CALM_PLAFA
ID CALM_PLAFA Reviewed; 149 AA.
AC P24044;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Calmodulin {ECO:0000303|PubMed:1915742};
GN Name=CAM {ECO:0000303|PubMed:3313391};
OS Plasmodium falciparum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate FC27;
RX PubMed=1915742; DOI=10.1016/0014-4894(91)90098-h;
RA Cowman A.F., Galatis D.;
RT "Plasmodium falciparum: the calmodulin gene is not amplified or
RT overexpressed in chloroquine resistant or sensitive isolates.";
RL Exp. Parasitol. 73:269-275(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T9/96 / Thailand;
RX PubMed=1852174; DOI=10.1016/0166-6851(91)90195-c;
RA Robson K.J.H., Jennings M.W.;
RT "The structure of the calmodulin gene of Plasmodium falciparum.";
RL Mol. Biochem. Parasitol. 46:19-34(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8366883; DOI=10.1016/0166-6851(93)90022-p;
RA Robson K.J.H.;
RT "Sequence diversity in the intron of the calmodulin gene from Plasmodium
RT falciparum.";
RL Mol. Biochem. Parasitol. 60:1-8(1993).
RN [4]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=FCB {ECO:0000269|PubMed:3313391};
RX PubMed=3313391; DOI=10.1073/pnas.84.20.7310;
RA Scheibel L.W., Colombani P.M., Hess A.D., Aikawa M., Atkinson C.T.,
RA Milhous W.K.;
RT "Calcium and calmodulin antagonists inhibit human malaria parasites
RT (Plasmodium falciparum): implications for drug design.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7310-7314(1987).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=8720124; DOI=10.1093/oxfordjournals.jbchem.a124996;
RA Orfa Rojas M., Wasserman M.;
RT "Stage-specific expression of the calmodulin gene in Plasmodium
RT falciparum.";
RL J. Biochem. 118:1118-1123(1995).
CC -!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
CC ion channels and other proteins by Ca(2+) (By similarity). Among the
CC enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number
CC of protein kinases and phosphatases (By similarity).
CC {ECO:0000250|UniProtKB:P62203}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3313391}. Note=In
CC trophozoites and schizonts, localizes throughout the cytoplasm
CC (PubMed:3313391). In merozoites, localizes to the apical complex
CC (PubMed:3313391). {ECO:0000269|PubMed:3313391}.
CC -!- DEVELOPMENTAL STAGE: During the asexual blood stage, expression is low
CC in rings, increases in trophozoites to reach a peak in schizonts (at
CC protein level). {ECO:0000269|PubMed:3313391,
CC ECO:0000269|PubMed:8720124}.
CC -!- MISCELLANEOUS: Calmodulin is not involved in the mechanism of
CC chloroquine resistance. {ECO:0000269|PubMed:1915742}.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; M59349; AAA29509.1; -; Genomic_DNA.
DR EMBL; X56950; CAA40264.1; -; Genomic_DNA.
DR EMBL; M59770; AAA29510.1; -; Genomic_DNA.
DR EMBL; M99442; AAA29508.1; -; Genomic_DNA.
DR PIR; B45594; MCZQF.
DR AlphaFoldDB; P24044; -.
DR SMR; P24044; -.
DR EnsemblProtists; CZU00039; CZU00039; PF3D7_1434200.
DR VEuPathDB; PlasmoDB:PF3D7_1434200; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000508000; -.
DR VEuPathDB; PlasmoDB:Pf7G8_140039400; -.
DR VEuPathDB; PlasmoDB:PfCD01_140039600; -.
DR VEuPathDB; PlasmoDB:PfDd2_140038600; -.
DR VEuPathDB; PlasmoDB:PfGA01_140039700; -.
DR VEuPathDB; PlasmoDB:PfGB4_140040300; -.
DR VEuPathDB; PlasmoDB:PfGN01_140039500; -.
DR VEuPathDB; PlasmoDB:PfHB3_140039900; -.
DR VEuPathDB; PlasmoDB:PfIT_140040600; -.
DR VEuPathDB; PlasmoDB:PfKE01_140039100; -.
DR VEuPathDB; PlasmoDB:PfKH01_140039700; -.
DR VEuPathDB; PlasmoDB:PfKH02_140039900; -.
DR VEuPathDB; PlasmoDB:PfML01_140039600; -.
DR VEuPathDB; PlasmoDB:PfNF135_140038400; -.
DR VEuPathDB; PlasmoDB:PfNF166_140037100; -.
DR VEuPathDB; PlasmoDB:PfNF54_140038000; -.
DR VEuPathDB; PlasmoDB:PfSD01_140037500; -.
DR VEuPathDB; PlasmoDB:PfSN01_140041400; -.
DR VEuPathDB; PlasmoDB:PfTG01_140039500; -.
DR OMA; SCDRHPP; -.
DR GO; GO:0020007; C:apical complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 1: Evidence at protein level;
KW Acetylation; Calcium; Cytoplasm; Metal-binding; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT CHAIN 2..149
FT /note="Calmodulin"
FT /id="PRO_0000198264"
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"
FT CONFLICT 28..30
FT /note="Missing (in Ref. 1; AAA29509/CAA40264)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 149 AA; 16931 MW; 30D806FDA42BC173 CRC64;
MADKLTEEQI SEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEIDTDG
NGTIDFPEFL TLMARKLKDT DTEEELIEAF RVFDRDGDGY ISADELRHVM TNLGEKLTNE
EVDEMIREAD IDGDGQINYE EFVKMMIAK
