CALM1_ARATH
ID CALM1_ARATH Reviewed; 149 AA.
AC P0DH95; P25854; Q03510; Q9FJ05;
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-1;
DE Short=CaM-1;
GN Name=CAM1; OrderedLocusNames=At5g37780; ORFNames=K22F20.2, T31G3.3;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [MRNA] OF 14-149.
RX PubMed=16668320; DOI=10.1104/pp.96.4.1196;
RA Ling V., Perera I.Y., Zielinski R.E.;
RT "Primary structures of Arabidopsis calmodulin isoforms deduced from the
RT sequences of cDNA clones.";
RL Plant Physiol. 96:1196-1202(1991).
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 MEE62.
RX PubMed=14720124; DOI=10.1042/bj20031045;
RA Charpenteau M., Jaworski K., Ramirez B.C., Tretyn A., Ranjeva R., Ranty B.;
RT "A receptor-like kinase from Arabidopsis thaliana is a calmodulin-binding
RT protein.";
RL Biochem. J. 379:841-848(2004).
RN [8]
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 [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ZAR1.
RX PubMed=27014878; DOI=10.1371/journal.pgen.1005933;
RA Yu T.Y., Shi D.Q., Jia P.F., Tang J., Li H.J., Liu J., Yang W.C.;
RT "The Arabidopsis receptor kinase ZAR1 is required for zygote asymmetric
RT division and its daughter cell fate.";
RL PLoS Genet. 12:E1005933-E1005933(2016).
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 ZAR1 (via CaMBD domain) (PubMed:27014878).
CC Binds to IQD1 (PubMed:23204523). Binds to MEE62 in a calcium-dependent
CC manner (PubMed:14720124). {ECO:0000269|PubMed:14720124,
CC ECO:0000269|PubMed:23204523, ECO:0000269|PubMed:27014878}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27014878}. Cell
CC membrane {ECO:0000269|PubMed:14593172}. Note=Localizes to the plasma
CC membrane when interacting with ZAR1. {ECO:0000269|PubMed:27014878}.
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=P0DH95-1; 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; AB016873; BAB10354.1; -; Genomic_DNA.
DR EMBL; AB026662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED94230.1; -; Genomic_DNA.
DR EMBL; AY059809; AAL24291.1; -; mRNA.
DR EMBL; AY048276; AAK82538.1; -; mRNA.
DR EMBL; AY072520; AAL66935.1; -; mRNA.
DR EMBL; AY072628; AAL62019.1; -; mRNA.
DR EMBL; M38379; AAA32762.1; -; mRNA.
DR PIR; T50929; T50929.
DR RefSeq; NP_176814.1; NM_105312.4. [P0DH95-1]
DR RefSeq; NP_198594.1; NM_123137.4. [P0DH95-1]
DR AlphaFoldDB; P0DH95; -.
DR SMR; P0DH95; -.
DR BioGRID; 19007; 143.
DR BioGRID; 28180; 3.
DR STRING; 3702.AT1G66410.2; -.
DR iPTMnet; P0DH95; -.
DR PRIDE; P0DH95; -.
DR EnsemblPlants; AT1G66410.1; AT1G66410.1; AT1G66410.
DR EnsemblPlants; AT5G37780.1; AT5G37780.1; AT5G37780.
DR GeneID; 833756; -.
DR GeneID; 842959; -.
DR Gramene; AT1G66410.1; AT1G66410.1; AT1G66410.
DR Gramene; AT5G37780.1; AT5G37780.1; AT5G37780.
DR KEGG; ath:AT1G66410; -.
DR KEGG; ath:AT5G37780; -.
DR Araport; AT5G37780; -.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; P0DH95; -.
DR OMA; HPEATHA; -.
DR PhylomeDB; P0DH95; -.
DR PRO; PR:P0DH95; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P0DH95; baseline and differential.
DR Genevisible; P0DH95; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; Cell membrane; Cytoplasm; Membrane;
KW Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..149
FT /note="Calmodulin-1"
FT /id="PRO_0000415789"
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; 16862 MW; 805B06B97552ECC1 CRC64;
MADQLTDEQI SEFKEAFSLF DKDGDGCITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL NLMAKKMKDT DSEEELKEAF RVFDKDQNGF ISAAELRHVM TNLGEKLTDE
EVEEMIREAD VDGDGQINYE EFVKIMMAK
