ID A0A3B3QQY2_9TELE Unreviewed; 1279 AA.
AC A0A3B3QQY2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Phosphatidylinositol-4-phosphate 3-kinase, catalytic subunit type 2 beta {ECO:0000313|Ensembl:ENSPKIP00000009072.1};
GN Name=PIK3C2B {ECO:0000313|Ensembl:ENSPKIP00000009072.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000009072.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000009072.1}
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-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
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 -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR AlphaFoldDB; A0A3B3QQY2; -.
DR STRING; 1676925.ENSPKIP00000009072; -.
DR Ensembl; ENSPKIT00000033169.1; ENSPKIP00000009072.1; ENSPKIG00000024263.1.
DR GeneTree; ENSGT00940000158263; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
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; cd04012; C2A_PI3K_class_II; 1.
DR CDD; cd08381; C2B_PI3K_class_II; 1.
DR CDD; cd00869; PI3Ka_II; 1.
DR Gene3D; 3.10.20.770; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
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 Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000008; C2_dom.
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; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF30; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 3-KINASE C2 DOMAIN-CONTAINING SUBUNIT BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00168; C2; 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; PF00787; PX; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50004; C2; 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; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 19..105
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 269..428
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 447..623
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 692..970
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1007..1123
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1148..1268
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 1279 AA; 145982 MW; 834CF0C300654D2E CRC64;
MRCQGSPLHT PSVTILQDKS AVYQSIYICY PCFSIATPGS STIDLLIYQT LCYAHDDLVL
IDVEDYLLKV CGHEEFLMNN QTLASLEYIQ QCLKFDWEIR LFLTKRSTIS QELVRTEEDD
ETPSTMNHSI LLQERPIKQT VTREALTLLL DTFHNEAESF VLSEMELPLR VERLVQSVKA
LCSSLASIET SDITAALSQL PACPCRLQPR VLKDISVLAS QENREKVVEK LTSSILELVE
LYCSTFNANF HTTPQSYRPS VPLQEAGFVT SVLSFSVYAA HRIPITWAAS YEGFFLSCSL
THGGAELCAP QHTSKQPVSK YLFHLVVWDQ RICFPVQINR LPRETQLTVT MYATLLPPPG
GTEDKNKQRR SMEALGWVTM PLFNFRHILT CGRKLLGFWP STPGSGNVRS STPNFSQPDS
IILQVDFPLF SFEVHFSTPP PAEFSPQYEF SRLDLNSQRQ LQDVLHKKSF LWLTNEDRKL
LWEKRYFCHA ESSGLPLVLA SAPNWEWACL PDIYALLHQW ACMNHLDSLG LLHAIFPDQE
LRHTAVQWMD SISDSELLDF LPQLVQALKY ECYLDSPLVR FLLRRAIGDI RIAHYLFWLL
KDALQDSQFS MRYQYLLAAL LCCTGRGLRE ELDRQGWLVS ILAKVAQNVR DTSPSTRQAT
LRDRLEEVHN FFCVSGSCRL PLNPGLMVKD INIQGCSYFN SNAVPLKLSF QNLDPLGDNI
NIIFKSGDDL RQDMLTLQII RIMNKIWIQE GLDMRMVNFR CFSTGRGRGM VEMIPNAETL
RKIQVEHGVT GSFKDRPLAD WLQKHNPSED EYEKAVENFI YSCAGCCVAT YVLGICDRHN
DNIMLKSSGH MFHIDFGKFL GHAQMFGNIK RDRAPFVFTS DMAYVINGGD KPSSRFHDFV
DLCCEAYNLI RKHTHLFLNL LGLMLSCGIP ELSDLQDLKY VYDALRPHES ESDATMYFTR
LIESSLGSVA TKLNFFIHNL AQMKFASSEE QPVLSFAPRV HTLKSDGLIR SLFVCRHIRT
YSPNKGYAYV VKVERDCQHG ATLVQRSFEE FHELHSKLRL IFPSSKLPSF PSRFVIGRSR
GEAMADRRKD ELNGYVWHLI HAAREVAQCD FIYTFFHPLP RDERPGTVYN TLQNKPSEVS
WAPIAGKIVG EVKLSISYKS NKLFIMVMHI RGLQPLQDGT DPDPYVKLYL LPDPQKTSKR
KTKAAKRTCN PTYNEMLVYD GIPWGDLQQR VIHLRVLSEG AFWENLLLGE AFISLTALLP
GERWVDWHQL GTGGSDGTR
//