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Entry version 127 (02 Jun 2021)
Sequence version 2 (23 Jan 2007)
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Protein

Calcium-dependent protein kinase 1

Gene

CDPK1

Organism
Plasmodium falciparum (isolate 3D7)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca2+ levels probably in part downstream of cGMP-activated PKG kinase (PubMed:18768477, PubMed:19307175, PubMed:28680058, PubMed:29716996).

By phosphorylating various proteins, required for microneme secretion and thus merozoite egress from and invasion of host erythrocytes (PubMed:23204525, PubMed:28680058, PubMed:29716996).

During gametogenesis, essential for the development of both male and female gametes (By similarity).

Phosphorylates SERA5 p50 which enhances SERA5 p50 protease activity; however, SERA5 p50 protease activity has been shown in other studies to be controversial (PubMed:29716996).

Probably by phosphorylating SERA5 p50, plays a role in merozoite egress from host erythrocytes (PubMed:29716996).

Probably prior or during merozoite invasion of host erythrocytes, phosphorylates rhoptry protein RhopH3 which is required for RhopH3 localization to rhoptries and for its secretion (PubMed:33024030).

Probably in late schizonts, phosphorylates myosin A tail domain-interacting protein MTIP and glideosome-associated protein 45 GAP45, both of which are components of the motor complex that generates the force required by the parasite to invade host cells (PubMed:18768477, PubMed:28680058, PubMed:22539638).

In late schizonts, phosphorylates inner membrane complex protein IMC1g (PubMed:28680058).

In late schizonts, phosphorylates PKA regulatory subunit PKAr in a calcium-dependent manner, which may contribute to the dissociation of regulatory PKAr and catalytic PKAc subunits and promote the activation of PKAc (PubMed:28680058).

May phosphorylate raf kinase inhibitory protein RKIP which in turn may regulate CDPK1 catalytic activity (PubMed:17123645).

May phosphorylate proteins of the host erythrocyte membranes (By similarity).

By similarity8 Publications

Caution

Unlike P.berghei CDPK1, appears to be involved in the asexual blood stage and in male gamete exflagellation prior host erythrocyte membrane rupture.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by calcium (PubMed:29716996, PubMed:18768477, PubMed:23204525, PubMed:17123645, PubMed:32484216). Upon calcium binding to the EF-hand domains, the C-terminus of the junction domain (J domain) undergoes a conformational change which results in the dissociation of the pseudo-substrate inhibitory motif from the catalytic domain (Probable) (PubMed:23204525). This, in turn may facilitate the autophosphorylation of the activation loop at Thr-231, which leads to the kinase activation (PubMed:19307175). May be negatively regulated by PKA-mediated phosphorylation (PubMed:28680058). Inhibited by purfalcamine (PubMed:23204525, PubMed:29716996).1 Publication7 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=9 µM for MTIP (at 30 degrees Celsius)1 Publication
  2. KM=18 µM for GAP45 (at 30 degrees Celsius)1 Publication
  3. KM=125 µM for ATP (with MTIP as substrate and at 30 degrees Celsius)1 Publication
  4. KM=96 µM for ATP (with GAP45 as substrate and at 30 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei85ATPPROSITE-ProRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei191Proton acceptorPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi62 – 70ATPPROSITE-ProRule annotation9
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi385 – 3961PROSITE-ProRule annotationAdd BLAST12
    Calcium bindingi429 – 4402PROSITE-ProRule annotationAdd BLAST12
    Calcium bindingi465 – 4763PROSITE-ProRule annotationAdd BLAST12
    Calcium bindingi499 – 5104PROSITE-ProRule annotationAdd BLAST12

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionKinase, Serine/threonine-protein kinase, Transferase
    LigandATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.7.11.1, 4889

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-PFA-111932, CaMK IV-mediated phosphorylation of CREB
    R-PFA-171007, p38MAPK events
    R-PFA-2559580, Oxidative Stress Induced Senescence
    R-PFA-4420097, VEGFA-VEGFR2 Pathway
    R-PFA-442729, CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde
    R-PFA-450302, activated TAK1 mediates p38 MAPK activation
    R-PFA-5687128, MAPK6/MAPK4 signaling

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Calcium-dependent protein kinase 1 (EC:2.7.11.17 Publications)
    Alternative name(s):
    PfCDPK11 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:CDPK11 Publication
    Synonyms:CPK1
    ORF Names:PF3D7_0217500, PFB0815w
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPlasmodium falciparum (isolate 3D7)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri36329 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaSarAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000001450 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

    Organism-specific databases

    Eukaryotic Pathogen, Vector and Host Database Resources

    More...
    VEuPathDBi
    PlasmoDB:PF3D7_0217500

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cilium, Cytoplasm, Flagellum, Host cell membrane, Host membrane, Membrane

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Conditional knockdown at the ring stage produces the development of mature schizonts and the subsequent release of merozoites from the host erythrocytes; however, the invasion of new erythrocytes by these merozoites is severely reduced due to a severe defect in adhesion to the erythrocyte membrane (PubMed:28680058). In merozoites, release of host glycophorin A/GYPA ligand EBA-175 from micronemes is impaired but not AMA1 (PubMed:28680058). In late schizont, phosphorylation of several proteins including GAP45, IMC1g and PKAr is reduced (PubMed:28680058). Reduced PKA activity (PubMed:28680058). Rhoptry protein RhopH3 phosphorylation and secretion are reduced in merozoites (PubMed:33024030).2 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2 – 50Missing : Severe loss of catalytic activity. 1 PublicationAdd BLAST49
    Mutagenesisi2 – 40Missing : Severe loss of catalytic activity. 1 PublicationAdd BLAST39
    Mutagenesisi2 – 30Missing : Severe loss of catalytic activity. 1 PublicationAdd BLAST29
    Mutagenesisi2 – 20Missing : No effect on catalytic activity. 1 PublicationAdd BLAST19
    Mutagenesisi2G → V: Loss of myristoylation. Severe reduction in membrane binding. Loss of membrane binding; when associated with 10-K--T-20 DEL. 1 Publication1
    Mutagenesisi10 – 20Missing : Does not affect myristoylation. Severe reduction in membrane binding. Loss of membrane binding; when associated with V-2. 1 PublicationAdd BLAST11
    Mutagenesisi27K → A: Severe loss of ATP binding. Partial loss of catalytic activity. 1 Publication1
    Mutagenesisi64S → A: Loss of phosphorylation. No effect on catalytic activity. 1 Publication1
    Mutagenesisi152E → A: Severe loss of catalytic activity. 1 Publication1
    Mutagenesisi154F → A: Severe loss of catalytic activity. 1 Publication1
    Mutagenesisi155E → A: No effect on catalytic activity. 1 Publication1
    Mutagenesisi157 – 158II → AA: Severe loss of catalytic activity. 1 Publication2
    Mutagenesisi191D → N: Loss of catalytic activity. 2 Publications1
    Mutagenesisi231T → A: Loss of catalytic activity. 1 Publication1
    Mutagenesisi335S → A: Loss of phosphorylation. Loss of catalytic activity. 1 Publication1
    Mutagenesisi335S → D: Phospho-mimetic mutant.No effect on catalytic activity. 1 Publication1
    Mutagenesisi339T → D: No effect on catalytic activity. 1 Publication1
    Mutagenesisi342 – 524Missing : Constitutively active. 1 PublicationAdd BLAST183
    Mutagenesisi347M → A: Severe loss of catalytic activity. 1 Publication1
    Mutagenesisi350F → A: Severe loss of catalytic activity. 2 Publications1
    Mutagenesisi353S → A: No effect on catalytic activity. 1 Publication1
    Mutagenesisi355K → A: No effect on catalytic activity. 1 Publication1
    Mutagenesisi356L → A: Severe loss of catalytic activity. 1 Publication1
    Mutagenesisi363 – 364FI → AA: Severe loss of catalytic activity. 1 Publication2
    Mutagenesisi366S → A: Slight decrease in catalytic activity. 1 Publication1
    Mutagenesisi369 – 370TT → AA: Slight decrease in catalytic activity. 1 Publication2
    Mutagenesisi456R → A: Severe loss of catalytic activity. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL1908387

    Drug and drug target database

    More...
    DrugBanki
    DB12010, Fostamatinib

    DrugCentral

    More...
    DrugCentrali
    P62344

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000858342 – 524Calcium-dependent protein kinase 1Add BLAST523

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine1 Publication1
    Lipidationi3S-palmitoyl cysteine2 Publications1
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei17Phosphoserine; by autocatalysis2 Publications1
    Modified residuei28Phosphoserine; by autocatalysis2 Publications1
    Modified residuei34Phosphoserine; by autocatalysis1 Publication1
    Modified residuei64Phosphoserine; by PKG; by autocatalysis3 Publications1
    Modified residuei100Phosphothreonine; by autocatalysis1 Publication1
    Modified residuei118Phosphoserine; by autocatalysis1 Publication1
    Modified residuei217Phosphoserine2 Publications1
    Modified residuei220Phosphoserine; by autocatalysis1 Publication1
    Modified residuei231Phosphothreonine; by PKG; by autocatalysis2 Publications1
    Modified residuei335Phosphoserine; by autocatalysis1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Myristoylated (PubMed:15491359). Myristoylation, palmitoylation and the basic cluster motif are required for the localization to the parasitophorous vacuole membrane (PubMed:15491359).1 Publication
    Palmitoylated (Probable) (PubMed:32003970). Palmitoylation increases in merozoites in response to low level of extracellular K+ in the host blood (PubMed:32003970). Myristoylation, palmitoylation and the basic cluster motif are required for the localization to the parasitophorous vacuole membrane (PubMed:15491359).1 Publication2 Publications
    Phosphorylation at Ser-64 occurs at late schizont stage and regulates CDPK1 protein-protein interaction (PubMed:26149123). Phosphorylated at Ser-28, Ser-34 and Ser-64 in merozoites in response to low extracellular level of K+ (PubMed:32817103). Phosphorylation at Thr-231 may regulate CDPK1 kinase activity (PubMed:26149123). Phosphorylation increases in response to an increase in intracellular Ca2+ levels (PubMed:32484216). Autophosphorylated in vitro (PubMed:17123645, PubMed:22539638, PubMed:23204525, PubMed:26149123, PubMed:32484216). Autophosphorylation does not affect membrane localization in vitro (PubMed:15491359).7 Publications

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P62344

    PTM databases

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P62344

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

    Expressed during parasite asexual blood stages, specifically at the ring and schizont stages, in free merozoites and to a lesser extent in trophozoites (at protein level).9 Publications

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer (PubMed:26149123).

    Forms a high molecular weight (250 and 400 kDa) complex (PubMed:26149123).

    Forms a complex composed of CDPK1, PKA regulatory subunit PKAr and 14-3-3I; the complex is formed in merozoites in response to low extracellular level of K+ and may play a role in microneme secretion (PubMed:32817103).

    Interacts (when phosphorylated) with 14-3-3I in a Ca2+-independent manner; the interaction does not regulate CDPK1 catalytic activity but is required for merozoite invasion of host erythrocytes (PubMed:32484216, PubMed:32817103).

    Interacts with PKA regulatory subunit PKAr; in a Ca2+-dependent manner (PubMed:28680058, PubMed:32817103).

    Interacts with SERA5 p50 in the late schizont stage (PubMed:29716996).

    Interacts with inner membrane complex protein IMC1g in late schizonts (PubMed:28680058).

    Interacts with rhoptry protein RhopH3 in merozoites (PubMed:33024030).

    6 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    1208081, 9 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P62344, 8 interactors

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P62344

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini56 – 325Protein kinasePROSITE-ProRule annotationAdd BLAST270
    Domaini372 – 407EF-hand 1PROSITE-ProRule annotationAdd BLAST36
    Domaini416 – 451EF-hand 2PROSITE-ProRule annotationAdd BLAST36
    Domaini452 – 487EF-hand 3PROSITE-ProRule annotationAdd BLAST36
    Domaini486 – 521EF-hand 4PROSITE-ProRule annotationAdd BLAST36

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 34DisorderedSequence analysisAdd BLAST34
    Regioni346 – 364J domain1 PublicationAdd BLAST19

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi10 – 20Basic cluster involved in membrane binding1 PublicationAdd BLAST11
    Motifi346 – 353J domain autoinhibitory motif1 Publication8
    Motifi354 – 364J domain interacts with the EF-hand domains1 Publication1 PublicationAdd BLAST11

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi18 – 34Polar residuesSequence analysisAdd BLAST17

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The junction domain (J domain) is composed of 2 motifs that maintain the kinase inactive (PubMed:19307175). The N-terminal autoinhibitory motif acts as a pseudosubstrate inhibiting the catalytic domain while the C-terminal motif binds the EF-hand domains (PubMed:19307175, PubMed:23204525).2 Publications

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_000288_37_4_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P62344

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    KFDECDA

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P62344

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00051, EFh, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR011992, EF-hand-dom_pair
    IPR018247, EF_Hand_1_Ca_BS
    IPR002048, EF_hand_dom
    IPR011009, Kinase-like_dom_sf
    IPR000719, Prot_kinase_dom
    IPR017441, Protein_kinase_ATP_BS
    IPR008271, Ser/Thr_kinase_AS

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF13499, EF-hand_7, 2 hits
    PF00069, Pkinase, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00054, EFh, 4 hits
    SM00220, S_TKc, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF47473, SSF47473, 1 hit
    SSF56112, SSF56112, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00018, EF_HAND_1, 4 hits
    PS50222, EF_HAND_2, 4 hits
    PS00107, PROTEIN_KINASE_ATP, 1 hit
    PS50011, PROTEIN_KINASE_DOM, 1 hit
    PS00108, PROTEIN_KINASE_ST, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P62344-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MGCSQSSNVK DFKTRRSKFT NGNNYGKSGN NKNSEDLAIN PGMYVRKKEG
    60 70 80 90 100
    KIGESYFKVR KLGSGAYGEV LLCREKHGHG EKAIKVIKKS QFDKMKYSIT
    110 120 130 140 150
    NKIECDDKIH EEIYNEISLL KSLDHPNIIK LFDVFEDKKY FYLVTEFYEG
    160 170 180 190 200
    GELFEQIINR HKFDECDAAN IMKQILSGIC YLHKHNIVHR DIKPENILLE
    210 220 230 240 250
    NKHSLLNIKI VDFGLSSFFS KDNKLRDRLG TAYYIAPEVL RKKYNEKCDV
    260 270 280 290 300
    WSCGVILYIL LCGYPPFGGQ NDQDIIKKVE KGKYYFDFND WKNISEEAKE
    310 320 330 340 350
    LIKLMLTYDY NKRITAKEAL NSKWIKKYAN NINKSDQKTL CGALSNMRKF
    360 370 380 390 400
    EGSQKLAQAA ILFIGSKLTT LEERKELTDI FKKLDKNGDG QLDKKELIEG
    410 420 430 440 450
    YNILRSFKNE LGELKNVEEE VDNILKEVDF DKNGYIEYSE FISVCMDKQI
    460 470 480 490 500
    LFSEERLRDA FNLFDTDKSG KITKEELANL FGLTSISEQM WNEVLGEADK
    510 520
    NKDNMIDFDE FVNMMHKICD NKSS
    Length:524
    Mass (Da):60,800
    Last modified:January 23, 2007 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD2A45E1579D2C951
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AE001362 Genomic DNA Translation: AAC71952.1
    LN999943 Genomic DNA Translation: CZT98189.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A45472

    NCBI Reference Sequences

    More...
    RefSeqi
    XP_001349680.1, XM_001349644.1

    Genome annotation databases

    Ensembl protists genome annotation project

    More...
    EnsemblProtistsi
    CZT98189; CZT98189; PF3D7_0217500

    GeneDB pathogen genome database from Sanger Institute

    More...
    GeneDBi
    PF3D7_0217500.1:pep

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    812762

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    pfa:PF3D7_0217500

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE001362 Genomic DNA Translation: AAC71952.1
    LN999943 Genomic DNA Translation: CZT98189.1
    PIRiA45472
    RefSeqiXP_001349680.1, XM_001349644.1

    3D structure databases

    SMRiP62344
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGRIDi1208081, 9 interactors
    IntActiP62344, 8 interactors

    Chemistry databases

    ChEMBLiCHEMBL1908387
    DrugBankiDB12010, Fostamatinib
    DrugCentraliP62344

    PTM databases

    SwissPalmiP62344

    Proteomic databases

    PRIDEiP62344

    Genome annotation databases

    EnsemblProtistsiCZT98189; CZT98189; PF3D7_0217500
    GeneDBiPF3D7_0217500.1:pep
    GeneIDi812762
    KEGGipfa:PF3D7_0217500

    Organism-specific databases

    VEuPathDBiPlasmoDB:PF3D7_0217500

    Phylogenomic databases

    HOGENOMiCLU_000288_37_4_1
    InParanoidiP62344
    OMAiKFDECDA
    PhylomeDBiP62344

    Enzyme and pathway databases

    BRENDAi2.7.11.1, 4889
    ReactomeiR-PFA-111932, CaMK IV-mediated phosphorylation of CREB
    R-PFA-171007, p38MAPK events
    R-PFA-2559580, Oxidative Stress Induced Senescence
    R-PFA-4420097, VEGFA-VEGFR2 Pathway
    R-PFA-442729, CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde
    R-PFA-450302, activated TAK1 mediates p38 MAPK activation
    R-PFA-5687128, MAPK6/MAPK4 signaling

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P62344

    Family and domain databases

    CDDicd00051, EFh, 1 hit
    InterProiView protein in InterPro
    IPR011992, EF-hand-dom_pair
    IPR018247, EF_Hand_1_Ca_BS
    IPR002048, EF_hand_dom
    IPR011009, Kinase-like_dom_sf
    IPR000719, Prot_kinase_dom
    IPR017441, Protein_kinase_ATP_BS
    IPR008271, Ser/Thr_kinase_AS
    PfamiView protein in Pfam
    PF13499, EF-hand_7, 2 hits
    PF00069, Pkinase, 1 hit
    SMARTiView protein in SMART
    SM00054, EFh, 4 hits
    SM00220, S_TKc, 1 hit
    SUPFAMiSSF47473, SSF47473, 1 hit
    SSF56112, SSF56112, 1 hit
    PROSITEiView protein in PROSITE
    PS00018, EF_HAND_1, 4 hits
    PS50222, EF_HAND_2, 4 hits
    PS00107, PROTEIN_KINASE_ATP, 1 hit
    PS50011, PROTEIN_KINASE_DOM, 1 hit
    PS00108, PROTEIN_KINASE_ST, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCDPK1_PLAF7
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P62344
    Secondary accession number(s): A0A143ZWW4, Q27731
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: January 23, 2007
    Last modified: June 2, 2021
    This is version 127 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
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