ID PK3CA_BOVIN Reviewed; 1068 AA. AC P32871; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 27-MAR-2024, entry version 189. DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform; DE Short=PI3-kinase subunit alpha; DE Short=PI3K-alpha; DE Short=PI3Kalpha; DE Short=PtdIns-3-kinase subunit alpha; DE EC=2.7.1.137 {ECO:0000269|PubMed:1322797, ECO:0000269|PubMed:14729945, ECO:0000305|PubMed:15178440}; DE EC=2.7.1.153 {ECO:0000250|UniProtKB:P42336}; DE AltName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha; DE Short=PtdIns-3-kinase subunit p110-alpha; DE Short=p110alpha; DE AltName: Full=Phosphoinositide-3-kinase catalytic alpha polypeptide; DE AltName: Full=Serine/threonine protein kinase PIK3CA; DE EC=2.7.11.1 {ECO:0000269|PubMed:14729945, ECO:0000269|PubMed:15178440}; GN Name=PIK3CA; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND RP CATALYTIC ACTIVITY. RC TISSUE=Brain; RX PubMed=1322797; DOI=10.1016/0092-8674(92)90166-a; RA Hiles I.D., Otsu M., Volinia S., Fry M.J., Gout I., Dhand R., Panayotou G., RA Ruiz-Larrea F., Thompson A., Totty N.F., Hsuan J.J., Courtneidge S.A., RA Parker P.J., Waterfield M.D.; RT "Phosphatidylinositol 3-kinase: structure and expression of the 110 kd RT catalytic subunit."; RL Cell 70:419-429(1992). RN [2] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=15178440; DOI=10.1016/j.bbrc.2004.04.191; RA Foukas L.C., Shepherd P.R.; RT "eIF4E binding protein 1 and H-Ras are novel substrates for the protein RT kinase activity of class-I phosphoinositide 3-kinase."; RL Biochem. Biophys. Res. Commun. 319:541-549(2004). RN [3] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=14729945; DOI=10.1128/mcb.24.3.966-975.2004; RA Foukas L.C., Beeton C.A., Jensen J., Phillips W.A., Shepherd P.R.; RT "Regulation of phosphoinositide 3-kinase by its intrinsic serine kinase RT activity in vivo."; RL Mol. Cell. Biol. 24:966-975(2004). CC -!- FUNCTION: Phosphoinositide-3-kinase (PI3K) phosphorylates CC phosphatidylinositol (PI) and its phosphorylated derivatives at CC position 3 of the inositol ring to produce 3-phosphoinositides CC (PubMed:1322797, PubMed:14729945). Uses ATP and PtdIns(4,5)P2 CC (phosphatidylinositol 4,5-bisphosphate) to generate CC phosphatidylinositol 3,4,5-trisphosphate (PIP3) (By similarity). PIP3 CC plays a key role by recruiting PH domain-containing proteins to the CC membrane, including AKT1 and PDPK1, activating signaling cascades CC involved in cell growth, survival, proliferation, motility and CC morphology. Participates in cellular signaling in response to various CC growth factors. Involved in the activation of AKT1 upon stimulation by CC receptor tyrosine kinases ligands such as EGF, insulin, IGF1, VEGFA and CC PDGF. Involved in signaling via insulin-receptor substrate (IRS) CC proteins. Essential in endothelial cell migration during vascular CC development through VEGFA signaling, possibly by regulating RhoA CC activity. Required for lymphatic vasculature development, possibly by CC binding to RAS and by activation by EGF and FGF2, but not by PDGF. CC Regulates invadopodia formation through the PDPK1-AKT1 pathway. CC Participates in cardiomyogenesis in embryonic stem cells through a AKT1 CC pathway. Participates in vasculogenesis in embryonic stem cells through CC PDK1 and protein kinase C pathway (By similarity). In addition to its CC lipid kinase activity, it displays a serine-protein kinase activity CC that results in the autophosphorylation of the p85alpha regulatory CC subunit as well as phosphorylation of other proteins such as 4EBP1, H- CC Ras, the IL-3 beta c receptor and possibly others (PubMed:15178440, CC PubMed:14729945). Plays a role in the positive regulation of CC phagocytosis and pinocytosis (By similarity). CC {ECO:0000250|UniProtKB:P42336, ECO:0000250|UniProtKB:P42337, CC ECO:0000269|PubMed:1322797, ECO:0000269|PubMed:14729945, CC ECO:0000269|PubMed:15178440}. 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:14729945, ECO:0000269|PubMed:15178440}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; CC Evidence={ECO:0000305|PubMed:14729945, ECO:0000305|PubMed:15178440}; 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:1322797, CC ECO:0000269|PubMed:14729945, ECO:0000305|PubMed:15178440}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710; CC Evidence={ECO:0000305|PubMed:1322797, ECO:0000305|PubMed:14729945, CC ECO:0000305|PubMed:15178440}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5- CC bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- CC inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:21292, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57836, CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.153; CC Evidence={ECO:0000250|UniProtKB:P42336}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21293; CC Evidence={ECO:0000250|UniProtKB:P42336}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5- CC bisphosphate) + ATP = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo- CC inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:55632, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:83416, CC ChEBI:CHEBI:83419, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:P42336}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55633; CC Evidence={ECO:0000250|UniProtKB:P42336}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero- CC 3-phospho-1D-myo-inositol 4,5-bisphosphate + ATP = 1-octadecanoyl-2- CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo- CC inositol 3,4,5-triphosphate) + ADP + H(+); Xref=Rhea:RHEA:43396, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77137, CC ChEBI:CHEBI:83243, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:P42336}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43397; CC Evidence={ECO:0000250|UniProtKB:P42336}; CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate CC biosynthesis. {ECO:0000305|PubMed:1322797, ECO:0000305|PubMed:14729945, CC ECO:0000305|PubMed:15178440}. CC -!- SUBUNIT: Heterodimer of a catalytic subunit PIK3CA and a p85 regulatory CC subunit (PIK3R1, PIK3R2 or PIK3R3). Interacts with IRS1 in nuclear CC extracts. Interacts with RUFY3. Interacts with RASD2. Interacts with CC APPL1. Interacts with HRAS and KRAS. Interaction with HRAS/KRAS is CC required for PI3K pathway signaling and cell proliferation stimulated CC by EGF and FGF2. Interacts with FAM83B; activates the PI3K/AKT CC signaling cascade. {ECO:0000250|UniProtKB:P42336, CC ECO:0000250|UniProtKB:P42337}. CC -!- INTERACTION: CC P32871; P23727: PIK3R1; NbExp=4; IntAct=EBI-1373130, EBI-520244; CC P32871; P23726: PIK3R2; NbExp=3; IntAct=EBI-1373130, EBI-1555978; CC -!- DOMAIN: The PI3K-ABD domain and the PI3K-RBD domain interact with the CC PI3K/PI4K kinase domain. The C2 PI3K-type domain may facilitate the CC recruitment to the plasma membrane. The inhibitory interactions with CC PIK3R1 are mediated by the PI3K-ABD domain and the C2 PI3K-type domain CC with the iSH2 (inter-SH2) region of PIK3R1, and the C2 PI3K-type CC domain, the PI3K helical domain, and the PI3K/PI4K kinase domain with CC the nSH2 (N-terminal SH2) region of PIK3R1. CC {ECO:0000250|UniProtKB:P42336}. CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE- CC ProRule:PRU00877, ECO:0000255|PROSITE-ProRule:PRU00879, CC ECO:0000255|PROSITE-ProRule:PRU00880}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M93252; AAA30698.1; -; mRNA. DR PIR; A43322; A43322. DR RefSeq; NP_776999.1; NM_174574.1. DR PDB; 2V1Y; X-ray; 2.40 A; A=1-108. DR PDBsum; 2V1Y; -. DR AlphaFoldDB; P32871; -. DR SMR; P32871; -. DR CORUM; P32871; -. DR DIP; DIP-39319N; -. DR IntAct; P32871; 4. DR STRING; 9913.ENSBTAP00000068953; -. DR BindingDB; P32871; -. DR ChEMBL; CHEMBL2498; -. DR iPTMnet; P32871; -. DR PaxDb; 9913-ENSBTAP00000012168; -. DR Ensembl; ENSBTAT00000012168.6; ENSBTAP00000012168.5; ENSBTAG00000009232.6. DR Ensembl; ENSBTAT00000072391.1; ENSBTAP00000068953.1; ENSBTAG00000009232.6. DR GeneID; 282306; -. DR KEGG; bta:282306; -. DR CTD; 5290; -. DR VEuPathDB; HostDB:ENSBTAG00000009232; -. DR VGNC; VGNC:32889; PIK3CA. DR eggNOG; KOG0904; Eukaryota. DR GeneTree; ENSGT00940000155531; -. DR HOGENOM; CLU_002191_1_1_1; -. DR InParanoid; P32871; -. DR OMA; WSEWLNY; -. DR OrthoDB; 10350at2759; -. DR TreeFam; TF102031; -. DR BRENDA; 2.7.1.137; 908. DR Reactome; R-BTA-109704; PI3K Cascade. DR Reactome; R-BTA-112399; IRS-mediated signalling. DR Reactome; R-BTA-114604; GPVI-mediated activation cascade. DR Reactome; R-BTA-1250342; PI3K events in ERBB4 signaling. DR Reactome; R-BTA-1257604; PIP3 activates AKT signaling. DR Reactome; R-BTA-1433557; Signaling by SCF-KIT. DR Reactome; R-BTA-1660499; Synthesis of PIPs at the plasma membrane. DR Reactome; R-BTA-180292; GAB1 signalosome. DR Reactome; R-BTA-186763; Downstream signal transduction. DR Reactome; R-BTA-1963642; PI3K events in ERBB2 signaling. DR Reactome; R-BTA-198203; PI3K/AKT activation. DR Reactome; R-BTA-201556; Signaling by ALK. DR Reactome; R-BTA-202424; Downstream TCR signaling. DR Reactome; R-BTA-2029485; Role of phospholipids in phagocytosis. DR Reactome; R-BTA-210993; Tie2 Signaling. DR Reactome; R-BTA-2424491; DAP12 signaling. DR Reactome; R-BTA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization. DR Reactome; R-BTA-388841; Costimulation by the CD28 family. DR Reactome; R-BTA-389357; CD28 dependent PI3K/Akt signaling. DR Reactome; R-BTA-416476; G alpha (q) signalling events. DR Reactome; R-BTA-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-BTA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling. DR Reactome; R-BTA-5654689; PI-3K cascade:FGFR1. DR Reactome; R-BTA-5654695; PI-3K cascade:FGFR2. DR Reactome; R-BTA-5654710; PI-3K cascade:FGFR3. DR Reactome; R-BTA-5654720; PI-3K cascade:FGFR4. DR Reactome; R-BTA-5673001; RAF/MAP kinase cascade. DR Reactome; R-BTA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR Reactome; R-BTA-8851907; MET activates PI3K/AKT signaling. DR Reactome; R-BTA-8853659; RET signaling. DR Reactome; R-BTA-9009391; Extra-nuclear estrogen signaling. DR Reactome; R-BTA-9013149; RAC1 GTPase cycle. DR Reactome; R-BTA-9013404; RAC2 GTPase cycle. DR Reactome; R-BTA-9027276; Erythropoietin activates Phosphoinositide-3-kinase (PI3K). DR Reactome; R-BTA-912526; Interleukin receptor SHC signaling. DR Reactome; R-BTA-912631; Regulation of signaling by CBL. DR Reactome; R-BTA-9607240; FLT3 Signaling. DR SABIO-RK; P32871; -. DR UniPathway; UPA00220; -. DR EvolutionaryTrace; P32871; -. DR PRO; PR:P32871; -. DR Proteomes; UP000009136; Chromosome 1. DR Bgee; ENSBTAG00000009232; Expressed in neutrophil and 113 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl. DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:BHF-UCL. DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IDA:BHF-UCL. DR GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; IBA:GO_Central. DR GO; GO:0005944; C:phosphatidylinositol 3-kinase complex, class IB; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IDA:BHF-UCL. DR GO; GO:0046934; F:1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC. DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0043560; F:insulin receptor substrate binding; IEA:Ensembl. DR GO; GO:0030295; F:protein kinase activator activity; IEA:Ensembl. 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:0030036; P:actin cytoskeleton organization; IEA:Ensembl. DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl. DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0141068; P:autosome genomic imprinting; IEA:Ensembl. DR GO; GO:0086003; P:cardiac muscle cell contraction; IEA:Ensembl. DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl. DR GO; GO:0071464; P:cellular response to hydrostatic pressure; IEA:Ensembl. DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl. DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl. DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl. DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; IEA:Ensembl. DR GO; GO:2000811; P:negative regulation of anoikis; IEA:Ensembl. DR GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IEA:Ensembl. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:BHF-UCL. DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:BHF-UCL. DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IDA:BHF-UCL. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:BHF-UCL. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:1905477; P:positive regulation of protein localization to membrane; IEA:Ensembl. DR GO; GO:0043457; P:regulation of cellular respiration; IEA:Ensembl. DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl. DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:0055119; P:relaxation of cardiac muscle; IEA:Ensembl. DR GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl. DR GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; IEA:Ensembl. DR CDD; cd08398; C2_PI3K_class_I_alpha; 1. DR CDD; cd00872; PI3Ka_I; 1. DR CDD; cd05175; PI3Kc_IA_alpha; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1. DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1. DR InterPro; IPR016024; ARM-type_fold. 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; IPR003113; PI3K_ABD. DR InterPro; IPR001263; PI3K_accessory_dom. DR InterPro; IPR042236; PI3K_accessory_sf. DR InterPro; IPR000341; PI3K_Ras-bd_dom. DR InterPro; IPR037704; PI3Kalpha_dom. DR InterPro; IPR015433; PI_Kinase. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR10048:SF107; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT ALPHA ISOFORM; 1. DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1. DR Pfam; PF00454; PI3_PI4_kinase; 1. DR Pfam; PF00792; PI3K_C2; 1. DR Pfam; PF02192; PI3K_p85B; 1. DR Pfam; PF00794; PI3K_rbd; 1. DR Pfam; PF00613; PI3Ka; 1. DR SMART; SM00142; PI3K_C2; 1. DR SMART; SM00143; PI3K_p85B; 1. DR SMART; SM00144; PI3K_rbd; 1. DR SMART; SM00145; PI3Ka; 1. DR SMART; SM00146; PI3Kc; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF54236; Ubiquitin-like; 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; PS51544; PI3K_ABD; 1. DR PROSITE; PS51546; PI3K_RBD; 1. DR PROSITE; PS51545; PIK_HELICAL; 1. PE 1: Evidence at protein level; KW 3D-structure; Angiogenesis; ATP-binding; Direct protein sequencing; Kinase; KW Nucleotide-binding; Phagocytosis; Proto-oncogene; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..1068 FT /note="Phosphatidylinositol 4,5-bisphosphate 3-kinase FT catalytic subunit alpha isoform" FT /id="PRO_0000088784" FT DOMAIN 16..105 FT /note="PI3K-ABD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00877" FT DOMAIN 187..289 FT /note="PI3K-RBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00879" FT DOMAIN 330..487 FT /note="C2 PI3K-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00880" FT DOMAIN 517..694 FT /note="PIK helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878" FT DOMAIN 765..1051 FT /note="PI3K/PI4K catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 771..777 FT /note="G-loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 912..920 FT /note="Catalytic loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 931..957 FT /note="Activation loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT STRAND 18..25 FT /evidence="ECO:0007829|PDB:2V1Y" FT STRAND 31..37 FT /evidence="ECO:0007829|PDB:2V1Y" FT HELIX 42..52 FT /evidence="ECO:0007829|PDB:2V1Y" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:2V1Y" FT HELIX 59..61 FT /evidence="ECO:0007829|PDB:2V1Y" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:2V1Y" FT STRAND 69..74 FT /evidence="ECO:0007829|PDB:2V1Y" FT STRAND 79..82 FT /evidence="ECO:0007829|PDB:2V1Y" FT HELIX 89..91 FT /evidence="ECO:0007829|PDB:2V1Y" FT STRAND 94..102 FT /evidence="ECO:0007829|PDB:2V1Y" SQ SEQUENCE 1068 AA; 124328 MW; C753DCC2F39FDDF0 CRC64; MPPRPSSGEL WGIHLMPPRI LVECLLPNGM IVTLECLREA TLITIKHELF KEARKYPLHQ LLQDESSYIF VSVTQEAERE EFFDETRRLC DLRLFQPFLK VIEPVGNREE KILNREIGFA IGMPVCEFDM VKDPEVQDFR RNILNVCKEA VDLRDLNSPH SRAMYVYPPN VESSPELPKH IYNKLDKGQI IVVIWVIVSP NNDKQKYTLK INHDCVPEQV IAEAIRKKTR SMLLSSEQLK LCVLEYQGKY ILKVCGCDEY FLEKYPLSQY KYIRSCIMLG RMPNLMLMAK ESLYSQLPMD CFTMPSYSRR ISTATPYMNG ETSTKSLWVI NSALRIKILC ATYVNVNIRD IDKIYVRTGI YHGGEPLCDN VNTQRVPCSN PRWNEWLNYD IYIPDLPRAA RLCLSICSVK GRKGAKEEHC PLAWGNINLF DYTDTLVSGK MALNLWPVPH GLEDLLNPIG VTGSNPNKET PCLELEFDWF SSVVKFPDMS VIEEHANWSV SREAGFSYSH AGLSNRLARD NELRENDKEQ LRAICTRDPL SEITEQEKDF LWSHRHYCVT IPEILPKLLL SVKWNSRDEV AQMYCLVKDW PPIKPEQAME LLDCNYPDPM VRGFAVRCLE KYLTDDKLSQ YLIQLVQVLK YEQYLDNLLV RFLLKKALTN QRIGHFFFWH LKSEMHNKTV SQRFGLLLES YCRACGMYLK HLNRQVEAME KLINLTDILK QEKKDETQKV QMKFLVEQMR RPDFMDALQG FLSPLNPAHQ LGNLRLEECR IMSSAKRPLW LNWENPDIMS ELLFQNNEII FKNGDDLRQD MLTLQIIRIM ENIWQNQGLD LRMLPYGCLS IGDCVGLIEV VRNSHTIMQI QCKGGLKGAL QFNSHTLHQW LKDKNKGEIY DAAIDLFTRS CAGYCVATFI LGIGDRHNSN IMVKDDGQLF HIDFGHFLDH KKKKFGYKRE RVPFVLTQDF LIVISKGAQE CTKTREFERF QEMCYKAYLA IRQHANLFIN LFSMMLGSGM PELQSFDDIA YIRKTLALDK TEQEALEYFM KQMNDAHHGG WTTKMDWIFH TIKQHALN //