KGP_TOXGO
ID KGP_TOXGO Reviewed; 994 AA.
AC Q8MMZ7; Q8MMP4;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=cGMP-dependent protein kinase {ECO:0000303|PubMed:11897122};
DE EC=2.7.11.12 {ECO:0000269|PubMed:11897122, ECO:0000269|PubMed:12455981};
DE AltName: Full=TgPKG {ECO:0000303|PubMed:11897122};
GN Name=PKG {ECO:0000303|PubMed:11897122};
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811 {ECO:0000312|EMBL:AAM20901.1};
RN [1] {ECO:0000312|EMBL:AAM20901.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11834729; DOI=10.1074/jbc.m108393200;
RA Gurnett A., Liberator P.A., Dulski P., Salowe S.P., Donald R.G.K.,
RA Anderson J.W., Wiltsie J., Diaz-Saldana C.A., Harris G., Chang B.,
RA Darkin-Rattray S.J., Nare B., Crumley T., Blum P., Misura A., Tamas T.,
RA Sardana M., Yuan J., Biftu T., Schmatz D.;
RT "Purification and molecular characterization of cGMP-dependent protein
RT kinase from Apicomplexan parasites. A novel chemotherapeutic target.";
RL J. Biol. Chem. 277:15913-15922(2002).
RN [2] {ECO:0000312|EMBL:AAM20901.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), DEVELOPMENTAL STAGE,
RP MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-4, AND MUTAGENESIS OF MET-1;
RP GLY-2; CYS-4; MET-103; ARG-263; ARG-382 AND ARG-635.
RC STRAIN=RH {ECO:0000303|PubMed:11897122};
RX PubMed=11897122; DOI=10.1016/s0166-6851(01)00451-0;
RA Donald R.G., Liberator P.A.;
RT "Molecular characterization of a coccidian parasite cGMP dependent protein
RT kinase.";
RL Mol. Biochem. Parasitol. 120:165-175(2002).
RN [3] {ECO:0000312|EMBL:AAM27174.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF THR-761.
RC STRAIN=RH {ECO:0000312|EMBL:AAM27174.1};
RX PubMed=12455981; DOI=10.1128/ec.1.3.317-328.2002;
RA Donald R.G., Allocco J., Singh S.B., Nare B., Salowe S.P., Wiltsie J.,
RA Liberator P.A.;
RT "Toxoplasma gondii cyclic GMP-dependent kinase: chemotherapeutic targeting
RT of an essential parasite protein kinase.";
RL Eukaryot. Cell 1:317-328(2002).
RN [4] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF THR-761.
RX PubMed=26933037; DOI=10.1074/jbc.m115.700518;
RA Brown K.M., Lourido S., Sibley L.D.;
RT "Serum Albumin Stimulates Protein Kinase G-dependent Microneme Secretion in
RT Toxoplasma gondii.";
RL J. Biol. Chem. 291:9554-9565(2016).
RN [5] {ECO:0000305}
RP FUNCTION (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION (ISOFORMS 1 AND 2),
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE (ISOFORMS 1 AND 2).
RX PubMed=28465425; DOI=10.1128/mbio.00375-17;
RA Brown K.M., Long S., Sibley L.D.;
RT "Plasma Membrane Association by N-Acylation Governs PKG Function in
RT Toxoplasma gondii.";
RL MBio 8:0-0(2017).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=30753127; DOI=10.7554/elife.42669;
RA Tosetti N., Dos Santos Pacheco N., Soldati-Favre D., Jacot D.;
RT "Three F-actin assembly centers regulate organelle inheritance, cell-cell
RT communication and motility in Toxoplasma gondii.";
RL Elife 8:0-0(2019).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, 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).
CC -!- FUNCTION: Serine/threonine protein kinase which acts as a downstream
CC effector of the second messenger cGMP (PubMed:11897122,
CC PubMed:12455981). Plays an essential role in tachyzoite invasion of and
CC egress from host cells (PubMed:28465425, PubMed:30753127,
CC PubMed:31235476). During invasion of host cells, regulates the apico-
CC basal flux of F-actin probably via Ca(2+)-mediated activation of CDPK1
CC (PubMed:30753127). In tachyzoites, required for microneme secretion
CC (PubMed:26933037, PubMed:28465425). Required for tachyzoite gliding
CC motility (PubMed:31235476). {ECO:0000269|PubMed:11897122,
CC ECO:0000269|PubMed:12455981, ECO:0000269|PubMed:26933037,
CC ECO:0000269|PubMed:28465425, ECO:0000269|PubMed:30753127,
CC ECO:0000269|PubMed:31235476}.
CC -!- FUNCTION: [Isoform 1]: Plays an essential role in parasite invasion of
CC and egress from host cells, and microneme secretion.
CC {ECO:0000269|PubMed:28465425}.
CC -!- FUNCTION: [Isoform 2]: Dispensable for parasite invasion of and egress
CC from host cells, and microneme secretion.
CC {ECO:0000269|PubMed:28465425}.
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=2.7.11.12;
CC Evidence={ECO:0000269|PubMed:11897122, ECO:0000269|PubMed:12455981};
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=2.7.11.12; Evidence={ECO:0000269|PubMed:11897122,
CC ECO:0000269|PubMed:12455981};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11897122};
CC -!- ACTIVITY REGULATION: Activated by cGMP (PubMed:11897122,
CC PubMed:12455981). The cGMP-binding domains acts cooperatively to
CC activate PKG (PubMed:11897122, PubMed:12455981). Inhibited by the
CC antiparasitic small molecule 4-[2-(4-fluorophenyl)-5-(1-
CC methylpiperidine-4-yl)-1Hpyrrol- 3-yl]pyridine (compound 1)
CC (PubMed:11897122, PubMed:12455981). {ECO:0000269|PubMed:11897122,
CC ECO:0000269|PubMed:12455981}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.3 uM for ATP {ECO:0000269|PubMed:11897122,
CC ECO:0000269|PubMed:12455981};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31235476}. Membrane
CC {ECO:0000269|PubMed:31235476}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:11834729, ECO:0000269|PubMed:28465425}; Lipid-
CC anchor {ECO:0000269|PubMed:11897122}. Note=Membrane localization is
CC essential to regulate parasite invasion, egress and microneme
CC secretion. {ECO:0000269|PubMed:28465425}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:11897122, ECO:0000269|PubMed:28465425}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=Isoform I {ECO:0000303|PubMed:11897122};
CC IsoId=Q8MMZ7-1; Sequence=Displayed;
CC Name=2; Synonyms=Isoform II {ECO:0000303|PubMed:11897122};
CC IsoId=Q8MMZ7-2; Sequence=VSP_060899;
CC -!- DEVELOPMENTAL STAGE: Expressed in tachyzoites (at protein level).
CC {ECO:0000269|PubMed:11897122, ECO:0000269|PubMed:12455981,
CC ECO:0000269|PubMed:28465425}.
CC -!- DISRUPTION PHENOTYPE: Knockout in tachyzoites is lethal
CC (PubMed:12455981). Conditional knockout in tachyzoites impairs lytic
CC growth in host cells (PubMed:28465425, PubMed:31235476). However,
CC parasite intracellular replication is only slightly affected
CC (PubMed:31235476). Impaired microneme secretion, motility and, invasion
CC of and egress from host cells (PubMed:28465425, PubMed:31235476).
CC {ECO:0000269|PubMed:12455981, ECO:0000269|PubMed:28465425,
CC ECO:0000269|PubMed:31235476}.
CC -!- DISRUPTION PHENOTYPE: [Isoform 1]: Impaired growth in host cells
CC (PubMed:28465425). Impaired microneme secretion and, invasion of and
CC egress from host cells (PubMed:28465425).
CC {ECO:0000269|PubMed:28465425}.
CC -!- DISRUPTION PHENOTYPE: [Isoform 2]: Normal growth in host cells
CC (PubMed:28465425). Microneme secretion and, invasion of and egress from
CC host cells are partially impaired (PubMed:28465425).
CC {ECO:0000269|PubMed:28465425}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cGMP subfamily. {ECO:0000305}.
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DR EMBL; AF413570; AAM20901.1; -; mRNA.
DR EMBL; AF448496; AAM27174.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8MMZ7; -.
DR SMR; Q8MMZ7; -.
DR VEuPathDB; ToxoDB:TGARI_311360A; -.
DR VEuPathDB; ToxoDB:TGARI_311360B; -.
DR VEuPathDB; ToxoDB:TGCAST_311300; -.
DR VEuPathDB; ToxoDB:TGCAST_311360A; -.
DR VEuPathDB; ToxoDB:TGCAST_311360B; -.
DR VEuPathDB; ToxoDB:TGCOUG_311360A; -.
DR VEuPathDB; ToxoDB:TGCOUG_311360B; -.
DR VEuPathDB; ToxoDB:TGDOM2_286470; -.
DR VEuPathDB; ToxoDB:TGDOM2_311300; -.
DR VEuPathDB; ToxoDB:TGDOM2_311360A; -.
DR VEuPathDB; ToxoDB:TGFOU_311360B; -.
DR VEuPathDB; ToxoDB:TGFOU_311360C; -.
DR VEuPathDB; ToxoDB:TGFOU_311360D; -.
DR VEuPathDB; ToxoDB:TGGT1_311360; -.
DR VEuPathDB; ToxoDB:TGMAS_311300; -.
DR VEuPathDB; ToxoDB:TGMAS_311360A; -.
DR VEuPathDB; ToxoDB:TGMAS_311360C; -.
DR VEuPathDB; ToxoDB:TGME49_311360; -.
DR VEuPathDB; ToxoDB:TGP89_242070; -.
DR VEuPathDB; ToxoDB:TGP89_311360A; -.
DR VEuPathDB; ToxoDB:TGP89_311360C; -.
DR VEuPathDB; ToxoDB:TGPRC2_311360A; -.
DR VEuPathDB; ToxoDB:TGPRC2_311360B; -.
DR VEuPathDB; ToxoDB:TGRH88_050830; -.
DR VEuPathDB; ToxoDB:TGRUB_242070B; -.
DR VEuPathDB; ToxoDB:TGRUB_311360A; -.
DR VEuPathDB; ToxoDB:TGRUB_311360C; -.
DR VEuPathDB; ToxoDB:TGVAND_311360A; -.
DR VEuPathDB; ToxoDB:TGVAND_311360B; -.
DR VEuPathDB; ToxoDB:TGVEG_311360; -.
DR BRENDA; 2.7.11.12; 6411.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030553; F:cGMP binding; IDA:UniProtKB.
DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:2000147; P:positive regulation of cell motility; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR CDD; cd00038; CAP_ED; 4.
DR CDD; cd05572; STKc_cGK; 1.
DR Gene3D; 2.60.120.10; -; 4.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR035014; STKc_cGK.
DR Pfam; PF00027; cNMP_binding; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00100; cNMP; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; SSF51206; 4.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 3.
DR PROSITE; PS50042; CNMP_BINDING_3; 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; Cell membrane; cGMP; cGMP-binding;
KW Cytoplasm; Kinase; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Myristate; Nucleotide-binding; Palmitate; Serine/threonine-protein kinase;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:11897122"
FT CHAIN 2..994
FT /note="cGMP-dependent protein kinase"
FT /id="PRO_0000452025"
FT DOMAIN 684..941
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 942..994
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..305
FT /note="cNMP-binding domain 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT REGION 308..407
FT /note="cNMP-binding domain 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT REGION 463..539
FT /note="cNMP-binding domain 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT REGION 561..660
FT /note="cNMP-binding domain 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT REGION 954..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 807
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 253
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 254
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 256
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 263
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 264
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 616
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 625
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 626
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 628
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 635
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 636
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 690..698
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 713
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:11897122"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:11897122"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_060899"
FT MUTAGEN 1
FT /note="M->A: Loss of isoform 1 expression."
FT /evidence="ECO:0000269|PubMed:11897122"
FT MUTAGEN 2
FT /note="G->A: Loss of membrane localization."
FT /evidence="ECO:0000269|PubMed:11897122"
FT MUTAGEN 2
FT /note="Missing: Loss of myristoylation and palmitoylation.
FT Loss of membrane localization."
FT /evidence="ECO:0000269|PubMed:11897122"
FT MUTAGEN 4
FT /note="C->S: Partial loss of myristoylation. Loss of
FT palmitoylation. Partial loss of membrane localization."
FT /evidence="ECO:0000269|PubMed:11897122"
FT MUTAGEN 103
FT /note="M->A: Loss of isoform 2 expression."
FT /evidence="ECO:0000269|PubMed:11897122"
FT MUTAGEN 263
FT /note="R->A: 16% reduction in catalytic activity. 64% and
FT 87% reduction in catalytic activity respectively; when
FT associated with A-382 or A-635. Complete loss of catalytic
FT activity; when associated with A-382 and A-635."
FT /evidence="ECO:0000269|PubMed:11897122"
FT MUTAGEN 382
FT /note="R->A: 28% reduction in catalytic activity. 64%
FT reduction in catalytic activity; when associated with A-
FT 263. Complete loss of catalytic activity; when associated
FT with A-263 and A-635."
FT /evidence="ECO:0000269|PubMed:11897122"
FT MUTAGEN 635
FT /note="R->A: 77% reduction in catalytic activity. 87%
FT reduction in catalytic activity; when associated with A-
FT 263. Complete loss of catalytic activity; when associated
FT with A-263 and A-382."
FT /evidence="ECO:0000269|PubMed:11897122"
FT MUTAGEN 761
FT /note="T->M,Q: No effect on catalytic activity. No effect
FT on virulence in mouse host. No effect on microneme
FT secretion. Reduces sensitivity to antiparasitic inhibitor
FT compound 1."
FT /evidence="ECO:0000269|PubMed:12455981,
FT ECO:0000269|PubMed:26933037"
FT CONFLICT 118
FT /note="P -> L (in Ref. 3; AAM27174)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 994 AA; 111255 MW; A1B605605713E296 CRC64;
MGACISKNSS ARVSRSSALS ASKQTVAASA PPGAAGDETS ATGAAEEASR NSLARVDGTR
ASAAELERAP DGVCPDREEP GTANAEQGGV TEKKDTRETL AGMNSPKTLE AEAQEDDPKR
EAPNQDVPSE APEGPKEKPG GDRKPAQKAI LKQDDSHTEE EKLNAHLAYR EKTPADFALI
QDSLKANLVC SSLNEGEIDA LAVAMQFFTF KKGDVVTKQG EPGSYFFIIH SGTFDVLVND
KRVNAMDKGK AFGEIALIHN TERSATVVAS STEGALWGVQ RHTFRETLKQ LSSRNFAENR
QFLASVKFFE MLTEAQKNVI TNALVVENFK PGQPIVKEGD AGDVLYILKS GKAKVSIGGR
EIRMLRKGDY FGERALLYKE PRSATITAEE FTVCVSIGRE LLDRVLGNLQ HVLFRNIMVE
ALQQSKVYEL FQGDQLSKLI EAAVVKDYGA DYVILDKENK TKGIRFFFVL EGELSVYAYT
QNPATKEEER KLAATLKRGQ AFGEEYVLNP TRPFNHYVKS VGPCKLALFT SSVLTATLGG
EDIDETLDFN NKRAIIRKMY IFRYLSDHQM TMLIKAFKTV RYMSGEYIIK EGERGTRFFI
IKAGEVAILK NNKRLRTLGR HDYFGERALL YDKPRTASVC ANSAGVDLWV VDKSVFNEII
KGPMLAHLEE RIRMQDTKVE FQDLQVVRVV GRGTFGTVKL VRHVPTDIRY ALKCVSRRSV
IALSQQQHIR LEREIMAEND HPFIIRLVRT FRDKEFLYFL TELVTGGELY DAIRKLGLLA
RSQAQFYLAS IVLAIEYLHE RNIAYRDLKP ENILLDSQGY VKLIDFGCAK KMQGRAYTLV
GTPHYMAPEV ILGKGYTLTA DTWAFGVCLY EFMCGPLPFG NDAEDQLEIF RDILTGKLVF
PHYVTDQDAI NLMKRLLCRL PEVRIGCSIN GYKDIKEHAF FGDFDWDKLA GRGLPPPLAP
KGETYAEDTE QSSFELDEDD TIVLEDEYDW DKDF
