ID A0A8B9VDP5_9AVES Unreviewed; 1040 AA.
AC A0A8B9VDP5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 08-OCT-2025, sequence version 2.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010};
DE EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010};
OS Anas zonorhyncha (Eastern spot-billed duck).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=75864 {ECO:0000313|Ensembl:ENSAZOP00000022841.1, ECO:0000313|Proteomes:UP000694549};
RN [1] {ECO:0000313|Ensembl:ENSAZOP00000022841.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSAZOP00000022841.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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: Phospholipid metabolism; phosphatidylinositol phosphate
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004805}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR AlphaFoldDB; A0A8B9VDP5; -.
DR Ensembl; ENSAZOT00000024536.1; ENSAZOP00000022841.1; ENSAZOG00000014583.1.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000694549; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-EC.
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; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0042113; P:B cell activation; IEA:UniProtKB-ARBA.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProtKB-ARBA.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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 GO; GO:0051094; P:positive regulation of developmental process; IEA:UniProtKB-ARBA.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:UniProtKB-ARBA.
DR GO; GO:0051240; P:positive regulation of multicellular organismal process; IEA:UniProtKB-ARBA.
DR GO; GO:0022603; P:regulation of anatomical structure morphogenesis; IEA:UniProtKB-ARBA.
DR GO; GO:2000026; P:regulation of multicellular organismal development; IEA:UniProtKB-ARBA.
DR CDD; cd08693; C2_PI3K_class_I_beta_delta; 1.
DR CDD; cd05174; PI3Kc_IA_delta; 1.
DR Gene3D; 3.10.20.770; -; 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; 3.30.1010.10; 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; IPR037703; PI3-kinase_delta_cat.
DR InterPro; IPR015433; PI3/4_kinase.
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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF35; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT DELTA 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000694549};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 21..110
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 190..282
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 306..479
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 494..671
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 742..1023
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1040 AA; 119675 MW; 7B031E7B54FF7681 CRC64;
MCFNRMPPGI YCPMEFWSKG ENQNIQVDFL LPTGIYLNLS VSCNASLGTI KQVVWKHAQY
EPLYHMLSDP EAYVFTCINQ TAEQQELEDE QRRLCDIQPF LPVLRLVARE GDRVKKLINS
QISLLIGKGL HEFDSMQDPE VNDFRTKMCQ FCEERAAKRQ QLSWAAWMEY NFPLQLEPML
VAEVAACTRG GKLFVYGWER STDPSSFTFQ IAPDEFPITL MSYAIKKQAT VFRHETMESP
EDYTLQVNGK YEYLYGNYPL YQFQYIRSCL HRGLTPHLTM VHSSTIIAMR DEQINCIANT
PKMSPKPPPL PKKKVKGHGS FVNGSNPRGL TVFSYFFSPQ LVVQAGLFHG NEMLCKMVSS
SEVNVCSEPV WKQRLDFDIN ICDLPRMARL CFALYAVIEK AKKARSTKKK SKKAVSKDCP
IAWVNVMLFD YKDQLKTGEC CLHMWSSFPD EKGELLNPMG TVQCNPNTES AASLVICFPN
VASHPVYYPS FDPLYALFCD SHEQKLQLKE ILERRSHTEL YEHEKDLVWK MRYDIRDQYP
QALAKLLIIT KWNKHEDVAQ MISLLQTWPE LPVLNALELL DFSFPDRYVG SFAINSLKKL
TDNELFQYLL QLVQVLKYES YLDCELTKFL LDRALSNRKI GHFLFWHLRS EMHVPAVALR
FGLILEAYCR GSTHHIKVLM KQGEALNKMK ALNDFVKVSS QKATKPQTKE MMHVCMKQET
YLEALSHLQS PLNPSIILAE VCVDQCTFMD SKMKPLWIVF NNEETSGGGV GIIFKNGDDL
RQDMLTLQMI QLMDVLWKQE GLDLRMTPYG CLSTGDKTGL IEVVMHSDTI ANIQLNKSNM
VATAAFNKDA LLNWLKSKNP GDALEQAIEE FTLSCAGYCV ATYVLGIGDR HSDNIMIRET
GQLFHIDFGH FLGNFKTKFG INRERVPFIL TYDFVHVIQQ GKTNNNEKFE RFRGYCEKAY
MILRRHGLLF LHLFALMKAA GLPELSCSKD IQYLKDSLAL GKTDEEALKH FRLKFNEALR
ESWKTKVNWL AHNVSKDNRQ
//
