P3C2B_HUMAN
ID P3C2B_HUMAN Reviewed; 1634 AA.
AC O00750; O95666; Q5SW99;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta;
DE Short=PI3K-C2-beta;
DE Short=PtdIns-3-kinase C2 subunit beta;
DE EC=2.7.1.137 {ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11533253, ECO:0000269|PubMed:9830063};
DE EC=2.7.1.154 {ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9830063};
DE AltName: Full=C2-PI3K;
DE AltName: Full=Phosphoinositide 3-kinase-C2-beta;
GN Name=PIK3C2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Mammary gland;
RX PubMed=9144573; DOI=10.1006/bbrc.1997.6495;
RA Brown R.A., Ho L.K.F., Weber-Hall S.J., Shipley J.M., Fry M.J.;
RT "Identification and cDNA cloning of a novel mammalian C2 domain-containing
RT phosphoinositide 3-kinase, HsC2-PI3K.";
RL Biochem. Biophys. Res. Commun. 233:537-544(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND COFACTOR.
RC TISSUE=Monocyte;
RX PubMed=9830063; DOI=10.1074/jbc.273.49.33082;
RA Arcaro A., Volinia S., Zvelebil M.J., Stein R.C., Watton S.J., Layton M.J.,
RA Gout I., Ahmadi K., Downward J., Waterfield M.D.;
RT "Human phosphoinositide 3-kinase C2beta, the role of calcium and the C2
RT domain in enzyme activity.";
RL J. Biol. Chem. 273:33082-33090(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP IDENTIFICATION IN A COMPLEX WITH ERBB2 AND EGFR, INTERACTION WITH EGFR AND
RP PDGFR, COFACTOR, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10805725; DOI=10.1128/mcb.20.11.3817-3830.2000;
RA Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D.,
RA Domin J.;
RT "Class II phosphoinositide 3-kinases are downstream targets of activated
RT polypeptide growth factor receptors.";
RL Mol. Cell. Biol. 20:3817-3830(2000).
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH GRB2 AND EGFR, INTERACTION WITH GRB2,
RP ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11533253; DOI=10.1128/mcb.21.19.6660-6667.2001;
RA Wheeler M., Domin J.;
RT "Recruitment of the class II phosphoinositide 3-kinase C2beta to the
RT epidermal growth factor receptor: role of Grb2.";
RL Mol. Cell. Biol. 21:6660-6667(2001).
RN [6]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=14563213; DOI=10.1186/1472-6890-3-4;
RA El Sheikh S.S., Domin J., Tomtitchong P., Abel P., Stamp G., Lalani E.-N.;
RT "Topographical expression of class IA and class II phosphoinositide 3-
RT kinase enzymes in normal human tissues is consistent with a role in
RT differentiation.";
RL BMC Clin. Pathol. 3:4-4(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC -!- FUNCTION: Phosphorylates PtdIns and PtdIns4P with a preference for
CC PtdIns (PubMed:10805725, PubMed:9830063, PubMed:11533253). Does not
CC phosphorylate PtdIns(4,5)P2 (PubMed:9830063). May be involved in EGF
CC and PDGF signaling cascades (PubMed:10805725).
CC {ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11533253,
CC ECO:0000269|PubMed:9830063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154;
CC Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9830063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374;
CC Evidence={ECO:0000305|PubMed:9830063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000269|PubMed:10805725,
CC ECO:0000269|PubMed:11533253, ECO:0000269|PubMed:9830063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000305|PubMed:9830063};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9830063};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9830063};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10805725};
CC -!- ACTIVITY REGULATION: Activated by GRB2. {ECO:0000269|PubMed:11533253}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 uM for ATP-Mg(2+) {ECO:0000269|PubMed:9830063};
CC KM=120 uM for ATP-Ca(2+) {ECO:0000269|PubMed:9830063};
CC Vmax=737 nmol/min/mg enzyme for ATP-Mg(2+)
CC {ECO:0000269|PubMed:9830063};
CC Vmax=737 nmol/min/mg enzyme for ATP-Ca(2+)
CC {ECO:0000269|PubMed:9830063};
CC -!- SUBUNIT: Part of a complex with ERBB2 and EGFR. Part of a complex with
CC phosphorylated EGFR and GRB2. Interacts with phosphorylated EGFR and
CC PDGFR, maybe indirectly. Interacts with GRB2.
CC {ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11533253}.
CC -!- INTERACTION:
CC O00750; P00533: EGFR; NbExp=10; IntAct=EBI-641107, EBI-297353;
CC O00750; P04626: ERBB2; NbExp=2; IntAct=EBI-641107, EBI-641062;
CC O00750; P62993: GRB2; NbExp=5; IntAct=EBI-641107, EBI-401755;
CC O00750; P16333: NCK1; NbExp=3; IntAct=EBI-641107, EBI-389883;
CC O00750; P14373: TRIM27; NbExp=5; IntAct=EBI-641107, EBI-719493;
CC O00750; P63104: YWHAZ; NbExp=2; IntAct=EBI-641107, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:14563213,
CC ECO:0000269|PubMed:9830063}. Cell membrane
CC {ECO:0000269|PubMed:14563213, ECO:0000269|PubMed:9830063}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:14563213, ECO:0000269|PubMed:9830063}.
CC Nucleus {ECO:0000269|PubMed:14563213}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:14563213}. Note=Found mostly in the microsome, but
CC also in the plasma membrane and cytosol. Nuclear in testis.
CC -!- TISSUE SPECIFICITY: Expressed in columnar and transitional epithelia,
CC mononuclear cells, and ganglion cells (at protein level). Widely
CC expressed, with highest levels in thymus and placenta and lowest in
CC peripheral blood, skeletal muscle and kidney.
CC {ECO:0000269|PubMed:14563213, ECO:0000269|PubMed:9144573}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00879, ECO:0000255|PROSITE-ProRule:PRU00880}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-26 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA74194.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y11312; CAA72168.1; -; mRNA.
DR EMBL; Y13892; CAA74194.1; ALT_INIT; mRNA.
DR EMBL; AL606489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS1446.1; -.
DR PIR; JC5500; JC5500.
DR PIR; PC4346; PC4346.
DR RefSeq; NP_002637.3; NM_002646.3.
DR RefSeq; XP_005245314.1; XM_005245257.2.
DR RefSeq; XP_011507932.1; XM_011509630.2.
DR RefSeq; XP_011507933.1; XM_011509631.2.
DR RefSeq; XP_016856962.1; XM_017001473.1.
DR RefSeq; XP_016856963.1; XM_017001474.1.
DR AlphaFoldDB; O00750; -.
DR SMR; O00750; -.
DR BioGRID; 111305; 42.
DR CORUM; O00750; -.
DR IntAct; O00750; 29.
DR MINT; O00750; -.
DR STRING; 9606.ENSP00000356155; -.
DR BindingDB; O00750; -.
DR ChEMBL; CHEMBL5554; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; O00750; -.
DR GuidetoPHARMACOLOGY; 2151; -.
DR SwissLipids; SLP:000000893; -.
DR CarbonylDB; O00750; -.
DR iPTMnet; O00750; -.
DR PhosphoSitePlus; O00750; -.
DR BioMuta; PIK3C2B; -.
DR EPD; O00750; -.
DR jPOST; O00750; -.
DR MassIVE; O00750; -.
DR MaxQB; O00750; -.
DR PaxDb; O00750; -.
DR PeptideAtlas; O00750; -.
DR PRIDE; O00750; -.
DR ProteomicsDB; 48017; -.
DR Antibodypedia; 34558; 237 antibodies from 30 providers.
DR DNASU; 5287; -.
DR Ensembl; ENST00000367187.7; ENSP00000356155.3; ENSG00000133056.14.
DR Ensembl; ENST00000684373.1; ENSP00000507222.1; ENSG00000133056.14.
DR GeneID; 5287; -.
DR KEGG; hsa:5287; -.
DR MANE-Select; ENST00000684373.1; ENSP00000507222.1; NM_001377334.1; NP_001364263.1.
DR UCSC; uc001haw.4; human.
DR CTD; 5287; -.
DR DisGeNET; 5287; -.
DR GeneCards; PIK3C2B; -.
DR HGNC; HGNC:8972; PIK3C2B.
DR HPA; ENSG00000133056; Tissue enhanced (brain).
DR MIM; 602838; gene.
DR neXtProt; NX_O00750; -.
DR OpenTargets; ENSG00000133056; -.
DR PharmGKB; PA33305; -.
DR VEuPathDB; HostDB:ENSG00000133056; -.
DR eggNOG; KOG0905; Eukaryota.
DR GeneTree; ENSGT00940000158263; -.
DR HOGENOM; CLU_002191_0_0_1; -.
DR InParanoid; O00750; -.
DR OMA; YVWSAVN; -.
DR OrthoDB; 204282at2759; -.
DR PhylomeDB; O00750; -.
DR TreeFam; TF102031; -.
DR BioCyc; MetaCyc:HS05725-MON; -.
DR BRENDA; 2.7.1.137; 2681.
DR BRENDA; 2.7.1.154; 2681.
DR PathwayCommons; O00750; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR SignaLink; O00750; -.
DR SIGNOR; O00750; -.
DR BioGRID-ORCS; 5287; 10 hits in 1075 CRISPR screens.
DR ChiTaRS; PIK3C2B; human.
DR GeneWiki; PIK3C2B; -.
DR GenomeRNAi; 5287; -.
DR Pharos; O00750; Tchem.
DR PRO; PR:O00750; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O00750; protein.
DR Bgee; ENSG00000133056; Expressed in pancreatic ductal cell and 207 other tissues.
DR ExpressionAtlas; O00750; baseline and differential.
DR Genevisible; O00750; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IDA:UniProtKB.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0001727; F:lipid kinase activity; IEA:Ensembl.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:1905037; P:autophagosome organization; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
DR CDD; cd07290; PX_PI3K_C2_beta; 1.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR042134; PX_PI3K_C2_beta.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cytoplasm; Endoplasmic reticulum; Kinase;
KW Lipid metabolism; Membrane; Microsome; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..1634
FT /note="Phosphatidylinositol 4-phosphate 3-kinase C2 domain-
FT containing subunit beta"
FT /id="PRO_0000088798"
FT DOMAIN 375..463
FT /note="PI3K-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00879"
FT DOMAIN 635..786
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041,
FT ECO:0000255|PROSITE-ProRule:PRU00880"
FT DOMAIN 805..981
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 1050..1328
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 1365..1481
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 1504..1624
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 2..298
FT /note="Interaction with GRB2"
FT /evidence="ECO:0000269|PubMed:11533253"
FT REGION 45..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1062
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1192..1200
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1211..1237
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 87..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 6
FT /note="G -> D (in Ref. 1; CAA72168)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="P -> S (in Ref. 2; CAA74194)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="R -> W (in Ref. 2; CAA74194)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="Q -> L (in Ref. 2; CAA74194)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="A -> V (in Ref. 1; CAA72168)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="K -> E (in Ref. 2; CAA74194)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="P -> S (in Ref. 2; CAA74194)"
FT /evidence="ECO:0000305"
FT CONFLICT 664..665
FT /note="EL -> DM (in Ref. 1; CAA72168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1634 AA; 184768 MW; CA817BA77C12E833 CRC64;
MSSTQGNGEH WKSLESVGIS RKELAMAEAL QMEYDALSRL RHDKEENRAK QNADPSLISW
DEPGVDFYSK PAGRRTDLKL LRGLSGSDPT LNYNSLSPQE GPPNHSTSQG PQPGSDPWPK
GSLSGDYLYI FDGSDGGVSS SPGPGDIEGS CKKLSPPPLP PRASIWDTPP LPPRKGSPSS
SKISQPSDIN TFSLVEQLPG KLLEHRILEE EEVLGGGGQG RLLGSVDYDG INDAITRLNL
KSTYDAEMLR DATRGWKEGR GPLDFSKDTS GKPVARSKTM PPQVPPRTYA SRYGNRKNAT
PGKNRRISAA PVGSRPHTVA NGHELFEVSE ERDEEVAAFC HMLDILRSGS DIQDYFLTGY
VWSAVTPSPE HLGDEVNLKV TVLCDRLQEA LTFTCNCSST VDLLIYQTLC YTHDDLRNVD
VGDFVLKPCG LEEFLQNKHA LGSHEYIQYC RKFDIDIRLQ LMEQKVVRSD LARTVNDDQS
PSTLNYLVHL QERPVKQTIS RQALSLLFDT YHNEVDAFLL ADGDFPLKAD RVVQSVKAIC
NALAAVETPE ITSALNQLPP CPSRMQPKIQ KDPSVLAVRE NREKVVEALT AAILDLVELY
CNTFNADFQT AVPGSRKHDL VQEACHFARS LAFTVYATHR IPIIWATSYE DFYLSCSLSH
GGKELCSPLQ TRRAHFSKYL FHLIVWDQQI CFPVQVNRLP RETLLCATLY ALPIPPPGSS
SEANKQRRVP EALGWVTTPL FNFRQVLTCG RKLLGLWPAT QENPSARWSA PNFHQPDSVI
LQIDFPTSAF DIKFTSPPGD KFSPRYEFGS LREEDQRKLK DIMQKESLYW LTDADKKRLW
EKRYYCHSEV SSLPLVLASA PSWEWACLPD IYVLLKQWTH MNHQDALGLL HATFPDQEVR
RMAVQWIGSL SDAELLDYLP QLVQALKYEC YLDSPLVRFL LKRAVSDLRV THYFFWLLKD
GLKDSQFSIR YQYLLAALLC CCGKGLREEF NRQCWLVNAL AKLAQQVREA APSARQGILR
TGLEEVKQFF ALNGSCRLPL SPSLLVKGIV PRDCSYFNSN AVPLKLSFQN VDPLGENIRV
IFKCGDDLRQ DMLTLQMIRI MSKIWVQEGL DMRMVIFRCF STGRGRGMVE MIPNAETLRK
IQVEHGVTGS FKDRPLADWL QKHNPGEDEY EKAVENFIYS CAGCCVATYV LGICDRHNDN
IMLKTTGHMF HIDFGRFLGH AQMFGNIKRD RAPFVFTSDM AYVINGGDKP SSRFHDFVDL
CCQAYNLIRK HTHLFLNLLG LMLSCGIPEL SDLEDLKYVY DALRPQDTEA NATTYFTRLI
ESSLGSVATK LNFFIHNLAQ MKFTGSDDRL TLSFASRTHT LKSSGRISDV FLCRHEKIFH
PNKGYIYVVK VMRENTHEAT YIQRTFEEFQ ELHNKLRLLF PSSHLPSFPS RFVIGRSRGE
AVAERRREEL NGYIWHLIHA PPEVAECDLV YTFFHPLPRD EKAMGTSPAP KSSDGTWARP
VGKVGGEVKL SISYKNNKLF IMVMHIRGLQ LLQDGNDPDP YVKIYLLPDP QKTTKRKTKV
ARKTCNPTYN EMLVYDGIPK GDLQQRELQL SVLSEQGFWE NVLLGEVNIR LRELDLAQEK
TGWFALGSRS HGTL
