ID CML1_ORYSI Reviewed; 187 AA.
AC Q40642; Q7G0S4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Calmodulin-like protein 1;
DE AltName: Full=OsCaM61;
DE Flags: Precursor;
GN Name=CML1; ORFNames=OsI_004066;
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 / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Guang-Lu-Ai No.4; TISSUE=Shoot;
RX PubMed=10470849; DOI=10.1093/dnares/6.3.179;
RA Xiao C., Xin H., Dong A., Sun C., Cao K.;
RT "A novel calmodulin-like protein gene in rice which has an unusual
RT prolonged C-terminal sequence carrying a putative prenylation site.";
RL DNA Res. 6:179-181(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Milyang 117;
RA Choi Y.J., Kim C.Y., Cheon S.Y., Cho M.J.;
RT "Identification and characterization of fungal elicitor responsive genes by
RT mRNA differential display.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP SUBCELLULAR LOCATION, AND ISOPRENYLATION AT CYS-184.
RX PubMed=11855722; DOI=10.1023/a:1013380814919;
RA Dong A., Xin H., Yu Y., Sun C., Cao K., Shen W.-H.;
RT "The subcellular localization of an unusual rice calmodulin isoform,
RT OsCaM61, depends on its prenylation status.";
RL Plant Mol. Biol. 48:203-210(2002).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF SER-27; ASN-63; LYS-67; GLY-71; LYS-80;
RP ALA-111; GLY-123; SER-127 AND CYS-145.
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 [6]
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: Calcium-binding protein that binds and activates CAMK1, a
CC calcium/calmodulin-dependent kinase. {ECO:0000269|PubMed:16842786}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:11855722}; Lipid-
CC anchor {ECO:0000305|PubMed:11855722}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, etiolated shoots and flowers.
CC {ECO:0000269|PubMed:10470849}.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; U37936; AAA98933.1; -; mRNA.
DR EMBL; AF064456; AAC18355.1; -; Genomic_DNA.
DR EMBL; AF231026; AAF33852.1; -; mRNA.
DR EMBL; CM000126; EAY76219.1; -; Genomic_DNA.
DR PIR; T02887; T02887.
DR AlphaFoldDB; Q40642; -.
DR SMR; Q40642; -.
DR IntAct; Q40642; 1.
DR MINT; Q40642; -.
DR STRING; 39946.Q40642; -.
DR EnsemblPlants; BGIOSGA004661-TA; BGIOSGA004661-PA; BGIOSGA004661.
DR Gramene; BGIOSGA004661-TA; BGIOSGA004661-PA; BGIOSGA004661.
DR HOGENOM; CLU_061288_2_0_1; -.
DR OMA; YICADEL; -.
DR Proteomes; UP000007015; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 2.
DR Gene3D; 1.10.238.10; EF-hand; 3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23050; CALCIUM BINDING PROTEIN; 1.
DR PANTHER; PTHR23050:SF562; CALMODULIN-LIKE PROTEIN 1; 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; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Lipoprotein; Membrane; Metal-binding; Methylation;
KW Prenylation; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..184
FT /note="Calmodulin-like protein 1"
FT /id="PRO_0000338415"
FT PROPEP 185..187
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396746"
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..152
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 153..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
FT MOD_RES 184
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 184
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000305|PubMed:11855722"
FT MUTAGEN 27
FT /note="S->C: No effect on CAMK1 activation."
FT /evidence="ECO:0000269|PubMed:16842786"
FT MUTAGEN 63
FT /note="N->T: No effect on CAMK1 activation."
FT /evidence="ECO:0000269|PubMed:16842786"
FT MUTAGEN 67
FT /note="K->P: No effect on CAMK1 activation."
FT /evidence="ECO:0000269|PubMed:16842786"
FT MUTAGEN 71
FT /note="G->N: No effect on CAMK1 activation."
FT /evidence="ECO:0000269|PubMed:16842786"
FT MUTAGEN 80
FT /note="K->T: No effect on CAMK1 activation."
FT /evidence="ECO:0000269|PubMed:16842786"
FT MUTAGEN 111
FT /note="A->T: No effect on CAMK1 binding. Decrease in CAMK1
FT activation. Loss of CAMK1 activation; when associated with
FT D-123 and R-127."
FT /evidence="ECO:0000269|PubMed:16842786"
FT MUTAGEN 123
FT /note="G->D: No effect on CAMK1 binding. Decrease in CAMK1
FT activation. Loss of CAMK1 activation; when associated with
FT T-111 and R-127."
FT /evidence="ECO:0000269|PubMed:16842786"
FT MUTAGEN 127
FT /note="S->R: No effect on CAMK1 binding. Decrease in CAMK1
FT activation. Loss of CAMK1 activation; when associated with
FT T-111 and D-123."
FT /evidence="ECO:0000269|PubMed:16842786"
FT MUTAGEN 145
FT /note="C->V: No effect on CAMK1 activation."
FT /evidence="ECO:0000269|PubMed:16842786"
SQ SEQUENCE 187 AA; 20973 MW; 7F47AE5CDC8ABB9C CRC64;
MADQLSEEQI VEFREAFSLF DKDGDGSITT KELGTVMRSL GQNPTEAELQ DMISEVDADS
NGNIEFKEFL GLMARKLRDK DSEEELKEAF RVFDKDQNGF ISAAELRHVM ANIGERLTDE
EVGEMISEAD VDGDGQINYE EFVKCMMAKK RRKRIEEKRE HDGGSRTKSA GPSAAPASKR
GQKCVIL
//
