CDPK1_PLAYO
ID CDPK1_PLAYO Reviewed; 535 AA.
AC Q7RAH3;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Calcium-dependent protein kinase 1;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P62344};
GN Name=CDPK1 {ECO:0000250|UniProtKB:P62344}; Synonyms=CPK1; ORFNames=PY06527;
OS Plasmodium yoelii yoelii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=73239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17XNL;
RX PubMed=12368865; DOI=10.1038/nature01099;
RA Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA Shoaibi A., Cummings L.M., Florens L., Yates J.R. III, Raine J.D.,
RA Sinden R.E., Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W.,
RA Vaidya A.B., van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA Carucci D.J.;
RT "Genome sequence and comparative analysis of the model rodent malaria
RT parasite Plasmodium yoelii yoelii.";
RL Nature 419:512-519(2002).
CC -!- FUNCTION: Calcium-dependent protein kinase which acts as a sensor and
CC effector of intracellular Ca(2+) levels probably in part downstream of
CC cGMP-activated PKG kinase (By similarity). During the liver stage,
CC involved in sporozoite motility and thus in sporozoite invasion of host
CC hepatocytes, probably together with CDPK4 and CDPK5. In the mosquito
CC midgut and during the last stage of male gamete exflagellation, may
CC play a role in the rupture of the host erythrocyte membrane. In the
CC mosquito midgut, required for the differentiation of the zygote into
CC the ookinete by promoting the translational activation of a subset of
CC repressed mRNAs; these mRNAs are kept repressed in the zygote by the
CC DOZI- or CITH-containing mRNP complexes. Dispensable during the asexual
CC blood stage (By similarity). {ECO:0000250|UniProtKB:A0A509AHB6,
CC ECO:0000250|UniProtKB:P62344}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P62344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P62344};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P62344};
CC -!- ACTIVITY REGULATION: Activated by calcium. Upon calcium binding to the
CC EF-hand domains, the C-terminus of the junction domain (J domain)
CC undergoes a conformational change which results in the dissociation of
CC the pseudo-substrate inhibitory motif from the catalytic domain. This,
CC in turn may facilitate the autophosphorylation of the activation loop
CC at Thr-230, which leads to the kinase activation.
CC {ECO:0000250|UniProtKB:P62344}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P62344}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P62344}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P62344}. Cell membrane
CC {ECO:0000250|UniProtKB:A0A509AHB6}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P62344}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P62344}. Parasitophorous vacuole membrane
CC {ECO:0000250|UniProtKB:P62344}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P62344}. Cytoplasm
CC {ECO:0000250|UniProtKB:A0A2I0BVG8}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:A0A2I0BVG8}. Host cell membrane
CC {ECO:0000250|UniProtKB:P62344}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P62344}. Note=Calcium and/or autophosphorylation
CC does not affect membrane localization. {ECO:0000250|UniProtKB:P62344}.
CC -!- DOMAIN: The junction domain (J domain) is composed of 2 motifs that
CC maintain the kinase inactive. The N-terminal autoinhibitory motif acts
CC as a pseudosubstrate inhibiting the catalytic domain while the C-
CC terminal motif binds the EF-hand domains.
CC {ECO:0000250|UniProtKB:P62344}.
CC -!- PTM: Myristoylated. Myristoylation and palmitoylation are required for
CC the localization to the parasitophorous vacuole membrane.
CC {ECO:0000250|UniProtKB:P62344}.
CC -!- PTM: Palmitoylated. Palmitoylation increases in merozoites in response
CC to low level of extracellular K(+) in the host blood. Myristoylation
CC and palmitoylation are required for the localization to the
CC parasitophorous vacuole membrane. {ECO:0000250|UniProtKB:P62344}.
CC -!- PTM: Phosphorylation at Thr-230 may regulate CDPK1 kinase activity.
CC Phosphorylation increases in response to an increase in intracellular
CC Ca(2+) levels. Autophosphorylated in vitro. Autophosphorylation does
CC not affect membrane localization in vitro.
CC {ECO:0000250|UniProtKB:P62344}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDPK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AABL01002214; EAA18754.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7RAH3; -.
DR SMR; Q7RAH3; -.
DR STRING; 73239.Q7RAH3; -.
DR EnsemblProtists; EAA18754; EAA18754; EAA18754.
DR InParanoid; Q7RAH3; -.
DR OMA; KFDECDA; -.
DR Proteomes; UP000008553; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020005; C:symbiont-containing vacuole membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; 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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13499; EF-hand_7; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00054; EFh; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Calcium; Cell membrane; Cell projection; Cilium; Cytoplasm;
KW Flagellum; Host cell membrane; Host membrane; Kinase; Lipoprotein;
KW Membrane; Metal-binding; Myristate; Nucleotide-binding; Palmitate;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62344"
FT CHAIN 2..535
FT /note="Calcium-dependent protein kinase 1"
FT /id="PRO_0000085836"
FT DOMAIN 57..324
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 371..406
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 415..450
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 451..486
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 497..532
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..363
FT /note="J domain"
FT /evidence="ECO:0000250|UniProtKB:P62344"
FT MOTIF 345..352
FT /note="J domain autoinhibitory motif"
FT /evidence="ECO:0000250|UniProtKB:P62344"
FT MOTIF 353..363
FT /note="J domain interacts with the EF-hand domains"
FT /evidence="ECO:0000250|UniProtKB:P62344"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 63..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 428
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 432
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 434
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 439
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 475
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 510
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 512
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 514
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 516
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 521
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62344"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62344"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62344"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62344"
FT MOD_RES 230
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62344"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62344"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P62344"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62344"
SQ SEQUENCE 535 AA; 62279 MW; 142682BF2AC1A557 CRC64;
MGCNQSKSAN DVRGNKVNNV NSKKKNNKRE DINDGEEIAI NPGMYVRKKE GKIGESYFKV
RKLGSGAYGE VLLCKEKNGH SEKAIKVIKK SQFDKGRYND DNKNIEKFHE EIYNEISLLK
SLDHPNIIKL FDVFEDKKYF YLVTEFYEGG ELFEQIINRH KFDECDAANI MKQILSGICY
LHKHNIVHRD IKPENILLEN KNSLLNIKIV DFGLSSFFSK DYKLRDRLGT AYYIAPEVLK
KKYNEKCDVW SCGVIMYILL CGYPPFGGQN DQDIIKKVEK GKYYFDFNDW KNISDEAKEL
IKLMLTYDYN KRCTAEEALN SRWIKKYANN INKSDQKTLC GALSNMRKFE GSQKLAQAAI
LFIGSKLTTL EERKELTDIF KKLDKNGDGQ LDKKELIEGY NVLRNFKNEL GELKNVEEEV
DNILKEVDFD KNGYIEYSEF ISVCMDKQIL FSEERLRRAF NLFDTDKSGK ITKEELANVI
IRGFYFFTYS LFGLTSVSEK TWNDVLGEAD QNKDNMIDFD EFVSMMHKIC DNKPF
