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Database: UniProt/TrEMBL
Entry: Q4RVP5_TETNG
LinkDB: Q4RVP5_TETNG
Original site: Q4RVP5_TETNG 
ID   Q4RVP5_TETNG            Unreviewed;      1157 AA.
AC   Q4RVP5;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 136.
DE   RecName: Full=phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010};
DE            EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010};
GN   ORFNames=GSTENG00028231001 {ECO:0000313|EMBL:CAG07537.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|EMBL:CAG07537.1};
RN   [1] {ECO:0000313|EMBL:CAG07537.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|EMBL:CAG07537.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope;
RG   Whitehead Institute Centre for Genome Research;
RL   Submitted (FEB-2004) 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 CTNNBIP1 family.
CC       {ECO:0000256|ARBA:ARBA00006505}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00006209}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CAG07537.1}.
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DR   EMBL; CAAE01014991; CAG07537.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4RVP5; -.
DR   KEGG; tng:GSTEN00028231G001; -.
DR   UniPathway; UPA00220; -.
DR   GO; GO:0046934; F:1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008013; F:beta-catenin binding; IEA:InterPro.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd08693; C2_PI3K_class_I_beta_delta; 1.
DR   Gene3D; 3.10.20.770; -; 1.
DR   Gene3D; 1.10.10.490; Beta-catenin-interacting ICAT; 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; IPR009428; ICAT_dom.
DR   InterPro; IPR036911; ICAT_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; PF06384; ICAT; 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; SSF81730; beta-catenin-interacting protein ICAT; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          16..105
FT                   /note="PI3K-ABD"
FT                   /evidence="ECO:0000259|PROSITE:PS51544"
FT   DOMAIN          187..290
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          332..497
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          442..630
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          683..964
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          971..991
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1009..1034
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1157 AA;  131877 MW;  A2E7BC62C91DBF5D CRC64;
     MPPGKYGMQE EWEKEGDQRI MMDFLLPTGI FLKFPVSRND TIKIIKKMVW KNAQNEALYA
     ALGDPDAYVF TCINQTAERE ELEEESRRIS DVRPFMCFLR LVAREGDRVE KLTNTQISQL
     TGKGLHEFEA QKNHEVDEFR AKMRAFCEEK AQERQMLPWL EWMEYNFPCD LEPCCSPVDC
     GATKSKNTKI FINVKFEACD ESFMLQQDPQ DLPVALMKAA LKKKATVFRS VRQEPEDYTL
     QVNGRWEFIY GRHPLSQFKV SGHEHPYAQC PQYIFSCLRN GQNPHLTMVH HSTIRKHQEE
     QGHMCSQVYK GRSQSRPPPL PLKKNTSSLW SINEPFYIRL LHGSRVNAAE GMKLVVQAGL
     FHGSELLCKV VTSSEVAVCS EPVWDQRLEF DISVSDLPRM SRLCFALYAV IEKNKKPRGT
     KKKNKKAVGA FKVQLDCPIA WVNTMVFDYK DQLKTGEFLL STWPSVPDDK GDLLNPMGTV
     EKNPNVDSAA GLLIHFPNVR PHPLYYPSPE KILKQPQLLL FTFGACLCSL QHMKLKEIMD
     NKNYTEIFED EKELLWKLRD DELLQYLIQL VQVLKYESYL DCDLTTFLLE RALSNSRIGH
     FLFWHLNLML EAYCRGNIWH IKLLIKQNEA LLKMKTLSDI VKTGSQKMTV DDLKLCIKQE
     SYVETLSDLL SPLNPSVFLA EICADKCRFM DSKMKPLWLM YKSPWAQGDM MGIIFKNGDD
     LRQDMLTLQM IRLMENLWKK EGLDLRMIPY GCLSTGDKMG LIEVVKNSDT IANIQRNSSN
     SAATAAFNKD ALLNWLKSKN PEGKLEKAIE EFTLSCAGYC VATYVLGIGD RHNDNIMIRE
     TGQLFHIDFG HFLGNFKRKL GINRERVPFI LTYDFVHVIQ QGRTNNSEKF ERFREYCERA
     YKILCRNGML FVNLFAMMKA AGLPELTSSK DIQYLKDSLA LGKSEEEALK NFKVKFNEAL
     RESWKTKVFP KNQAATVGPT APPAAAGGTE PPAGRAALVL RSSADWRDVT PEQDASFSNT
     PFKRSTEERK PGPGGMLAVP GLVSSVCAAA PPNHRSSQYR EVMHIQCACI ITINVGRATG
     EAGMNREEAP GKSPEDMYIQ QKVRVLLMLK KMGSNLTPSE EAFLRNYAGV VHSQMSQLPQ
     HNIDQGKALK VPQVCTA
//
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