CDPK4_PLABA
ID CDPK4_PLABA Reviewed; 528 AA.
AC P62345; A0A509AH59;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Calcium-dependent protein kinase 4 {ECO:0000303|PubMed:15137943};
DE EC=2.7.11.1 {ECO:0000269|PubMed:15137943};
DE AltName: Full=PbCDPK4 {ECO:0000303|PubMed:27425827};
GN Name=CDPK4 {ECO:0000303|PubMed:15137943}; Synonyms=CPK4 {ECO:0000305};
GN ORFNames=PBANKA_0615200 {ECO:0000312|EMBL:VUC54827.1};
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823 {ECO:0000312|Proteomes:UP000074855};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, DEVELOPMENTAL STAGE, AND AUTOPHOSPHORYLATION.
RX PubMed=15137943; DOI=10.1016/s0092-8674(04)00449-0;
RA Billker O., Dechamps S., Tewari R., Wenig G., Franke-Fayard B.,
RA Brinkmann V.;
RT "Calcium and a calcium-dependent protein kinase regulate gamete formation
RT and mosquito transmission in a malaria parasite.";
RL Cell 117:503-514(2004).
RN [2] {ECO:0000312|Proteomes:UP000074855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANKA {ECO:0000312|Proteomes:UP000074855};
RX PubMed=25359557; DOI=10.1186/s12915-014-0086-0;
RA Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA Janse C.J.;
RT "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT expression.";
RL BMC Biol. 12:86-86(2014).
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=27425827; DOI=10.1111/mmi.13466;
RA Govindasamy K., Jebiwott S., Jaijyan D.K., Davidow A., Ojo K.K.,
RA Van Voorhis W.C., Brochet M., Billker O., Bhanot P.;
RT "Invasion of hepatocytes by Plasmodium sporozoites requires cGMP-dependent
RT protein kinase and calcium dependent protein kinase 4.";
RL Mol. Microbiol. 102:349-363(2016).
RN [4]
RP FUNCTION, INTERACTION WITH THE MCM COMPLEX, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MYRISTOYLATION AT GLY-2, AND
RP MUTAGENESIS OF GLY-2; MET-57 AND SER-147.
RX PubMed=28481199; DOI=10.7554/elife.26524;
RA Fang H., Klages N., Baechler B., Hillner E., Yu L., Pardo M., Choudhary J.,
RA Brochet M.;
RT "Multiple short windows of calcium-dependent protein kinase 4 activity
RT coordinate distinct cell cycle events during Plasmodium gametogenesis.";
RL Elife 6:0-0(2017).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=30315162; DOI=10.1038/s41467-018-06733-w;
RA Fang H., Gomes A.R., Klages N., Pino P., Maco B., Walker E.M.,
RA Zenonos Z.A., Angrisano F., Baum J., Doerig C., Baker D.A., Billker O.,
RA Brochet M.;
RT "Epistasis studies reveal redundancy among calcium-dependent protein
RT kinases in motility and invasion of malaria parasites.";
RL Nat. Commun. 9:4248-4248(2018).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF SER-147.
RX PubMed=32866196; DOI=10.1371/journal.ppat.1008131;
RA Govindasamy K., Bhanot P.;
RT "Overlapping and distinct roles of CDPK family members in the pre-
RT erythrocytic stages of the rodent malaria parasite, Plasmodium berghei.";
RL PLoS Pathog. 16:e1008131-e1008131(2020).
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 (PubMed:15137943). Plays a central role in
CC the host erythrocytes and hepatocytes infection cycles, sexual
CC reproduction and mosquito transmission of the parasite
CC (PubMed:15137943, PubMed:27425827, PubMed:28481199, PubMed:30315162,
CC PubMed:32866196). During the liver stage, involved in sporozoite
CC motility and thus in sporozoite invasion of host hepatocytes, probably
CC together with CDPK1 and CDPK5 (PubMed:27425827, PubMed:32866196).
CC Involved in merosome egress from host hepatocytes, probably together
CC with CDPK5 (PubMed:32866196). During the asexual blood stage, involved
CC in merozoite invasion of host erythrocytes and motility by stabilizing
CC the inner membrane complex, a structure below the plasma membrane which
CC acts as an anchor for the glidosome, an acto-myosin motor
CC (PubMed:30315162). Required for cell cycle progression in the male
CC gametocyte (PubMed:15137943, PubMed:28481199, PubMed:30315162). During
CC male gametogenesis in the mosquito gut, required to initiate the first
CC round of DNA replication, probably by facilitating the assembly of the
CC pre-replicative MCM complex, to assemble the first mitotic spindle and,
CC at the end of gametogenesis, to initiate axoneme motility, cytokinesis
CC and subsequent exflagellation (PubMed:28481199). For each of these
CC steps, may phosphorylate SOC1, SOC2 and SOC3, respectively
CC (PubMed:28481199). Together with CDPK1, regulates ookinete gliding in
CC the mosquito host midgut (PubMed:30315162).
CC {ECO:0000269|PubMed:15137943, ECO:0000269|PubMed:27425827,
CC ECO:0000269|PubMed:28481199, ECO:0000269|PubMed:30315162,
CC ECO:0000269|PubMed:32866196}.
CC -!- FUNCTION: [Isoform 1]: During male gametogenesis in the mosquito gut,
CC required to initiate the first round of DNA replication, probably by
CC facilitating the assembly of the pre-replicative MCM complex, and to
CC assemble the first mitotic spindle. {ECO:0000269|PubMed:28481199}.
CC -!- FUNCTION: [Isoform 2]: At the end of male gametogenesis in the mosquito
CC gut, required to initiate axoneme motility, cytokinesis and subsequent
CC exflagellation. {ECO:0000269|PubMed:28481199}.
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:0000269|PubMed:15137943};
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:0000269|PubMed:15137943};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8IBS5};
CC -!- ACTIVITY REGULATION: Activated by calcium (PubMed:15137943). Upon
CC calcium binding to the EF-hand domains, the C-terminus of the junction
CC domain (J domain) undergoes a conformational change which results in
CC the dissociation of the pseudo-substrate inhibitory motif from the
CC catalytic domain (By similarity). This, in turn, may facilitate the
CC autophosphorylation of the activation loop at Thr-234, which leads to
CC the kinase activation (By similarity). Intracellular calcium increase
CC is triggered by xanthurenic acid (XA), a small mosquito molecule that
CC induces the differentiation of specialized transmission stages, the
CC gametocytes, into male and female gametes (Probable). Activated by a
CC decrease in temperature (20 degrees Celsius) and an increase in pH
CC (7.6) occurring when the parasite is ingested by in the mosquito (By
CC similarity). {ECO:0000250|UniProtKB:Q8IBS5,
CC ECO:0000269|PubMed:15137943, ECO:0000305|PubMed:15137943}.
CC -!- SUBUNIT: May interact with the pre-replication MCM complex prior male
CC gametogenesis activation. {ECO:0000269|PubMed:28481199}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30315162}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:28481199}. Membrane {ECO:0000269|PubMed:28481199};
CC Lipid-anchor {ECO:0000269|PubMed:28481199}. Chromosome
CC {ECO:0000269|PubMed:28481199}. Note=A small fraction of the protein
CC localizes to membranes and to chromatin. {ECO:0000269|PubMed:28481199}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=large {ECO:0000303|PubMed:28481199};
CC IsoId=P62345-1; Sequence=Displayed;
CC Name=2; Synonyms=short {ECO:0000303|PubMed:28481199};
CC IsoId=P62345-2; Sequence=VSP_061065;
CC -!- DEVELOPMENTAL STAGE: Expressed in sporozoites and in liver stages (at
CC protein level) (PubMed:27425827). Highly expressed in male gametocytes
CC and exflagellated gametes, and to a lesser extent, in female
CC gametocytes (at protein level) (PubMed:15137943, PubMed:28481199).
CC Expressed in ookinetes (PubMed:15137943). Weakly or not expressed in
CC asexual parasite stages (PubMed:15137943).
CC {ECO:0000269|PubMed:15137943, ECO:0000269|PubMed:27425827,
CC ECO:0000269|PubMed:28481199}.
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:Q8IBS5}.
CC -!- PTM: [Isoform 1]: Myristoylated; myristoylation may target it to
CC different subcellular compartments (PubMed:28481199). During male
CC gametogenesis, myristoylation is required to initiate DNA replication
CC but not for mitotic spindle assembly or axoneme activation
CC (PubMed:28481199). {ECO:0000269|PubMed:28481199}.
CC -!- PTM: [Isoform 1]: Not palmitoylated. {ECO:0000269|PubMed:28481199}.
CC -!- PTM: May be autophosphorylated on Thr-234 in vitro.
CC {ECO:0000250|UniProtKB:Q8IBS5}.
CC -!- DISRUPTION PHENOTYPE: Host hepatocyte invasion is reduced in knockout
CC sporozoites; the few intracellular parasites develop and egress
CC normally (PubMed:27425827). In infected mice, formation of schizonts
CC and merozoite invasion of host erythrocytes are normal
CC (PubMed:30315162). In a PKG T622Q mutant background, reduces ring
CC formation and thus the number of schizonts (PubMed:30315162). In
CC addition, merozoites have a discontinuous inner membrane complex
CC (PubMed:30315162). Impaired exflagellation of male gametocytes which
CC fails to assemble the mitotic spindle and are arrested at the first
CC round of DNA replication (PubMed:28481199). In a PKG T622Q mutant
CC background, male gametocytes fail to exflagellate in the mosquito
CC vector (PubMed:30315162). {ECO:0000269|PubMed:27425827,
CC ECO:0000269|PubMed:28481199, ECO:0000269|PubMed:30315162}.
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; AY555067; AAS99650.1; -; mRNA.
DR EMBL; LK023121; VUC54827.1; -; Genomic_DNA.
DR RefSeq; XP_676632.1; XM_671540.1.
DR AlphaFoldDB; P62345; -.
DR SMR; P62345; -.
DR STRING; 5823.A0A509AH59; -.
DR VEuPathDB; PlasmoDB:PBANKA_0615200; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_4_1; -.
DR OMA; LEHEWIR; -.
DR Proteomes; UP000074855; Chromosome 6.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031224; C:intrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:1904931; F:MCM complex binding; IDA:UniProtKB.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0048232; P:male gamete generation; IMP:UniProtKB.
DR GO; GO:0140530; P:MCM complex loading; IMP:UniProtKB.
DR GO; GO:2000147; P:positive regulation of cell motility; IMP:UniProtKB.
DR GO; GO:0003353; P:positive regulation of cilium movement; IMP:UniProtKB.
DR GO; GO:0032298; P:positive regulation of DNA-templated DNA replication initiation; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Alternative initiation; ATP-binding; Calcium; Chromosome; Cytoplasm;
KW Developmental protein; Differentiation; Kinase; Lipoprotein; Magnesium;
KW Membrane; Metal-binding; Myristate; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:28481199"
FT CHAIN 2..528
FT /note="Calcium-dependent protein kinase 4"
FT /id="PRO_0000085841"
FT DOMAIN 70..328
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 376..411
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 423..458
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 459..494
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 498..528
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..386
FT /note="J domain"
FT /evidence="ECO:0000250|UniProtKB:Q8IBS5"
FT MOTIF 350..358
FT /note="J domain autoinhibitory motif"
FT /evidence="ECO:0000250|UniProtKB:Q8IBS5"
FT MOTIF 359..368
FT /note="J domain EF-hand interaction motif"
FT /evidence="ECO:0000250|UniProtKB:Q8IBS5"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 76..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 393
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 400
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 436
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 438
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 440
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 442
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 474
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 478
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 506
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 508
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
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 517
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:28481199"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_061065"
FT MUTAGEN 2
FT /note="G->A: Impaired exflagellation of male gametocytes
FT which are arrested at the first round of DNA replication.
FT Assembly of the mitotic spindle is normal. No effect on
FT CDPK4 localization; however, a minor CDPK4 population fails
FT to localize to the plasma membrane and to chromatin."
FT /evidence="ECO:0000269|PubMed:28481199"
FT MUTAGEN 57
FT /note="M->A: Loss of the short isoform. In male
FT gametocytes, DNA replication and axoneme assembly are
FT normal, but exflagellation is severely reduced."
FT /evidence="ECO:0000269|PubMed:28481199"
FT MUTAGEN 147
FT /note="S->M: No defect in male gametogenesis. No defect in
FT sporozoite infection of host hepatocytes. Severe reduction
FT in sensitivity to compound 1294 inhibition."
FT /evidence="ECO:0000269|PubMed:28481199,
FT ECO:0000269|PubMed:32866196"
SQ SEQUENCE 528 AA; 60590 MW; AC7E91D4316389C6 CRC64;
MGQEMSTQSD MQNENQKGNK RNLKGSQGKN GLKERSTSIS KEIVKNSFNN SKLRPGMFIQ
NSNVVFNEQY KGIKILGKGS FGEVILSKDK HTGHEYAIKV ISKKHVKRKT DKQSLLREVE
LLKMLDHINI MKLYEFFEDN NYYYLVSDVY SGGELFDEII SRKRFYEVDA ARIIKQVLSG
ITYMHKNNVV HRDLKPENIL LETKNKEDMI IKIIDFGLST HFEYSKKMKD KIGTAYYIAP
DVLHGTYDEK CDIWSCGVIL YILLSGCPPF NGSNEYDILK KVETGKYTFD LPQFKKISDK
AKDLIKKMLM YTSAVRISAR DALEHEWIRL MTSKDNVNID IPSLELSITN IKQFQSTQKL
AQAALLYMGS KLTTIDETKE LTKIFKKMDK NGDGQLDRNE LIIGYKELLK LKGDDTTDLD
NAAIEVEVDQ ILSSIDLDQN GYIEYSEFLT VAIDRKLLLS TERLEKAFKL FDKDGSGKIS
ANELAQLFGL GDVSSDCWKT VLKEVDQNND GEIDFKEFRD MLIKLCNY
