CALM1_ORYSI
ID CALM1_ORYSI Reviewed; 149 AA.
AC A2WN93; A2XG28; A2YQ37; A6N0J2; O49184; P29612; Q7F8I8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Calmodulin-1;
DE Short=CaM-1;
GN Name=CAM1-1; ORFNames=OsI_011021;
GN and
GN Name=CAM1-2; ORFNames=OsI_026430;
GN and
GN Name=CAM1-3; ORFNames=OsI_001286;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CAM1-2).
RC STRAIN=cv. IR36;
RA Choi Y., Kim S.R., Poovaiah B.W., An G.;
RT "Structural organization of monocot calmodulin genes and promoter activity
RT in transgenic tobacco plants.";
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (CAM1-1; CAM1-2 AND CAM1-3).
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (CAM1-1).
RC STRAIN=cv. Pokkali; TISSUE=Root;
RA Kumari S., Panjabi V., Singla-Pareek S.L., Sopory S.K., Pareek A.;
RT "A comparative transcriptome map of early and late salinity stress
RT responses in contrasting genotypes of Oryza sativa L.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP MUTAGENESIS OF THR-111; ASP-123 AND ARG-127.
RX PubMed=16842786; DOI=10.1016/j.febslet.2006.06.090;
RA Li D.-F., Li J., Ma L., Zhang L., Lu Y.-T.;
RT "Calmodulin isoform-specific activation of a rice calmodulin-binding kinase
RT conferred by only three amino-acids of OsCaM61.";
RL FEBS Lett. 580:4325-4331(2006).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17263873; DOI=10.1186/1471-2229-7-4;
RA Boonburapong B., Buaboocha T.;
RT "Genome-wide identification and analyses of the rice calmodulin and related
RT potential calcium sensor proteins.";
RL BMC Plant Biol. 7:4-4(2007).
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 -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; Z12827; CAA78287.1; -; Genomic_DNA.
DR EMBL; L18913; AAA33901.1; -; Genomic_DNA.
DR EMBL; CM000128; EAY89788.1; -; Genomic_DNA.
DR EMBL; CM000132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EF576174; ABR25762.1; -; mRNA.
DR PIR; S24952; S24952.
DR AlphaFoldDB; A2WN93; -.
DR SMR; A2WN93; -.
DR IntAct; A2WN93; 1.
DR MINT; A2WN93; -.
DR STRING; 39946.A2WN93; -.
DR iPTMnet; A2WN93; -.
DR EnsemblPlants; BGIOSGA001926-TA; BGIOSGA001926-PA; BGIOSGA001926.
DR EnsemblPlants; BGIOSGA012515-TA; BGIOSGA012515-PA; BGIOSGA012515.
DR EnsemblPlants; BGIOSGA023690-TA; BGIOSGA023690-PA; BGIOSGA023690.
DR Gramene; BGIOSGA001926-TA; BGIOSGA001926-PA; BGIOSGA001926.
DR Gramene; BGIOSGA012515-TA; BGIOSGA012515-PA; BGIOSGA012515.
DR Gramene; BGIOSGA023690-TA; BGIOSGA023690-PA; BGIOSGA023690.
DR HOGENOM; CLU_061288_2_0_1; -.
DR OMA; HQIEFDE; -.
DR Proteomes; UP000007015; Chromosome 1.
DR Proteomes; UP000007015; Chromosome 3.
DR Proteomes; UP000007015; Chromosome 7.
DR ExpressionAtlas; A2WN93; differential.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 Acetylation; Calcium; Metal-binding; Methylation; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..149
FT /note="Calmodulin-1"
FT /id="PRO_0000293081"
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
FT MOD_RES 116
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 111
FT /note="T->A: Triggers activation of CAMK1; when associated
FT with G-123 and S-127."
FT /evidence="ECO:0000269|PubMed:16842786"
FT MUTAGEN 123
FT /note="D->G: Triggers activation of CAMK1; when associated
FT with A-111 and S-127."
FT /evidence="ECO:0000269|PubMed:16842786"
FT MUTAGEN 127
FT /note="R->S: Triggers activation of CAMK1; when associated
FT with A-111 and G-123."
FT /evidence="ECO:0000269|PubMed:16842786"
SQ SEQUENCE 149 AA; 16832 MW; F52AF0516677508D CRC64;
MADQLTDDQI AEFKEAFSLF DKDGDGCITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL NLMARKMKDT DSEEELKEAF RVFDKDQNGF ISAAELRHVM TNLGEKLTDE
EVDEMIREAD VDGDGQINYE EFVKVMMAK
