ID A0A3B3XCW0_9TELE Unreviewed; 1121 AA.
AC A0A3B3XCW0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010};
DE EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000012804.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000012804.1}
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 RefSeq; XP_014832095.1; XM_014976609.1.
DR RefSeq; XP_014832100.1; XM_014976614.1.
DR AlphaFoldDB; A0A3B3XCW0; -.
DR STRING; 48701.ENSPMEP00000012804; -.
DR Ensembl; ENSPMET00000020341.1; ENSPMEP00000012804.1; ENSPMEG00000015091.1.
DR GeneID; 106910053; -.
DR KEGG; pmei:106910053; -.
DR CTD; 5294; -.
DR OrthoDB; 10350at2759; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000261480; Unplaced.
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 CDD; cd00894; PI3Kc_IB_gamma; 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; 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; PF00454; PI3_PI4_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 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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 36..137
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 219..311
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 359..535
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 559..741
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 815..1098
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1121 AA; 128810 MW; 3558A8F1DABC595C CRC64;
MDRQQIQVSD EEREVAREES RRRRRKKAIT SASSTSMDQI SVEFVLPTVA RGGSSPDSLL
LEVAGNWTVE QVKAQVWMKA VSLNLCPDFY QRFCPDHCIL LYQKKGTVCE IYDKHQVFQT
LDCIRYWRAL KKDVGRIQLV PRPQPTDESQ QYQRYLNYLI GYDVTDVSNV HDDELEFTRR
KLLTPRRIEL SDRDPNLYSM DPWVTRKPLP EHLLSKVNNG YILVVIHVST SSQTIKVSID
DTPSQVLASF FAKTANKRVL LGIPEHLSDE DFVLRVCGRE EYLYGEKALQ SFNWIRQSLK
NGEEIHLVLE TPPDPELDLV QREDWAQVDD CTGVAGTHEQ LTIAEKDHER VFTISMWDCN
RKFRVKVLGI DIPSLPKVPE FMVFIEASIF HGQQLLAQER TTSKTFNEEV LWNCWLEFNI
KIKDLPKGAR LNLQVICGKQ PQTPNSKSSY HDNTSGSSTL EGKTKNRLLY YVNLLLIDHR
SLLRQGEFIL HMWKMPEKSE ESSSSINADK LTSATNPDKA SSMAIAILLD KYCYPVVLPK
SREVGRDCGA GSEEGDGGER GQREMPNHLK KQFAAIVSTD PLHPLSPEDK ELLWHFRHEC
MRDPRAYPKL LGSVRWGKQE DVLATHRLLD RSNAWDTSGL DVGLAMQLLD CHYSDAQVRS
MAVRKLETLE DDDVLRYLLQ LVQAVKFEPY HDSALVRFLL KRALRSKRIG HFLFWFLRSE
IAQSMHYQQR YAVLLEAYLR GCGENMLQDF RKQVEMTEAL QKVTREMKAM SADKYDVTQQ
VVIQLRQKLE TLQLSGLPES FRVPYDPGLR AGTLLIEQCK VMASKKKPLW LQFKRADPTT
LSKDPVGIIF KDGDDLRQDM LILQILLIME SIWETESLDL CLLPYGCIST GNKIGMIEIV
KDATTIATIQ QSVVGSTGAF KDEILYQWLR DKCVSEEKFQ QAVERFLYSC GGYCVATYVL
GIGDRHNDNI MITESGNLFH IDFGHILGNY KSFMGISKEW VPFVLTPDFL YVMGTSGKKS
SPHFQKFQDV CVKAYLALRH HTNLLIILFS MMLMTGMPQL TSKEDIEYIR EALTVGRSED
EAQRHLLDQI EICREKGWMV QINWFVHLVL GIKQGVEKRS T
//
