ID A0A3Q1DDN4_AMPOC Unreviewed; 1123 AA.
AC A0A3Q1DDN4;
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};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000029421.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000029421.1}
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 STRING; 80972.ENSAOCP00000029421; -.
DR Ensembl; ENSAOCT00000023521.1; ENSAOCP00000029421.1; ENSAOCG00000002034.1.
DR Ensembl; ENSAOCT00000031670.1; ENSAOCP00000014980.1; ENSAOCG00000002034.1.
DR GeneTree; ENSGT00940000156858; -.
DR OMA; WDCDRRF; -.
DR OrthoDB; 10350at2759; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000257160; 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 Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 37..138
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 220..312
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 360..537
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 561..743
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 817..1100
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 128905 MW; E2498286FAD89B76 CRC64;
MDGQQIQVSD EEPEVLREES RRRRRRKKAI TSSPCTSMDQ ISVEFVLPTV ARGGNGPDSL
LLEVAGNWTV EQVKAQVWLK AVTLNLCPDF YQQFSPDHCI LLYQKKGNVC EIYDKHQVFQ
TLDCIRYWRA LKKDVGRIQL VPRPQPSEES QQYQNYLNCL IGYDVTDVSN VHDDELEFTR
RKLLTPRRIE LSDRDPKLYS MDPWVTRKPL HEHLRTKINN SHILVVIHIS TASQTIKVSI
DDTPTQVLAS FFAKTANKRV LLGIPENKCE TDFVLRVCGR EEYLYGEKPL QNFNWVRQCL
KNGEEIHLVL ETPPDPELDL VQKEDWAQVD DCTGVAGTHE QLTIDEKDHE RVFTISMWDC
NRKFRVKVLG IDIPSLPKVP EFVVFIEASI FHGQQLLAQE RTTSKSFNEE VLWNCWLEFN
IKIKDLPKGA RLNLQVICGK QPQTSNSKGG YYQDNTAGTS SLDGKTKSRL LYYVNLLLID
HRSLLRQGEF ILHMWKMPEK SEESSSSINA DKLTSATNPD KASSMAIAIL LDKYCYPVVL
PKSRDVGRDY GAAGEEAEGG ERGQREMPNH LKKQFEAIVA TDPLHPLSPE DKELLWHFRH
ECMRDPRAYP KLLGSVRWGK QEDVLATHRL LERSSAWDTS GLDVGLAMQL LDCHYSDAQV
RSMAVRKLET LEDDDVLRYL LQLVQAVKFE PYHDSALVRF LLKRALRSKR IGHFLFWFLR
SEIAQSMHYQ QRYAVLLEAY LRGCGENMLQ DFRKQVEMTE ALQKVTCEIK AMSDDKYHVT
AQVVFQLRQK LETLQASGLP ESFRVPYDPG LRAGVLLIEQ CKVMASKKKP LWLQFKRADP
TTLSKDPIGI IFKDGDDLRQ DMLILQILLI MESIWETESL DLCLLPYGCI STGNRIGMIE
IVKDATTIAN IQQSVVGSTG AFKDELLCQW LRDKCVSEEK FQQAVERFLF SCGGYCVATY
VLGIGDRHND NIMITESGNL FHIDFGHILG NYKSFMGISK EWVPFVLTPD FLYVMGTSGK
KSSPHFQKFQ DVCVKAYLAL RHHTNLLIIL FSMMLMTGMP QLTSKEDIEY IREALTVGRS
EDDAQRHLLD QIEICREKGW MVQVNWFVHL VLGIKQGVEK RST
//
