ID A0A3Q1J789_ANATE Unreviewed; 1040 AA.
AC A0A3Q1J789;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010};
DE EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000026238.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000026238.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3Q1J789; -.
DR STRING; 64144.ENSATEP00000026238; -.
DR Ensembl; ENSATET00000026657.2; ENSATEP00000026238.1; ENSATEG00000018121.2.
DR GeneTree; ENSGT00940000159079; -.
DR InParanoid; A0A3Q1J789; -.
DR OMA; HDPEVND; -.
DR OrthoDB; 10350at2759; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0046934; F:1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08693; C2_PI3K_class_I_beta_delta; 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; 1.10.1070.11; 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:UP000265040};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 16..105
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 187..277
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 320..477
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 498..675
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; 119978 MW; CBD79EAE7EBA3B54 CRC64;
MPPGKYGMQG EWEKEGDHEI MMDFLLPTGI FLKFPVSRND TIKTIKRMVW KNARSEALFT
ALGDPDAYVF TCINHTAERE ELEEESRRIS DVQPFMCVLR LVAREGDRVE KLTNAQISLL
IGKGLHEFEV QKNHEVNEFR TKMRVFCEEK AQERQRLPWH QWMEYSFPCD LEPCCSPQCG
SSRSKNTKKI LINIKFEASD ESFMLQQDPQ DPPLVLMRSA LKKKATVFRS VRQEPEDYTL
QVNGRWEFIY GNHPLCQFKY IFSCLRNGQN PHLIMVHHST ISKYQEEQGR MCNQVYKSCS
LSRPPPLPLK KQNTSSLWSI NEPFCIHLVQ GSRVNADEGM KLVVQAGLFH GSELLCKVVT
SSEVTVCSEP LWDQKLEFDI NVADLPRMGR LCFALYAVIE KAKKPRGTKK KNKKADCPIA
WVNTMVFDYK DQLKTGEFLL STWPSVPDDK SDLLNPMGTV ERNPNVDSAA GLLIRFANIR
PYPLYYPPLD KISDVERNGD ATTGTKEEFV KLKEIMDNKN YTEFFEDEKE LLWKLRAEVR
SSYPESLSKL LLITKWNKRE DVVQMVSLLR NWPDLPAIHA LELLDYSFPD PAVRSFTIRC
LRNLSDDELL QYLIQLVQVL KYESYLDCDL TTFLLERALS NRRIGHFLFW HLRSEIHVAS
VSLRFGLILE AYCRGNIHHI RLLTKQNEAL AKMKSLSDFV KSGSQKMTVE DLKLCIRQES
YLEALSDLLS PLNPSIILSG ICADKCRFMD SKMKPLWLMY KNPGTQGDMV GIIFKNGDDL
RQDMLTIQMI QLMENLWKKE GLDLRMIPYG CLSTGNKTGL IEVVKNSDTI ANIQRNCSNS
AATAAFNKDA LLNWLKSKNP GDKLDQAIEV FTLSCAGYCV ATYVLGIGDR HNDNIMIRET
GQLFHIDFGH FLGNFKRKLG INRERVPFIL TYDFVHVIQQ GRTNNSEKFE RFREYCERAY
KILCRNGTLF VNLFAMMKAA GLPELTSFKD IQYLKDSLCL GKSDDEALKN FKVKFNEALR
ESWKTKVNWM MHSLAKDNRP
//