ID A0A9D3QE22_MEGAT Unreviewed; 1072 AA.
AC A0A9D3QE22;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 18-JUN-2025, entry version 13.
DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform {ECO:0000256|ARBA:ARBA00073893};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073};
DE EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE AltName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha {ECO:0000256|ARBA:ARBA00083121};
DE AltName: Full=Phosphoinositide-3-kinase catalytic alpha polypeptide {ECO:0000256|ARBA:ARBA00078524};
DE AltName: Full=Serine/threonine protein kinase PIK3CA {ECO:0000256|ARBA:ARBA00076072};
GN ORFNames=MATL_G00031240 {ECO:0000313|EMBL:KAG7488113.1};
OS Megalops atlanticus (Tarpon) (Clupea gigantea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Elopiformes; Megalopidae; Megalops.
OX NCBI_TaxID=7932 {ECO:0000313|EMBL:KAG7488113.1, ECO:0000313|Proteomes:UP001046870};
RN [1] {ECO:0000313|EMBL:KAG7488113.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YG-15Mar2019-1 {ECO:0000313|EMBL:KAG7488113.1};
RC TISSUE=Brain {ECO:0000313|EMBL:KAG7488113.1};
RA Zahm M., Roques C., Cabau C., Klopp C., Donnadieu C., Jouanno E.,
RA Lampietro C., Louis A., Herpin A., Echchiki A., Berthelot C., Parey E.,
RA Roest-Crollius H., Braasch I., Postlethwait J., Bobe J., Montfort J.,
RA Bouchez O., Begum T., Mejri S., Adams A., Chen W.-J., Guiguen Y.;
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00050641};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55633;
CC Evidence={ECO:0000256|ARBA:ARBA00050641};
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:0000256|ARBA:ARBA00051347};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43397;
CC Evidence={ECO:0000256|ARBA:ARBA00051347};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); 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:0000256|ARBA:ARBA00048977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000256|ARBA:ARBA00048977};
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:0000256|ARBA:ARBA00023985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000256|ARBA:ARBA00023985};
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:0000256|ARBA:ARBA00023981};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21293;
CC Evidence={ECO:0000256|ARBA:ARBA00023981};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004805}.
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:0000256|ARBA:ARBA00065166}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG7488113.1}.
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DR EMBL; JAFDVH010000002; KAG7488113.1; -; Genomic_DNA.
DR OrthoDB; 67688at2759; -.
DR Proteomes; UP001046870; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA.
DR GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; IEA:TreeGrafter.
DR GO; GO:0005944; C:phosphatidylinositol 3-kinase complex, class IB; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:InterPro.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:TreeGrafter.
DR CDD; cd08398; C2_PI3K_class_I_alpha; 1.
DR CDD; cd00872; PI3Ka_I; 1.
DR CDD; cd05175; PI3Kc_IA_alpha; 1.
DR FunFam; 1.10.1070.11:FF:000006; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 1.25.40.70:FF:000001; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 2.60.40.150:FF:000041; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 3.10.20.770:FF:000005; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 3.10.20.90:FF:000074; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 3.30.1010.10:FF:000007; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 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; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 2.
DR Gene3D; 3.30.1010.10; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 4; 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; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Angiogenesis {ECO:0000256|ARBA:ARBA00022657};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phagocytosis {ECO:0000256|ARBA:ARBA00022907};
KW Reference proteome {ECO:0000313|Proteomes:UP001046870};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 191..293
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 334..491
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 521..698
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 769..1055
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1072 AA; 124845 MW; E20FF78634A51227 CRC64;
MGTRAGEGQS PGLELLRGAC RETVGAAYWK EEQGKWDCSD TLPVSRRQCW WSEIEREIIP
SRENNSIGLR GERLVLTTFE AEREEFYDET RRLCDLRLFQ PFLKVIEPVG NREEKILNRE
IGFAIGMPVC EFDLVKDPEV QDFRRNILNV CKDSVDLRDA NGPHSRALYV YPPNVESSPE
LPKHIYSKLD KGQIIVVIWV IVSPNNDKQK YTLKINHDCV PEQVIAEAIR KKTRSMLLSP
EQLKMCVQEY QGKYILKVCG CDEYLLEKYP LSQYKYVRSC IMLGRMPNLM LMAKESLYSQ
LPMDNFTMPS YARRISTATP YMNGEASTKS LWTINGTLRI RILCATYVNV NIRDIDKIYV
RTGIYHGGEQ MCDNVNTQRV PCSNPRWNEW LNYDMYIPDI PRAARLCLSI CSVKGRKGAK
EEHCPLAWGN VNLFDYTHTL VSGKMALNLW PVPHGLEDLL NPIGVTGSNP NKETPCLELE
FDYFSSPVKF PDMATIEDHA NWTISRELGF NYCHTGLSNR LARDNALTDS DNEQLRLVCN
RDPLSEITEQ EKDFLWRHRH YCVNMPEILP KILLAVKWNS RDEVAQMYCL LKDWPAIKPE
QAMELLDCNY PDPMIRDFAV RCLEKYLTDD KLSQYLIQLV QVLKYEQYLD NPLVRFLLKK
ALTNQRIGHF FFWHLKSEMH NKTVSQRFGL LLESYCRACG MYLKHLSRQV EAMEKLINLT
DILKQEKKDE TQKVQMKFLV EQMRRPDYMD ALQNFTSPLN PAHQLGNLRL EECRIMSSAK
RPLWLNWENP DIMSELLFQN NEIIFKNGDD LRQDMLTLQI IRIMENIWQN QGLDLRMLPY
GCLSIGDCVG LIEVVRNSHT IMQIQCKGGL KGALQFNSHT LHQWLKDKNK GEMYDLAIDL
FTRSCAGYCV ATFILGIGDR HNSNIMVKDD GQLFHIDFGH FLDHKKKKFG YKRERVPFVL
TQDFLIVISK GTQECTKTRE FERFQEMCYK AYLAIRQHAN LFINLFSMML GSGMPELQSF
DDIAYIRKTL ALDKTEQEAL DYFMKQMNDA HHGGWTTKMD WIFHTIRQHA LN
//
