ID A0A7L0RAA6_GLABR Unreviewed; 1046 AA.
AC A0A7L0RAA6;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 24.
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};
DE Flags: Fragment;
GN Name=Pik3cd {ECO:0000313|EMBL:NXL27685.1};
GN ORFNames=GLABRA_R10339 {ECO:0000313|EMBL:NXL27685.1};
OS Glaucidium brasilianum (Ferruginous pygmy-owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Strigiformes;
OC Strigidae; Glaucidium.
OX NCBI_TaxID=78217 {ECO:0000313|EMBL:NXL27685.1, ECO:0000313|Proteomes:UP000591073};
RN [1] {ECO:0000313|EMBL:NXL27685.1, ECO:0000313|Proteomes:UP000591073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-008-63 {ECO:0000313|EMBL:NXL27685.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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:NXL27685.1}.
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DR EMBL; VXAP01000018; NXL27685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L0RAA6; -.
DR OrthoDB; 67688at2759; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000591073; Unassembled WGS sequence.
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, ECO:0000313|EMBL:NXL27685.1};
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:UP000591073};
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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXL27685.1"
FT NON_TER 1046
FT /evidence="ECO:0000313|EMBL:NXL27685.1"
SQ SEQUENCE 1046 AA; 120105 MW; 5CC4332E24AEFA5F CRC64;
MPPGIYCPME FWSKGENQNI QVDFLLPTGI YLNLSVSCNA SLGTIKQVVW KHAQYEPLYH
MLSDPEAYVF TCINQTAEQQ ELEDEQRRLC DIQPFLPVLR LVAREGDRVK KVINSQISLL
IGKGLHEFDS VQDPEVNDFR TKMCQFCEER AAKRQQLSWS AWMEYNFPLQ LEPMAKGLGT
GPLHNPTKNI FVNVKFQSGG ESFTFQISPK EFPITLMSYA IKKQATVFRH ETLESPEDYT
LQVNGKCEYL YGNYPLYQFQ YIRSCLHRGL TPHLTMVHSS TIIAMRDEQT NCIASPPKMA
AKPPPLPKKK PNYGSLWSLE QSFYIELVQG SKVNADERMK LVVQAGLFHG NEMLCKTVSS
SEVNVCSEPV WKQRLDFDIN ICDLPRMARL CFALYAVIEK AKKARSTKKK SKKADCPIAW
VNVMLFDYKD QLKTGECCLH MWSSFPDEKG ELLNPMGTVQ CNPNTESAAA LVICFPSVAS
HPVYYPSFEQ LLELGRNGEQ PRAAPEDPEE KLQLREILER RSHTELYEHE KDLVWKMRYD
IRDQYPQALA KLLIITKWNK HEDVAQMISL LQTWPELPVL NALELLDFSF PDRYVGSFAI
NSLKKLTDHE LFQYLLQLVQ VLKYESYLDC ELTKFLLDRA LSNRKIGHFL FWHLRSEMHV
PAVALRFGLI LEAYCRGSTH HMKVLMKQGE ALNKMKALND FVKSSSQKAP KPQTKEMMHV
CMKQETYLEA LSHLQSPLNP NIILAEVCVD QCTFMDSKMK PLWIVFNNEE TGGGGVGIIF
KNGDDLRQDM LTLQMIQLMD ILWKQEGLDL RMTPYGCLST GDKTGLIEVV MHSDTIANIQ
LNKSNMAATA AFNKDALLNW LKSKNPGDAL EQAIEEFTLS CAGYCVATYV LGIGDRHSDN
IMIRETGQLF HIDFGHFLGN FKTKFGINRE RVPFILTYDF VHVIQQGKTN NNEKFERFRG
YCEKAYMILR RHGLLFLHLF ALMKAAGLPE LSCSKDIQYL KDSLALGKTD EEALKHFRLK
FNEALRESWK TKVNWLAHNV SKDNRQ
//
