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Database: UniProt
Entry: A0A3P8V5V7_CYNSE
LinkDB: A0A3P8V5V7_CYNSE
Original site: A0A3P8V5V7_CYNSE 
ID   A0A3P8V5V7_CYNSE        Unreviewed;       960 AA.
AC   A0A3P8V5V7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010};
DE            EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010};
OS   Cynoglossus semilaevis (Tongue sole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC   Cynoglossinae; Cynoglossus.
OX   NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000009937.1, ECO:0000313|Proteomes:UP000265120};
RN   [1] {ECO:0000313|Ensembl:ENSCSEP00000009937.1, ECO:0000313|Proteomes:UP000265120}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24487278;
RA   Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA   Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA   Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA   Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA   Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA   Zhao Y., Schartl M., Tang Q., Wang J.;
RT   "Whole-genome sequence of a flatfish provides insights into ZW sex
RT   chromosome evolution and adaptation to a benthic lifestyle.";
RL   Nat. Genet. 46:253-260(2014).
RN   [2] {ECO:0000313|Ensembl:ENSCSEP00000009937.1}
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; A0A3P8V5V7; -.
DR   STRING; 244447.ENSCSEP00000009937; -.
DR   Ensembl; ENSCSET00000010055.1; ENSCSEP00000009937.1; ENSCSEG00000006369.1.
DR   GeneTree; ENSGT00940000159079; -.
DR   InParanoid; A0A3P8V5V7; -.
DR   UniPathway; UPA00220; -.
DR   Proteomes; UP000265120; Chromosome 10.
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; 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:UP000265120};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          16..105
FT                   /note="PI3K-ABD"
FT                   /evidence="ECO:0000259|PROSITE:PS51544"
FT   DOMAIN          184..274
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          316..509
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          418..595
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          662..943
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   960 AA;  111298 MW;  7FBD295536149DC4 CRC64;
     MPPGKYGMQE EWEKEGVQEI VMDFLLPTGI FLKFPVSRND TIKNIKKMVW RNARSEALFS
     ALGDPDAYVF TCINQTAERE ELEEESRRIS DVQPFMCVLR LVAREGDRVE KLTNAQISLL
     IGKGLHEFEA QKNHEVNEFR LKMRTFCEDK ALEQQRLPWQ QWMEYSFPTD LEPCGSPPQK
     SKNIKKIFII VKFEACDESF MLQQNPQDNP GALIRSALKK KATVFRSMRQ EPEDYTLQVN
     GRWEFIYGKH PLCQFKYIFS CLTNGQNPHL IMVHRSTISK YQEEQGRMCS QVFKSHSSSR
     PPPLPLKKCT SSLWSINEPF CVQLLQGIRV NADEGMKLVV QAGLFHGSEL LCKIVTSSEV
     TVCSEPLWDQ KLNFDINVAD LPRMSRLCFA LYAVIEKNKK PRGTKKKNKK AISEVETNGD
     IAHVTKEEHM KLKEIMDNKN YTEFFEDEKE LLWKLRAEVR NHYPESLSKL LQITKWNKRE
     DVVQMVSLLR NWPDLPAIQA LELLDYSFPE PAVRYFTIRC LRMLSDDELL QYLIQLVQVL
     KYESYLDCDL TTFLLERALS NKRIGHFLFW HLKSEMHVPS VTLRFGLILE AYCRGNIHHI
     KLLSKQNEAL GKMKALSDFV KSGSQKLTAE DLKMCIRQES YLEALSDILS PLNPSIILTE
     ICADKCRFMD SKMKPLWLMY KNNLSQGDMV GIIFKNGDDL RQDMLTLQMI QLMETLWKKE
     GLDLRMIPYG CLSTGNKMGL IEVVKNSDTI ANIQRNNSNS AATAAFNKDA LLNWLKSKNP
     EDKLDQAIEE FTLSCAGYCV ATYVLGIGDR HNDNIMIRET GQLFHIDFGH FLGNFKRKLG
     INRERVPFIL TYDFVHVIQE GRTNNSEKFE RFREYCERAY KILCRNGTLF VNLFAMMKAA
     GLPELTSFKD IQYLKDSLAL GKTEEEALKN FKVKFNEALR ESWKTKVNWM MHSLAKDNRP
//
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