Res. 39:509-516(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8564305;
RA Ito T., Hirano M., Akama K., Shimura Y., Okada K.;
RT "Touch-inducible genes for calmodulin and a calmodulin-related protein are
RT located in tandem on a chromosome of Arabidopsis thaliana.";
RL Plant Cell Physiol. 36:1369-1373(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-149.
RX PubMed=8507825; DOI=10.1007/bf00014930;
RA Gawienowski M.C., Szymanski D., Perera I.Y., Zielinski R.E.;
RT "Calmodulin isoforms in Arabidopsis encoded by multiple divergent mRNAs.";
RL Plant Mol. Biol. 22:215-225(1993).
RN [7]
RP INTERACTION WITH KCBP.
RX PubMed=10531384; DOI=10.1074/jbc.274.44.31727;
RA Reddy V.S., Safadi F., Zielinski R.E., Reddy A.S.;
RT "Interaction of a kinesin-like protein with calmodulin isoforms from
RT Arabidopsis.";
RL J. Biol. Chem. 274:31727-31733(1999).
RN [8]
RP INTERACTION WITH CAM2.
RX PubMed=11346951; DOI=10.1007/s004250000440;
RA Buaboocha T., Liao B., Zielinski R.E.;
RT "Isolation of cDNA and genomic DNA clones encoding a calmodulin-binding
RT protein related to a family of ATPases involved in cell division and
RT vesicle fusion.";
RL Planta 212:774-781(2001).
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 INTERACTION WITH IQD1 AND IQD20, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
CC ion channels and other proteins by Ca(2+). Among the enzymes to be
CC stimulated by the calmodulin-Ca(2+) complex are a number of protein
CC kinases and phosphatases.
CC -!- SUBUNIT: Interacts with KCBP and CIP111 (PubMed:10531384,
CC PubMed:11346951). Binds to IQD1 and IQD20 (PubMed:23204523).
CC {ECO:0000269|PubMed:10531384, ECO:0000269|PubMed:11346951,
CC ECO:0000269|PubMed:23204523}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23204523}. Cytoplasm {ECO:0000269|PubMed:23204523}.
CC Note=Recruited by IQD1 to microtubules. {ECO:0000269|PubMed:23204523}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P0DH97-1; Sequence=Displayed;
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; X67273; CAA47690.1; -; Genomic_DNA.
DR EMBL; D45848; BAA08283.1; -; Genomic_DNA.
DR EMBL; AC004261; AAD12000.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09932.1; -; Genomic_DNA.
DR EMBL; AY065179; AAL38355.1; -; mRNA.
DR EMBL; AY128752; AAM91152.1; -; mRNA.
DR EMBL; Z12023; CAA78058.1; -; mRNA.
DR PIR; H84667; H84667.
DR PIR; S22503; S22503.
DR RefSeq; NP_180271.1; NM_128261.5. [P0DH97-1]
DR RefSeq; NP_191239.1; NM_115539.5. [P0DH97-1]
DR RefSeq; NP_850344.1; NM_180013.3. [P0DH97-1]
DR AlphaFoldDB; P0DH97; -.
DR SMR; P0DH97; -.
DR BioGRID; 10163; 5.
DR BioGRID; 2597; 11.
DR BioGRID; 4047; 3.
DR IntAct; P0DH97; 1.
DR STRING; 3702.AT2G27030.3; -.
DR iPTMnet; P0DH97; -.
DR PaxDb; P0DH97; -.
DR PRIDE; P0DH97; -.
DR EnsemblPlants; AT2G27030.1; AT2G27030.1; AT2G27030.
DR EnsemblPlants; AT2G41110.1; AT2G41110.1; AT2G41110.
DR EnsemblPlants; AT3G56800.1; AT3G56800.1; AT3G56800.
DR GeneID; 817245; -.
DR GeneID; 818710; -.
DR GeneID; 824847; -.
DR Gramene; AT2G27030.1; AT2G27030.1; AT2G27030.
DR Gramene; AT2G41110.1; AT2G41110.1; AT2G41110.
DR Gramene; AT3G56800.1; AT3G56800.1; AT3G56800.
DR KEGG; ath:AT2G27030; -.
DR KEGG; ath:AT2G41110; -.
DR KEGG; ath:AT3G56800; -.
DR Araport; AT2G41110; -.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; P0DH97; -.
DR OMA; HQIEFDE; -.
DR PhylomeDB; P0DH97; -.
DR PRO; PR:P0DH97; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P0DH97; baseline and differential.
DR Genevisible; P0DH97; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
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 Alternative splicing; Calcium; Cytoplasm; Cytoskeleton; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..149
FT /note="Calmodulin-2"
FT /id="PRO_0000198281"
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"
SQ SEQUENCE 149 AA; 16820 MW; 722B188A90AD423A CRC64;
MADQLTDDQI SEFKEAFSLF DKDGDGCITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL NLMARKMKDT DSEEELKEAF RVFDKDQNGF ISAAELRHVM TNLGEKLTDE
EVDEMIKEAD VDGDGQINYE EFVKVMMAK
