GCY_TOXGG
ID GCY_TOXGG Reviewed; 4367 AA.
AC S7VVK4;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Guanylate cyclase {ECO:0000303|PubMed:30449726};
DE Short=TgGC {ECO:0000303|PubMed:30449726};
DE EC=4.6.1.2 {ECO:0000305|PubMed:30742070, ECO:0000305|PubMed:30992368, ECO:0000305|PubMed:31235476};
DE AltName: Full=Guanylyl cyclase {ECO:0000305};
DE AltName: Full=TgATPaseP-GC {ECO:0000303|PubMed:31235476};
GN Name=GC {ECO:0000303|PubMed:30449726};
GN ORFNames=TGGT1_254370 {ECO:0000312|EMBL:EPR59074.1};
OS Toxoplasma gondii (strain ATCC 50853 / GT1).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=507601 {ECO:0000312|Proteomes:UP000005641};
RN [1] {ECO:0000312|Proteomes:UP000005641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50853 / GT1 {ECO:0000312|Proteomes:UP000005641};
RA Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA Roos D., Caler E., Lorenzi H.;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 2-LYS--ASP-2699; ASP-782; 2700-MET--SER-4367 AND GLU-2987.
RC STRAIN=RH {ECO:0000269|PubMed:30449726};
RX PubMed=30449726; DOI=10.1016/j.chom.2018.10.015;
RA Brown K.M., Sibley L.D.;
RT "Essential cGMP Signaling in Toxoplasma Is Initiated by a Hybrid P-Type
RT ATPase-Guanylate Cyclase.";
RL Cell Host Microbe 24:804-816.e6(2018).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=RH {ECO:0000269|PubMed:30992368};
RX PubMed=30992368; DOI=10.1074/jbc.ra118.005491;
RA Yang L., Uboldi A.D., Seizova S., Wilde M.L., Coffey M.J., Katris N.J.,
RA Yamaryo-Botte Y., Kocan M., Bathgate R.A.D., Stewart R.J., McConville M.J.,
RA Thompson P.E., Botte C.Y., Tonkin C.J.;
RT "An apically located hybrid guanylate cyclase-ATPase is critical for the
RT initiation of Ca2+ signaling and motility in Toxoplasma gondii.";
RL J. Biol. Chem. 294:8959-8972(2019).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP DOMAIN, TOPOLOGY, AND DISRUPTION PHENOTYPE.
RC STRAIN=RH {ECO:0000269|PubMed:31235476};
RX PubMed=31235476; DOI=10.26508/lsa.201900402;
RA Guenay-Esiyok O., Scheib U., Noll M., Gupta N.;
RT "An unusual and vital protein with guanylate cyclase and P4-ATPase domains
RT in a pathogenic protist.";
RL Life. Sci Alliance 2:0-0(2019).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CDC50.1 AND UGO, SUBCELLULAR
RP LOCATION, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-782.
RC STRAIN=RH {ECO:0000269|PubMed:30742070};
RX PubMed=30742070; DOI=10.1038/s41564-018-0339-8;
RA Bisio H., Lunghi M., Brochet M., Soldati-Favre D.;
RT "Phosphatidic acid governs natural egress in Toxoplasma gondii via a
RT guanylate cyclase receptor platform.";
RL Nat. Microbiol. 4:420-428(2019).
CC -!- FUNCTION: Catalyzes the synthesis of the second messenger cGMP from GTP
CC (PubMed:30992368, PubMed:31235476, PubMed:30742070). During the
CC tachyzoite lytic growth cycle in host cells, detects and transduces
CC environmental changes in potassium, phosphatidic acid and pH levels
CC (PubMed:31235476, PubMed:30992368). By producing cGMP in response to
CC these environmental changes, activates PKG and thereby regulates PKG-
CC dependent microneme secretion which is essential for tachyzoite
CC motility, host cell attachment invasion of and egress from host cells
CC (PubMed:30449726, PubMed:30992368, PubMed:31235476, PubMed:30742070).
CC May play a role in the fission of connected tachyzoites at their basal
CC pole during egress (PubMed:30742070). Does not display flippase
CC activity towards phosphatidylserine, phosphatidic acid or
CC phosphatidylcholine (PubMed:30742070). {ECO:0000269|PubMed:30449726,
CC ECO:0000269|PubMed:30742070, ECO:0000269|PubMed:30992368,
CC ECO:0000269|PubMed:31235476}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC Evidence={ECO:0000305|PubMed:30742070, ECO:0000305|PubMed:30992368,
CC ECO:0000305|PubMed:31235476};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8IDA0};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8IDA0};
CC Note=Binds 2 magnesium ions per subunit (By similarity). Is also active
CC with manganese (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:P30803, ECO:0000250|UniProtKB:Q8IDA0};
CC -!- SUBUNIT: Interacts with chaperone CDC50.1; the interaction regulates
CC guanylate cyclase GC trafficking and sensing environmental changes
CC (PubMed:30742070). Interacts with UGO; the interaction regulates
CC guanylate cyclase GC trafficking and catalytic activity
CC (PubMed:30742070). {ECO:0000269|PubMed:30742070}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30449726,
CC ECO:0000269|PubMed:30742070, ECO:0000269|PubMed:30992368,
CC ECO:0000269|PubMed:31235476}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to the apical cap in extracellular
CC tachyzoites (PubMed:30449726, PubMed:30992368). During tachyzoite
CC intracellular replication in the host cell, localizes to the apical
CC cap, to the cytoplasm in disperse foci and to the residual body
CC (PubMed:30992368, PubMed:31235476, PubMed:30742070).
CC {ECO:0000269|PubMed:30449726, ECO:0000269|PubMed:30742070,
CC ECO:0000269|PubMed:30992368, ECO:0000269|PubMed:31235476}.
CC -!- DEVELOPMENTAL STAGE: Expressed in tachyzoites.
CC {ECO:0000269|PubMed:31235476}.
CC -!- DOMAIN: The P-type ATPase-like domain is required for GC apical
CC localization and microneme secretion in tachyzoites (PubMed:30449726).
CC May act as a sensor for external changes in ionic conditions such as
CC potassium or pH levels (Probable). May act as a sensor for vacuolar
CC changes in phosphatidic acid or pH levels (Probable). Does not display
CC flippase activity towards phosphatidylserine, phosphatidic acid or
CC phosphatidylcholine (PubMed:30742070). {ECO:0000269|PubMed:30449726,
CC ECO:0000269|PubMed:30742070, ECO:0000305|PubMed:30742070,
CC ECO:0000305|PubMed:31235476}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout in tachyzoites blocks lytic
CC parasite growth in host cells (PubMed:30449726, PubMed:30992368,
CC PubMed:31235476, PubMed:30742070). Reduces tachyzoite attachment to
CC host cell (PubMed:30449726, PubMed:30992368). Prevents invasion of and
CC egress from host cells without affecting tachyzoite replication inside
CC the host cell (PubMed:30449726, PubMed:30992368, PubMed:31235476,
CC PubMed:30742070). Impairs tachyzoite gliding motility (PubMed:30449726,
CC PubMed:30992368, PubMed:31235476). Impairs stimulated microneme
CC secretion without affecting basal microneme secretion or dense granule
CC protein secretion (PubMed:30449726, PubMed:30992368, PubMed:30742070).
CC cGMP production is reduced (PubMed:30992368, PubMed:31235476). cGMP
CC production and microneme secretion is impaired in response to
CC phosphatidic acid (PubMed:30742070). Increase in cytoplasmic Ca(2+)
CC levels in response to a decrease in extracellular potassium levels or
CC in pH is impaired (PubMed:30992368). Basal phosphatidic acid levels are
CC reduced (PubMed:30992368). Infection of mice with knockout parasites
CC (strain ME49) does not cause lethal toxoplasmosis; mice show severe
CC reduction in parasite burden and have no detectable cyst formation in
CC tissues (PubMed:30449726). {ECO:0000269|PubMed:30449726,
CC ECO:0000269|PubMed:30742070, ECO:0000269|PubMed:30992368,
CC ECO:0000269|PubMed:31235476}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the cation transport
CC ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the adenylyl cyclase
CC class-4/guanylyl cyclase family. {ECO:0000305}.
CC -!- CAUTION: The guanylate cyclase domains 1 and 2 lack catalytic activity
CC when expressed on their own or in combination.
CC {ECO:0000269|PubMed:31235476}.
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DR EMBL; AAQM03000244; EPR59074.1; -; Genomic_DNA.
DR EnsemblProtists; EPR59074; EPR59074; TGGT1_254370.
DR VEuPathDB; ToxoDB:TGGT1_254370; -.
DR Proteomes; UP000005641; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035865; P:cellular response to potassium ion; IMP:UniProtKB.
DR GO; GO:0006182; P:cGMP biosynthetic process; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:2000147; P:positive regulation of cell motility; IMP:UniProtKB.
DR GO; GO:1903307; P:positive regulation of regulated secretory pathway; IMP:UniProtKB.
DR GO; GO:0010447; P:response to acidic pH; IMP:UniProtKB.
DR GO; GO:0075293; P:response to host pH environment; IMP:UniProtKB.
DR CDD; cd07302; CHD; 2.
DR Gene3D; 3.30.70.1230; -; 2.
DR Gene3D; 3.40.1110.10; -; 2.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; SSF55073; 2.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 1: Evidence at protein level;
KW Cell membrane; cGMP biosynthesis; Hydrolase; Lyase; Magnesium; Membrane;
KW Metal-binding; Transmembrane; Transmembrane helix.
FT CHAIN 1..4367
FT /note="Guanylate cyclase"
FT /id="PRO_0000452808"
FT TOPO_DOM 1..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..174
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..452
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..2258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2259..2279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2280..2289
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2290..2310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2311..2343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2344..2364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2365..2376
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2377..2397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2398..2408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2409..2429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2430..2444
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2445..2465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2466..2724
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2725..2745
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2746..2762
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2763..2783
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2784..2785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2786..2806
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2807..2823
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2824..2844
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2845..2858
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2859..2879
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2880..2903
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2904..2924
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2925..3693
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3694..3714
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3715..3736
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 3737..3757
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3758..3772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3773..3793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3794..3895
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 3896..3916
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3917..3921
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3922..3942
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3943..3950
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 3951..3971
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3972..4367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31235476"
FT DOMAIN 2942..3150
FT /note="Guanylate cyclase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT DOMAIN 4024..4159
FT /note="Guanylate cyclase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1607..1652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1773..1861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1881..1946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3214..3245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3359..3402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3456..3475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3485..3508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3523..3596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3620..3653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4292..4367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1047
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1524..1546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1775..1794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1805..1821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1884..1922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3219..3243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3359..3374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3385..3401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3524..3546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3554..3568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3632..3646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4321..4346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 4029
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 4029
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 4030
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 4073
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 4073
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT MUTAGEN 2..2699
FT /note="Missing: Stimulated microneme secretion is partially
FT reduced. Complete loss of parasite lytic growth. Loss of
FT apical localization."
FT /evidence="ECO:0000269|PubMed:30449726"
FT MUTAGEN 782
FT /note="D->A: Loss of basal microneme secretion but
FT stimulated microneme secretion is only partially reduced.
FT Complete loss of parasite lytic growth. No effect on apical
FT localization."
FT /evidence="ECO:0000269|PubMed:30449726"
FT MUTAGEN 782
FT /note="D->E: Lethal in tachyzoites."
FT /evidence="ECO:0000269|PubMed:30742070"
FT MUTAGEN 2700..4367
FT /note="Missing: Loss of basal and stimulated microneme
FT secretion. Complete loss of parasite lytic growth. No
FT effect on apical localization."
FT /evidence="ECO:0000269|PubMed:30449726"
FT MUTAGEN 2987
FT /note="E->A: Loss of basal and stimulated microneme
FT secretion. Complete loss of parasite lytic growth. No
FT effect on apical localization."
FT /evidence="ECO:0000269|PubMed:30449726"
SQ SEQUENCE 4367 AA; 477084 MW; 3F8D239D1B22ED99 CRC64;
MKKTRTTAAE RSQRARKRPH DEHRGRGREH GGARDPGAGG QAMKGAEKGR NPKHQATQKQ
MSFLQGKHQQ RVGNVVSRLG PAAVGQTTLM DKKRKLYSDT SQQPLWSLRK ITINPTDKDD
LRRFPSNAIY THRYSAMTFI FKNLWEQFHR VINWWFLVMA IIQAIPQLHY NPNHAWSTAL
PFAIVLVFGM LKDAFTDLGR RERDRVLNQR VCCIVDGHTP QLRLLQWQGV RVGNILRLTD
GEEVPADIVV LATSNTDGVA YVETSKLDGE TNLKFKQGVK ETRGESSPLS IAGIRGRVVC
EKPCAVMDAF TGSLKLDAHP RATPLDIVNF IQRGSHIRNT EWLYGVVIYT GEDTRIQKNA
APPGFKRPHI EKDINTYLFI SFFIVFLTIL ISVMSKWSVQ ERDSGDTGVT DAGASSGSGS
SSGETSQTYG SSVEFMLGSR DLLQNPWMSI LRFLAVYAPV LPLSLPLILD VVYLLQSVLI
EGDIHIRGGG RTPATGRGNG STSSMTVADD GLPDGEAGGL DSAHSSQNAS LQQPLSIVSK
GFSKTRRFLS EKFSSPSSGQ IGGNQDRRET PREDDERETN GENVPSATPL LPGGEAACVA
TGDEETLRAD AEGAQERDRE AEGNREQLKS VPTGTHAAWR PGALDSTAEA NEDEDPDVLH
AEKASGFGAR RSDDRDRKSS CSRYPETGGE KTSHAISGRF TGSVMPSTYT KLHGDIANAG
FESAWQPYAN GHTHTRTLLL ATGGGPNSLC ATGNFEREDV WAEVHTPALN PNLGQVDFIF
TDKTGTITEN DMTFSMCSVA GKIYGMASCG GAGYEGAESS EYGSRVWTAN ETSARSSRDR
LVPHLQRGTS AASSRSQSAP ASANDEGTPR RIPTLMLRPQ TLTNQQTGQQ SPVLPASRED
EKGKDASPGA ADSPASSLSV SRFFGSVSYE GRLEETGSQK EEDSRSDRVS LSPSEGRVSG
SRPQLACEGI HGATLRRRTV GIQSQHSSQS LLSSRQQSED ERQYTEGEEG ETEDDRSTVS
RRGRDRMYSR DYHRESRSSS PRDGELSDRY PLRCIRSIGD GYIIRGGRTG NVVMRHPSGM
SFDSRPSSQF TFSSPVVGDD SFDDPRRAMY FGRGSPRSLT PPSERGTASP SVGEEGPPLS
PQISPTGSAR GRVPRSSSLY MPAVDEGEDR ERYFRPRRRM LRPGASLLPP LSPSPSRAGV
PFLYDNIDFP TGFRETPMEG QIRRNCDFYD ASIFTDLARK DLRSHRINEF IKCMALCNTV
VPWVYTATPC SSSCPGLPST ANFSVAAYPT GGGANSLFSC SASAFAGPVT QGFPSVTHPA
ALASDGAAGA DEDEEKNVSQ LLLPSGTSAS SGAPSGPRGD PQLVSLLGRQ GQGHGSLGAP
GSGLPTSGCL GGAGGSGARG PMGLHGSRRS LPGSSDCRVP STARPAPLLG SDAAGRGFGP
DYVPSPRPLS PAGPPNASTG SLGEAPKADK PASPEEAASP GKDGEEAPSS TPRCVFAPST
LVPPSVLRSH TGAGGLRPSK SLARGVSFKE KHEEFAFSKD EDTATVDQDD TQSATDEEHD
VEGEEEEAGK SAERLTKAKR NRSASASLMS LKSKVTASGR DVADLLFRRG SRGNSGTDPD
PASARTVGRS SSVERAQQPP THGGFSTVTG TGESRSSLVS IIKYQASSPD EECLVSAASH
MGYTLVSRTN NYAILNINGQ ERRWQIIGVN EFTQKRGRMS IVVRPQEWTE GSILYVKGAD
VAMLDLLSTS FTRGHDFRQS FSCLSRYAES FSGGRGPQVS LSRLQSNSSA KGSGGPPVRR
SVSGSDPRLQ PSRSVSLPRT VPPGQETPMA GDQLEGPEAA ETVNPSGQTY SQGEEEEGLR
SRLARADSML RSLNPALYNY DKQHQRGHGP EGDEGSHELE GHDAHTGDSH GGHHRDQAEP
RAGDAVGPES ASRLPQKTQN RLPQHLGNAG VCAHGHAWTP SEENYCAAFF DDDEDELIAL
GDIALVEQHL KRFSLQGLRT MALACRYLTQ EETETYKRLY TDACASVYCR AERLEEVAED
MERDLEYLGI TGVRDKLQEQ VPETLQLMME AGIRVWMVTG DNVEYALHIC HSCRLLTSRT
RIFHAALEFS GRKAKREGVM LYELFRKARR LKRSDEHICL VVTGPNLRTF LNHPDLQTYF
LNMACCSDVV VAARVTPSQK AEMVRLVKKR LTPQPITMAV GDGGNDVAML QEAHVGVAIR
GKDSAAAVAA AYADYSFTEF RFLQRLLFVH GRLSLMRVST VILWSFFKSL CIGLPTFLFQ
PQAFWSAVEV YDPLLLMIVD FFWTTLPGII HGYSDQDLPT HLLPSVPVLY TPGRRRLYFN
GFRFILWTVE GIIYSFLIFY LLQATWMDGN TFHDGQVLGF HSYGILLLFG SLLQSNVRII
LETSLWTPTF LFTTIVLCTI MFFPTVLLYS VTGWPRRYME LAGRVVFAWP MLYFLIPLWV
SIGILVQLLL QVFTSSLFPN ISGSVKQYLA QKQADVNYRR KASKHPFSQP RPRLLPGGHD
EYGLFCGMGS CWSLFKRSLW FMGGCCLMDT PNVADDFTAS PALCAELRER FNPLRRKSVA
DRLPPPRRFR INENFLSYTG ASEEKGADGV QRDLGGKGSA CGPGAAGLAA GTGAPGAGRS
KSVFGGGGGV MPMADMAADL ETENSLSSNG SEQEKAGDNV TKLVKVSHLI NRFTLRFKDM
QLEADYQIHN KKSFLKRLVP WYRVIFMLIA LYQLLSFLTE YFIDIHWNPG ETEMEPWMCV
PTLVVEIGFA AVVVCTFYDF IFLDHFSLIL NSIVFLMVSS SIVFYTASHV DGTLTSVLFP
VFTFVILRIS FLQAVVWNIL FLIVTVARFM LDKKYLPPLN FVHYIPLFIG IDVFVAFVGY
RLEYNQRKSF LLDYSVDASR RKQREILNTM LPSFVVDQMI NSELNEEGIP TSLKAEDRGT
VSVIFCDVYE FQHVVASIEP TRLVEVLDSL FLCFDRSAEQ FGCTKIETVF ETYLAAAGLQ
PGREASPASY QQDACDALDM ALAMLEVAAQ IRYEVKSNQG VLSGSAVGSS SAVGPAVSAS
NLEASGNHME PRLSLHGHNS GVAMGSRMNS SRFHRQKTGS VVRTVLQSRP QRIRVKIGIH
SGRVISGVVG AKKPQYALFG DTVNTASRMK TTGQPGYIHI SEDSYELVKG DDTLEYESRH
TEVKGKGLMN TYLLVRVKGS PYPHFDDQEA DEGDVISETG GQNGESRRST ASLPRQLETA
GASSGVHTGE AMGCFASVGS RGESQTAADA AAAEAIEEDI QVEIDEEGVV EDTVEKAVED
VRRLRNEGSH AVASDDFPVS QAGAAQPRRC SRFLFQNAEE HGAAEPQRGE GARLILSPGQ
TEGTRQSEKE GSALGSNIAA SARADRRPAG RREDSRGDSR FDYESMTTQQ LLRIYRRQQK
VAKVLQWIDE ELRGQRDTAH RHARTADIVA KLLASSGDEQ AAGESSEADH DEVPLDEIKE
ELRRQAREAN EQESAKRSGG DAPPHTPTRK ALLKAFRSEI VHGCAAPTEE EKTAKEGRES
EVALASPETE SRDANGQRVS ERDASDAREG SASPQPDHAA PPSGLPQGLK GQETEKQQGW
KLFRSASLVR AAGQSFASLF RRRKPAAPSE AASPSSADTP MDSRVSPTSV DDEDLEQNRV
TRIGVSSEWL LLKFKDKNLE ARYRTHFYNN KSNINTIEQA LIIFLVTFCV QTLTRLALPR
FYVVCSHHTI NLHVCTGLYW AVRATYTLAA FVLWMLFHYR NRKEVATCLE LRWMVFLLNL
LFISASCVFA LSNSWGVCGQ QQEDHGASET AVENTLVALS HLAKDGSFPA DDAEVNSVAG
SPLAQAMHSP FTTAGVSRAS RMLRSGGVSV SGGTDCTGVG TSGEEGSDLV TANGRAYTYW
LLSDTIELFF YIVILHHNTG LLFQNCILVD VLLMTMSLTF IITTARETAS TVSTIATFPC
YVFFNLVSAY CKEYIDRLTF YVNEHAKTTE SRATQLLNDM LPKQVLEEFQ QDKLKLAYLH
ENVTFLFADI CGFTSWAKGV DACEVVTMLQ KLFAKFDKDS TKFGLYKLCT IGDAYVAVSE
PVTAENAQDT DPREGMWLVY EMAKAMIGNI TEVRERLCIP NLNMRIGLHY GSCVGGVIGS
GRLRYDLWGM DVLTGNMMES NGVPGKINVS EILKNEMEKG FPGEFVFKFN KTVAVLQSTV
DSYLIRPAKD FDEDEELAAA AATMAVAGPS ASLQQGGGAI PQVQAVASGL RRDATSIRGN
YRRRFTILGS APRVLGRRQS LRGHQFSALA LASHGDSGPS DEPRHLGDEG QAAGSVTSHD
GPLREEVEDD EIDGLKQLRK EIERAGGLGL DASPSDIGST PGSALGS
