PK3CA_RAT
ID PK3CA_RAT Reviewed; 1068 AA.
AC A0A0G2K344;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform {ECO:0000312|RGD:620916};
DE Short=PI3-kinase subunit alpha {ECO:0000305};
DE Short=PI3K-alpha {ECO:0000305};
DE Short=PI3Kalpha {ECO:0000305};
DE Short=PtdIns-3-kinase subunit alpha {ECO:0000305};
DE EC=2.7.1.137 {ECO:0000250|UniProtKB:P42336};
DE EC=2.7.1.153 {ECO:0000250|UniProtKB:P42336};
DE AltName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha {ECO:0000305};
DE Short=PtdIns-3-kinase subunit p110-alpha {ECO:0000305};
DE Short=p110alpha {ECO:0000303|PubMed:20236230};
DE AltName: Full=Phosphoinositide-3-kinase catalytic alpha polypeptide {ECO:0000305};
DE AltName: Full=Serine/threonine protein kinase PIK3CA {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P32871};
GN Name=Pik3ca {ECO:0000312|RGD:620916};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000303|PubMed:20236230};
RX PubMed=20236230; DOI=10.1111/j.1365-2826.2010.01975.x;
RA Tups A., Anderson G.M., Rizwan M., Augustine R.A., Chaussade C.,
RA Shepherd P.R., Grattan D.R.;
RT "Both p110alpha and p110beta isoforms of phosphatidylinositol 3-OH-kinase
RT are required for insulin signalling in the hypothalamus.";
RL J. Neuroendocrinol. 22:534-542(2010).
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. Uses
CC ATP and PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to
CC generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a
CC key role by recruiting PH domain-containing proteins to the membrane,
CC including AKT1 and PDPK1, activating signaling cascades involved in
CC cell growth, survival, proliferation, motility and morphology.
CC Participates in cellular signaling in response to various growth
CC 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 (PubMed:20236230). Essential in endothelial cell migration
CC during vascular development through VEGFA signaling, possibly by
CC regulating RhoA activity. Required for lymphatic vasculature
CC development, possibly by binding to RAS and by activation by EGF and
CC FGF2, but not by PDGF. Regulates invadopodia formation through the
CC PDPK1-AKT1 pathway. Participates in cardiomyogenesis in embryonic stem
CC cells through a AKT1 pathway. Participates in vasculogenesis in
CC embryonic stem cells through PDK1 and protein kinase C pathway. In
CC addition to its lipid kinase activity, it displays a serine-protein
CC kinase activity that results in the autophosphorylation of the p85alpha
CC regulatory subunit as well as phosphorylation of other proteins such as
CC 4EBP1, H-Ras, the IL-3 beta c receptor and possibly others (By
CC similarity). Plays a role in the positive regulation of phagocytosis
CC and pinocytosis (By similarity). {ECO:0000250|UniProtKB:P42336,
CC ECO:0000250|UniProtKB:P42337, ECO:0000269|PubMed:20236230}.
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=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:0000250|UniProtKB:P42336};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000250|UniProtKB:P42336};
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:0000250|UniProtKB:P32871};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000250|UniProtKB:P32871};
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:0000250|UniProtKB:P42336}.
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 -!- TISSUE SPECIFICITY: Detected in the hypothalamus (at protein level).
CC {ECO:0000269|PubMed:20236230}.
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}.
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DR EMBL; AABR07009968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_596890.2; NM_133399.2.
DR AlphaFoldDB; A0A0G2K344; -.
DR SMR; A0A0G2K344; -.
DR IntAct; A0A0G2K344; 3.
DR STRING; 10116.ENSRNOP00000014527; -.
DR BindingDB; A0A0G2K344; -.
DR jPOST; A0A0G2K344; -.
DR PaxDb; A0A0G2K344; -.
DR Ensembl; ENSRNOT00000083720; ENSRNOP00000072496; ENSRNOG00000056371.
DR GeneID; 170911; -.
DR KEGG; rno:170911; -.
DR CTD; 5290; -.
DR RGD; 620916; Pik3ca.
DR eggNOG; KOG0904; Eukaryota.
DR GeneTree; ENSGT00940000155531; -.
DR OMA; EHANWTV; -.
DR OrthoDB; 204282at2759; -.
DR BRENDA; 2.7.1.153; 5301.
DR Reactome; R-RNO-109704; PI3K Cascade.
DR Reactome; R-RNO-112399; IRS-mediated signalling.
DR Reactome; R-RNO-114604; GPVI-mediated activation cascade.
DR Reactome; R-RNO-1250342; PI3K events in ERBB4 signaling.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-RNO-180292; GAB1 signalosome.
DR Reactome; R-RNO-186763; Downstream signal transduction.
DR Reactome; R-RNO-1963642; PI3K events in ERBB2 signaling.
DR Reactome; R-RNO-198203; PI3K/AKT activation.
DR Reactome; R-RNO-201556; Signaling by ALK.
DR Reactome; R-RNO-202424; Downstream TCR signaling.
DR Reactome; R-RNO-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-RNO-210993; Tie2 Signaling.
DR Reactome; R-RNO-2424491; DAP12 signaling.
DR Reactome; R-RNO-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-RNO-388841; Costimulation by the CD28 family.
DR Reactome; R-RNO-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-RNO-5654689; PI-3K cascade:FGFR1.
DR Reactome; R-RNO-5654695; PI-3K cascade:FGFR2.
DR Reactome; R-RNO-5654710; PI-3K cascade:FGFR3.
DR Reactome; R-RNO-5654720; PI-3K cascade:FGFR4.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-RNO-8851907; MET activates PI3K/AKT signaling.
DR Reactome; R-RNO-8853659; RET signaling.
DR Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9027276; Erythropoietin activates Phosphoinositide-3-kinase (PI3K).
DR Reactome; R-RNO-912526; Interleukin receptor SHC signaling.
DR Reactome; R-RNO-912631; Regulation of signaling by CBL.
DR Reactome; R-RNO-9607240; FLT3 Signaling.
DR UniPathway; UPA00220; -.
DR PRO; PR:A0A0G2K344; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000056371; Expressed in thymus and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0014704; C:intercalated disc; ISO:RGD.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IDA:RGD.
DR GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; ISO:RGD.
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:RGD.
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; ISO:RGD.
DR GO; GO:0016301; F:kinase activity; ISO:RGD.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0052812; F:phosphatidylinositol-3,4-bisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0030295; F:protein kinase activator activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0060612; P:adipose tissue development; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0086003; P:cardiac muscle cell contraction; ISO:RGD.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:RGD.
DR GO; GO:0071464; P:cellular response to hydrostatic pressure; ISO:RGD.
DR GO; GO:0097009; P:energy homeostasis; ISO:RGD.
DR GO; GO:0006006; P:glucose metabolic process; ISO:RGD.
DR GO; GO:0044029; P:hypomethylation of CpG island; ISO:RGD.
DR GO; GO:0001889; P:liver development; ISO:RGD.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; ISO:RGD.
DR GO; GO:2000811; P:negative regulation of anoikis; ISO:RGD.
DR GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IGI:BHF-UCL.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:RGD.
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:0016310; P:phosphorylation; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0043491; P:protein kinase B signaling; ISO:RGD.
DR GO; GO:0110053; P:regulation of actin filament organization; ISO:RGD.
DR GO; GO:0043457; P:regulation of cellular respiration; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:2000653; P:regulation of genetic imprinting; ISO:RGD.
DR GO; GO:0040014; P:regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0055119; P:relaxation of cardiac muscle; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:1903544; P:response to butyrate; IEP:RGD.
DR GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR GO; GO:0043201; P:response to leucine; IEP:RGD.
DR GO; GO:0014870; P:response to muscle inactivity; IEP:RGD.
DR GO; GO:0035994; P:response to muscle stretch; ISO:RGD.
DR GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; ISO:RGD.
DR CDD; cd05175; PI3Kc_IA_alpha; 1.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 1.
DR Gene3D; 2.60.40.150; -; 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; PTHR10048; 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; SSF48371; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF56112; SSF56112; 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 Angiogenesis; ATP-binding; Kinase; Nucleotide-binding; Phagocytosis;
KW Proto-oncogene; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1068
FT /note="Phosphatidylinositol 4,5-bisphosphate 3-kinase
FT catalytic subunit alpha isoform"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435723"
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"
SQ SEQUENCE 1068 AA; 124354 MW; C0C63273CF161F9C CRC64;
MPPRPSSGEL WGIHLMPPRI LVECLLPNGM IVTLECLREA TLVTIKHELF KEARKYPLHQ
LLQDESSYIF VSVTQEAERE EFFDETRRLC DLRLFQPFLK VIEPVGNREE KILNREIGFV
IGMPVCEFDM VKDPEVQDFR RNILNVCKEA VDLRDLNSPH SRAMYVYPPN VESSPELPKH
IYNKLDKGQI IVVIWVIVSP NNDKQKYTLK INHDCVPEQV IAEAIRKKTR SMLLSSEQLK
LCVLEYQGKY ILKVCGCDEY FLEKYPLSQY KYIRSCIMLG RMPNLMLMAK ESLYSQLPID
SFTMPSYSRR ISTATPYMNG ETATKSLWVI NSALRIKILC ATYVNVNIRD IDKIYVRTGI
YHGGEPLCDN VNTQRVPCSN PRWNEWLNYD IYIPDLPRAA RLCLSICSVK GRKGAKEEHC
PLAWGNINLF DYTDTLVSGK MALNLWPVPH GLEDLLNPIG VTGSNPNKET PCLELEFDWF
SSVVKFPDMS VIEEHANWSV SREAGFSYSH TGLSNRLARD NELRENDKEQ LRALCTRDPL
SEITEQEKDF LWSHRHYCVT IPEILPKLLL SVKWNSRDEV AQMYCLVKDW PPIKPEQAME
LLDCNYPDPM VRSFAVRCLE KYLTDDKLSQ YLIQLVQVLK YEQYLDNLLV RFLLKKALTN
QRIGHFFFWH LKSEMHNKTV SQRFGLLLES YCRACGMYLK HLNRQVEAME KLINLTDILK
QEKKDETQKV QMKFLVEQMR QPDFMDALQG FLSPLNPAHQ LGNLRLEECR IMSSAKRPLW
LNWENPDIMS ELLFQNNEII FKNGDDLRQD MLTLQIIRIM ENIWQNQGLD LRMLPYGCLS
IGDCVGLIEV VRNSHTIMQI QCKGGLKGAL QFNSHTLHQW LKDKNKGEIY DAAIDLFTRS
CAGYCVATFI LGIGDRHNSN IMVKDDGQLF HIDFGHFLDH KKKKFGYKRE RVPFVLTQDF
LIVISKGAQE YTKTREFERF QEMCYKAYLA IRQHANLFIN LFSMMLGSGM PELQSFDDIA
YIRKTLALDK TEQEALEYFT KQMNDAHHGG WTTKMDWIFH TIKQHALN
