ID A0A8C0VJM5_CYACU Unreviewed; 1046 AA.
AC A0A8C0VJM5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform {ECO:0000256|ARBA:ARBA00067682};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073};
DE EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010};
DE AltName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta {ECO:0000256|ARBA:ARBA00075758};
GN Name=PIK3CD {ECO:0000313|Ensembl:ENSCCEP00000022461.1};
OS Cyanistes caeruleus (Eurasian blue tit) (Parus caeruleus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Paridae; Cyanistes.
OX NCBI_TaxID=156563 {ECO:0000313|Ensembl:ENSCCEP00000022461.1, ECO:0000313|Proteomes:UP000694410};
RN [1] {ECO:0000313|Ensembl:ENSCCEP00000022461.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCEP00000022461.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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=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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR RefSeq; XP_023796328.1; XM_023940560.1.
DR AlphaFoldDB; A0A8C0VJM5; -.
DR Ensembl; ENSCCET00000034097.1; ENSCCEP00000022461.1; ENSCCEG00000020285.1.
DR GeneID; 111938683; -.
DR KEGG; ccae:111938683; -.
DR CTD; 5293; -.
DR OrthoDB; 67688at2759; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000694410; 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 FunFam; 1.10.1070.11:FF:000001; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 1.25.40.70:FF:000008; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 2.60.40.150:FF:000046; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 3.10.20.770:FF:000002; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 3.30.1010.10:FF:000005; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta; 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 Adaptive immunity {ECO:0000256|ARBA:ARBA00023130};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694410};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 16..105
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 187..278
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 319..476
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 500..677
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 748..1029
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1046 AA; 119992 MW; 471D38287B080299 CRC64;
MPPGIYCPTE FWSKGEHQNI QVDFLLPTGI YLNLCVPCNA SLGTIKQVLW KHAQYEPLFH
MLSDPEAYVF TCINQTAEQQ ELEDEQRRLC DIQPFLPVLR LVAREGDRVK KVINSQISLL
IGKGLHEFDS VQDPEVSDFR SKMCQFCEEK AAKRQQLGWA AWMEYNFPLQ LEPMAKGPGT
GSLQIPTKNI FVNVKFQSGG ESFTFQISPW EFPITLMSYA IKKQATVFRH ETVQKPEDYT
LQVNGKCEYL YGNYPLYQFQ HIRSCLQRGL TPHLTMVHSS AIIAMRDEQN SCFTSPPKAA
SKPPPLPKKK PNYGSLWSLE QPFYIELVQG SKVNADERMK LVVQAGLFHG NEMLCKTVSS
SEVSVCSEPV WKQRLDFDIN ICDLPRMARL CLALYAVIEK AKKARSTKKK SKKADCPIAW
VNVMLFDYKD QLKTGECCLH MWSSFPDEKG ELLNPMGTVQ CNPNTESAAA LVICFPSVAA
HPVYYPSFEQ LLELGRNGEQ PRAAPEDSEE KLQLREILER RSHTELYEHE KDLVWKMRYD
IRDQYPQALA KLLIITKWNK HEDVAQMISL LQTWPELPVL NALELLDFSF PDRYVGSFAI
NSLKKLTDDD VFQYLLQLVQ VLKYESYLDC ELTKFLLERA LSNRKIGHFL FWHLRSEMHV
AAVSLRFGLI LEAYCRGSTH HMKVLMKQGE ALNKMKALND FVKVSSQKAT KPQTKEMMHM
CMKQETYREA LSHLQSPLNP NIILAEVCVD QCTFMDSKMK PLWIVFNNEE TGGGGVGIIF
KNGDDLRQDM LTLQMIQLMD ILWKQEGLDL RMTPYGCLST GDKTGLIEVV MHSDTIANIQ
LNKSNMVATA AFNKDALLNW LKSKNPGDAL DQAIEEFTLS CAGYCVATYV LGIGDRHSDN
IMVRETGQLF HIDFGHFLGN FKTKFGINRE RVPFILTYDF VHVIQQGKTN NNEKFERFRG
YCERAYMILR RHGLLFLHLF ALMKAAGLPE LSCSKDIQYL KDSLALGKTD EEALKHFRLK
FNEALRESWK TKVNWLAHNV SKDNRQ
//
