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Database: UniProt
Entry: I3J294_ORENI
LinkDB: I3J294_ORENI
Original site: I3J294_ORENI 
ID   I3J294_ORENI            Unreviewed;      1041 AA.
AC   I3J294;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010};
DE            EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000002984.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000002984.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) 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; I3J294; -.
DR   Ensembl; ENSONIT00000002985.2; ENSONIP00000002984.2; ENSONIG00000002388.2.
DR   GeneTree; ENSGT00940000159079; -.
DR   InParanoid; I3J294; -.
DR   OMA; CCEPQIT; -.
DR   UniPathway; UPA00220; -.
DR   Proteomes; UP000005207; Linkage group LG20.
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; cd08693; C2_PI3K_class_I_beta_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; 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; IPR015433; PI_Kinase.
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   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          16..105
FT                   /note="PI3K-ABD"
FT                   /evidence="ECO:0000259|PROSITE:PS51544"
FT   DOMAIN          186..276
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          497..676
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          743..1024
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   1041 AA;  120776 MW;  DBC6D6A0C2B77656 CRC64;
     MPPGKYGMQE EWEKEGDQAI NMDFLLPTGI FLKFPVSRND TIKNIKKMVW KNARSEALFC
     GLGDPDGYVF TCINETAERE ELEEESRRIS DVRPFMCVLR LVAREGDRVE KLTNAQISLL
     IGKGLHEFEA QKNDEVNEFR TKMRVFCEEK AQDRQSLPWQ KWMEYSFPCE LEPCCSLPQS
     LKSKNIKKIF INVKFEASDE SFMLQQDPHD QPLALMKSAL KKKATVFRLM RQEPEDYTLQ
     VNGRWDFIYG KHPLCQFKYI FSCLRNGQNP HLTMVHYSTI TKYQEEQGRM CSQVYKSRSL
     SRPPPLPLKK QNTSSLWSIN EPFHIHLVQG KRVNADEGMK LVVQAGLFHG SELLCKVVTS
     SEVTVSSEPL WNQKLEFDIN VADLPRMSRL CFALYGVIEK TKKPRGTKKK NKKADCPIAW
     VNTMVFDYKD QLKTGEFHLS TWPSVPDDKS DLLNPMGTVE KNPNVDSAAE LLIHFPNIRP
     HPLYYPPLEK ICDMERNGDL SLANKEEYFK LKEIMDNKNY TEFFEDEKEL LWKLRTEVRD
     HYPESLSKLL LITKWNKRED VVQVRMVNLL RNWPDLPAIH ALELLDYSFP DPAVRSFTIR
     CLRKLSDDEL LHYLIQLVQV LKYESYLDCD LTTFLLERAL SNRRIGHFLF WHLRSETHVA
     SVGLRFGLIL EAYCRGNIHH IKLLTKQNEA LGKMKALSDF VKLGSQKVTA EDLKQCIRQE
     SYLEALSDLL SPLNPSIILS EICTDRCRFM DSKMKPLWLM FKNPAVEGDM VGIIFKNGDD
     LRQDMLTLQM IQLMENLWKK EGLDLRMIPY GCLSTGNKMG LIEVVKNSDT IANIQRNSSN
     SAATAAFNKD ALLNWLKSKN PEDKLDQAIE EFTLSCAGYC VATYVLGIGD RHNDNIMIRE
     TGQLFHIDFG HFLGNFKRKL GINRERVPFI LTYDFVHVIQ QGRTNNSEKF ERFREYCERA
     YKILCRNGTL FVNLFAMMKA AGLPELTSFK DIQYLKDSLA LGKTEDEALK NFKVKFNEAL
     RESWKTKVNW MMHSLAKDNR P
//
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