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
//