ID A0A091UEB7_PHORB Unreviewed; 801 AA.
AC A0A091UEB7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010};
DE EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010};
DE Flags: Fragment;
GN ORFNames=N337_04633 {ECO:0000313|EMBL:KFQ88891.1};
OS Phoenicopterus ruber ruber.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Phoenicopteriformes; Phoenicopteridae;
OC Phoenicopterus.
OX NCBI_TaxID=9218 {ECO:0000313|EMBL:KFQ88891.1, ECO:0000313|Proteomes:UP000053700};
RN [1] {ECO:0000313|EMBL:KFQ88891.1, ECO:0000313|Proteomes:UP000053700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N337 {ECO:0000313|EMBL:KFQ88891.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|PROSITE-
CC ProRule:PRU00879}.
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DR EMBL; KK430438; KFQ88891.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091UEB7; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000053700; Unassembled WGS sequence.
DR GO; GO:0046934; F:1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08399; C2_PI3K_class_I_gamma; 1.
DR CDD; cd00872; PI3Ka_I; 1.
DR Gene3D; 3.10.20.770; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 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; 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; IPR015433; PI_Kinase.
DR InterPro; IPR045580; PIK3CG_ABD.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF34; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT GAMMA ISOFORM; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF19710; PIK3CG_ABD; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51547; C2_PI3K; 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 Kinase {ECO:0000313|EMBL:KFQ88891.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053700};
KW Transferase {ECO:0000313|EMBL:KFQ88891.1}.
FT DOMAIN 34..141
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 217..309
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 357..524
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 544..726
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 801
FT /evidence="ECO:0000313|EMBL:KFQ88891.1"
SQ SEQUENCE 801 AA; 93388 MW; AAE30F1EE0032ADC CRC64;
MELGDYEQPV VMREENKRRR RRMKPHCTSS NLSSMELIAI EFILPTSNKH TKVPEMMLLE
IAGNCTVEQM KAQIWMRAIE MSQTTDFYHT FTPDQFILQY QKKGQWYEIY DKHQVLQTLD
CILYWKVLQK KVGKIYVIQK QKPSEEVQEF QRQLNNLIGY DVTDVSNVHD DELEFTRRRL
VTPRMIEVAC RDPKLYAMHP WTTSKPLPEY LFKKITNNNI FIIIHRGTTS QKIKVSIDDT
PDMILQSFFT KMAKKKSLMD IPEDHSELDF VLRICGRDEY ITGETPIKDF HWIRQCLKNG
EEIHLVLDNP PDPNEDEVQK EEWPLVDDCT GVTGYHEQLT IDGKDHERVF TISLWDCNRK
FRVKIIGIDI PVLPRNTDLT VFVEANIQHG QQLLSQRRTS SKPFTEEVLW NIWLEFDIKI
KDLPKGALLN LQIYCGKAQG LSTKTNLQSH ESPNSDSKCK TQLLYYVNLL LIDHRFLLRS
GEYVLHMWKI PGKGEEQGSI NADKLTSATN PDKENSMAIS IVLDKYCHPI ALPKHRITSD
PQGDRTRAEM PNQLRKQLEE IIATDPLNPL SPEDKELLWH FRYESIKHPK AYPKLLSSVK
WGQQEIVAKT YQLLAKKEVW DQSTLDVGLT MQLLDCNFSD ENVRAMAVQK LESLEDDDVL
HYLLQLVQAV KFEPYHDSAL ARFLLKRGLR NKRIGHFLFW FLRSEIAQSM HYQQRFAVIL
EAYLRGCGKA MLHDFMKQVQ VIELLHKVTM EIKSVSAEKY DVTSQVIAQL RQKLEKLQSS
KLPESFRVPY DPGLRAGALV V
//
