ID A0A3P8YLC8_ESOLU Unreviewed; 1098 AA.
AC A0A3P8YLC8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010};
DE EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000017410.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000017410.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000017410.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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 AlphaFoldDB; A0A3P8YLC8; -.
DR Ensembl; ENSELUT00000026996.2; ENSELUP00000017410.2; ENSELUG00000017187.2.
DR GeneTree; ENSGT00940000156858; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000265140; LG23.
DR Bgee; ENSELUG00000017187; Expressed in head kidney and 14 other cell types or tissues.
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; 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:UP000265140};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 36..143
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 205..300
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 348..513
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 536..718
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 792..1075
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 518..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 126700 MW; C08ED8D09E8A6B78 CRC64;
MAKQVSDEDL HSVVHREENR RRRRKMKAFT STFSVIMDQI SIEFVLPTST KSSRSPDTLL
LEVAANWTVE QVKAQVWLRA VASNLCPEFY QKFSPDHCIL LYQKKGNWCE IYDKHQVFQT
LDCIRYWKAL KKDVGKIHLT CRPQPSEDSV RYQRYLNYLI GYDVTDVSNV HDDELEFTRR
KLFSPRRIEL SDRDPKLYSM DPWITSKPLP DISCLTVSTA SQTIKVSIDD TPVQVLQTFF
AKIANKRALL GIPDDMCEAD YVLRVCGREE YIYGNHPVRD FHWIRQCLKN GEEIHLVLES
APNPEQDQVQ REDWAQVDDC TGVAGTHEQL TIEEKDHERV FTISLWDCSR KFRVKVLGID
IPTLPRNPEL IVFVEASIFH GQQLLAQERT TSKAFTEEVL WNTWLEFNIR IRDLPKGSRL
SLQVNVLYHS VTPSLTRRHS LLTKSRLLYY VNLLLVDHRS LLRQGEFILH MWKMPEKTED
NSSVNADKLT SATNPDKASS MALAILLDKY CYPVALPKSR ESKEPGGDGR SAEGGERGLR
EMPNHLRKQF EAIIETDPLH HLSPEDKELL WHFRQECMRH PSAYPKLLSS VRWGRQEAVL
ATHRLLERST VWDRSPLDVG LAMQLLDCHY SDANVRSMAV RKLETLGDDD VLRYLLQLVQ
AVKFEPYHDS ALARFLLKRA LRSKRIGHFL FWFLRSEIAT SMHYQQRYAV LLEAYLRGCG
DDMLQDFRHQ VEMTEALQKV TREIKTMSAE KYDVSAQVVF QLRQKLENLQ TSGLPESFRV
PYDPGLRAGA LVIEQCKVMA SKKKPLWLQF KRADPTTRSS DTIGIIFKDG DDLRQDMLIL
QILLIMESIW EEESLDLSLL PYGCISTGNK IGMIEIVKDA TTIANIQQSV VGSTGAFKDE
ILNQWLQDKC VNEEKFQQAV ERFVFSCGGY CVATYVLGVG DRHNDNIMIT ESGNLFHIDF
GHILGNYKSF LGISKERVPF VLTPDFLYVM GTSGKKSSPH FLKFQDVCVR AYLALRHHTN
LLIILFSMML MTGMPQLTSK EDIEYIREAL TVGHPEEEAQ RHLLDQIEIC RDKGWTVQFN
WFLHLVLGIK QGVEKRSA
//
