ID A0A0S7K0U3_9TELE Unreviewed; 1034 AA. AC A0A0S7K0U3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-APR-2021, entry version 35. DE RecName: Full=Phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010}; DE EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010}; GN Name=PK3CA {ECO:0000313|EMBL:JAO70964.1}; OS Poeciliopsis prolifica (blackstripe livebearer). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae; OC Poeciliopsis. OX NCBI_TaxID=188132 {ECO:0000313|EMBL:JAO70964.1}; RN [1] {ECO:0000313|EMBL:JAO70964.1} RP NUCLEOTIDE SEQUENCE. RA Jue N.K., Foley R.J., Obergfell C., Reznick D.N., O'Neill R.J., RA O'Neill M.J.; RT "Parallel Evolution in Life History Adaptation Evident in the Tissue- RT Specific Poeciliopsis prolifica transcriptome."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000256|PROSITE- CC ProRule:PRU00879}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GBYX01224107; JAO70964.1; -; Transcribed_RNA. DR UniPathway; UPA00220; -. DR GO; GO:0052812; F:phosphatidylinositol-3,4-bisphosphate 5-kinase activity; IEA:UniProtKB-EC. DR GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC. DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.1070.11; -; 1. DR InterPro; IPR016024; ARM-type_fold. 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; IPR001263; PI3K_accessory_dom. DR InterPro; IPR003113; PI3K_adapt-bd_dom. DR InterPro; IPR002420; PI3K_C2_dom. DR InterPro; IPR000341; PI3K_Ras-bd_dom. DR InterPro; IPR015433; PI_Kinase. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR10048; PTHR10048; 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; SSF48371; 1. DR SUPFAM; SSF54236; SSF54236; 1. DR SUPFAM; SSF56112; SSF56112; 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; PS51547; PI3K_C2; 1. DR PROSITE; PS51546; PI3K_RBD; 1. DR PROSITE; PS51545; PIK_HELICAL; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE- KW ProRule:PRU00269}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU00269}. FT DOMAIN 16..105 FT /note="PI3K-ABD" FT /evidence="ECO:0000259|PROSITE:PS51544" FT DOMAIN 187..289 FT /note="PI3K-RBD" FT /evidence="ECO:0000259|PROSITE:PS51546" FT DOMAIN 332..489 FT /note="C2 PI3K-type" FT /evidence="ECO:0000259|PROSITE:PS51547" FT DOMAIN 518..695 FT /note="PIK helical" FT /evidence="ECO:0000259|PROSITE:PS51545" FT DOMAIN 798..1034 FT /note="PI3K/PI4K" FT /evidence="ECO:0000259|PROSITE:PS50290" FT COILED 710..730 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 1034 AA; 119376 MW; B0B6BCC7C417020A CRC64; MVPRPSSGEL WGLHLMPPRI LVDCCLPNGM MVSLECLRET PLINIKQQLF IEARKYPLYH LLQEESCYIF VGVTQEAERE EFYDETRRLC DLRLFHPILK VIEPLGNREE KILNREIGFA IGMPVCEFEM MKDPEIQDFR RSILSVCREA MEEREGGGAH TQALYVYPPN VESSPHLPQH IYSKLDKGRL IVTIWVIMSP SNSKQKYTLK VSHDSLPEQL IAESIRKKSR SMHLSPQQLR LCVQEYQGQY ILKVCGCDEY LLENFPLSQY KYIRSCIIVG RLPHLMLVSK DSLYSQLPAS GFVTPSYSRR TPQPSPCPGG GDGSPPRSLW AFNTLLRVRL LCATYVNVNI RDIDKIYVRT GIYHGGEPLC ENVNTQRVPC SNPRWNEWLT YDIYLADLPR SARLCLSICS VKGRKGAKEE HCPLAWGNVS LFDYMDILVS GKVALSLWPV PHGLEDLLNP IGVAGSNPNK ETPCVELEFS RFSQTVVFPD EQQIEEHANW TISRELGYNY CHGLSSRLAC DSSVSATDAE QLRSLCSRDP LYELSEQEKD FLWRHRHYCL NIPESLPKLL LSVKWNSRDE VSQMYCLLKE WPLMEPESAL ELLDCNFPDP IVREFALRCL VQGLTDDKLS QYLLQLVQVL KYEMYLDNPL ARFLIKKALT NQRIGHFFFW HLKSEMHNKT VSRRFGLLLE AFCRACGMYL KHLNRQVEAM DKLVNLTDTL KQEKKDETQK TQMKFLVEHM SRPDYMESLQ GFVSPLNPVH QLGNLRLEEC RIMSSAKRPL WLNWENPDIM SELLFTNNEI IFKNGDDLRQ DMLTLQIIKI MENIWQNQGL DLRMLPYGCL SIGDRVGLIE VVKNSYTIMQ IQCKGGLKGA LQFNSNTLHH WIKDKNHGEA YDRAIDLFTR SCAGYCVATF ILGIGDRHNS NIMVKENGQL FHIDFGHFLD HKKKKFGYKR ERVPFVLTQD FLIVISKGIQ ESTKTKEFER FQEMCYKAYL AIRQHASLFI NLFSLMLGCG MPELQSFDDI AYLRKTLALG KTGE //