CALM_PLAF7
ID CALM_PLAF7 Reviewed; 149 AA.
AC P62203; A0A144A1Y0;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Calmodulin {ECO:0000303|PubMed:12368864};
DE Short=PfCaM {ECO:0000303|PubMed:32821880};
GN Name=CAM {ECO:0000305}; ORFNames=PF14_0323, PF3D7_1434200;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2]
RP FUNCTION.
RX PubMed=32821880; DOI=10.1096/fba.2020-00013;
RA Juhasz T., Kardos J., Duervanger Z., Harmat V., Liliom K.;
RT "Comparison of ligand binding and conformational stability of human
RT calmodulin with its homolog from the malaria parasite Plasmodium
RT falciparum.";
RL FASEB Bioadv. 2:489-505(2020).
CC -!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
CC ion channels and other proteins by Ca(2+) (PubMed:32821880). Among the
CC enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number
CC of protein kinases and phosphatases (PubMed:32821880).
CC {ECO:0000269|PubMed:32821880}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P24044}. Note=In
CC trophozoites and schizonts, localizes throughout the cytoplasm. In
CC merozoites, localizes to the apical complex.
CC {ECO:0000250|UniProtKB:P24044}.
CC -!- MISCELLANEOUS: Calmodulin is not involved in the mechanism of
CC chloroquine resistance. {ECO:0000250|UniProtKB:P24044}.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; LN999946; CZU00039.1; -; Genomic_DNA.
DR RefSeq; XP_001348497.1; XM_001348461.1.
DR AlphaFoldDB; P62203; -.
DR SMR; P62203; -.
DR BioGRID; 1207263; 10.
DR IntAct; P62203; 7.
DR STRING; 5833.PF14_0323; -.
DR PRIDE; P62203; -.
DR EnsemblProtists; CZU00039; CZU00039; PF3D7_1434200.
DR GeneID; 811905; -.
DR KEGG; pfa:PF3D7_1434200; -.
DR VEuPathDB; PlasmoDB:PF3D7_1434200; -.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; P62203; -.
DR OMA; SCDRHPP; -.
DR PhylomeDB; P62203; -.
DR Reactome; R-PFA-111932; CaMK IV-mediated phosphorylation of CREB.
DR Reactome; R-PFA-111957; Cam-PDE 1 activation.
DR Reactome; R-PFA-114608; Platelet degranulation.
DR Reactome; R-PFA-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-PFA-203615; eNOS activation.
DR Reactome; R-PFA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-PFA-4086398; Ca2+ pathway.
DR Reactome; R-PFA-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR Reactome; R-PFA-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-PFA-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR Reactome; R-PFA-6798695; Neutrophil degranulation.
DR Reactome; R-PFA-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-PFA-9619229; Activation of RAC1 downstream of NMDARs.
DR Proteomes; UP000001450; Chromosome 14.
DR GO; GO:0020007; C:apical complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0061891; F:calcium ion sensor activity; IDA:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; IDA:UniProtKB.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:UniProt.
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 3: Inferred from homology;
KW Acetylation; Calcium; Cytoplasm; Metal-binding; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT CHAIN 2..149
FT /note="Calmodulin"
FT /id="PRO_0000198265"
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 100
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|UniProtKB:P0DP23"
SQ SEQUENCE 149 AA; 16931 MW; 30D806FDA42BC173 CRC64;
MADKLTEEQI SEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEIDTDG
NGTIDFPEFL TLMARKLKDT DTEEELIEAF RVFDRDGDGY ISADELRHVM TNLGEKLTNE
EVDEMIREAD IDGDGQINYE EFVKMMIAK
