ID A0A3Q2DZZ1_CYPVA Unreviewed; 1038 AA.
AC A0A3Q2DZZ1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=PIK3CA {ECO:0000313|Ensembl:ENSCVAP00000024569.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000024569.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000024569.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q2DZZ1; -.
DR STRING; 28743.ENSCVAP00000024569; -.
DR Ensembl; ENSCVAT00000003851.1; ENSCVAP00000024569.1; ENSCVAG00000008772.1.
DR GeneTree; ENSGT00940000155531; -.
DR OMA; YKYIRQC; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000265020; 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 GO; GO:0048696; P:regulation of collateral sprouting in absence of injury; IEA:Ensembl.
DR CDD; cd00872; PI3Ka_I; 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:SF107; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT ALPHA 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; 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:UP000265020};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
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 235..457
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 488..664
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 735..1021
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1038 AA; 120993 MW; 719E6971BF02848C CRC64;
MPPRPSSGEL WGMHLMPPSI LVDCLLPNGM ILTLECLREA TLVTVKHELF KEARKYPLYH
LLQEESSYIF VSVTQEAERE EFYDETRRLC DLRLFQAFLK VIEPVGNREE KILNREIGFA
IGMPICEFDL VKDSEVQDFR RNILNVCKEA VDLRDSNGSH SRALYVYPPN VESSAELPRH
IYNKLDKGQI IVVIWVIVSP SNDKQKYTLK INHDCVPEQV IAEAIRKKTR SMLLTQEQLK
MCVQEYQGKY ILKVCGCDEY LLEKYPLSQY KVFLCCDHGV RGWPFLLKYS KGPIILLQPH
TSNVACFWSR TSFGGMPLHR RSRISRDTQL FPAKAQGGYY WRTRKNLSGW SRLSSKTTVA
PLQDITVTEM DLELLDIEEE QVLLMEFEHC PLAWGNINLF DYTHTLVAGK MALNLWPVPH
GLEDLLNPIG VTGSNPNKET PCLELEFDHF SCPVKFPNMS QIEEHANWNI STELGFNYSH
NGSSNRFARD NPLTESDNEQ LRQVCNRDPL SEITEQEKDF LWRHRHHCIN IPDILPKILL
AVKWNSRDEV AQMYCLLKDW PAIRPEQAME LLDCNFPDPM IREFAVKCLE KYLTDDKLSQ
YLIQLVQVLK YEQYLDNPLA RFLLKKALTN QRIGHFFFWH LKSEMHNKTV SQRFGLLLES
YCRACGVYLK HLSRQVEAME KLINLTDLLK QEKKDEAQKV QMKFLVEQMK RPDYMDALQS
FTSPLNPAHQ LGNLRLEECR MMSSAKRPLW LNWENPDMMS ELLFQNNEII FKNGDDLRQD
MLTLQIIRIM ENIWQNQGLD LRMLPYGCLS IGDCVGLIEV VRNSHTIMQI QCKGGLKGAL
QFNSHALHQW LKDKNKGEMY DQAIDLFTRS CAGYCVATFI LGIGDRHNSN IMVKDDGQLF
HIDFGHFLDH KKKKFGYKRE RVPFVLTQDF LIVISKGTQE CTKTREFERF QEMCYKAYLA
IRQHANLFIN LFSMMLGSGM PELQSFDDIA YIRKTLALDK SEQEALDYFM KQMNDAHHGG
WTTKMDWIFH TIRQHAMN
//
