ID W5MA77_LEPOC Unreviewed; 1074 AA.
AC W5MA77;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=PIK3CB {ECO:0000313|Ensembl:ENSLOCP00000005286.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000005286.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000005286.1}
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 EMBL; AHAT01029706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MA77; -.
DR STRING; 7918.ENSLOCP00000005286; -.
DR Ensembl; ENSLOCT00000005294.1; ENSLOCP00000005286.1; ENSLOCG00000004421.1.
DR eggNOG; KOG0904; Eukaryota.
DR GeneTree; ENSGT00940000157522; -.
DR HOGENOM; CLU_002191_1_3_1; -.
DR InParanoid; W5MA77; -.
DR OMA; KGCKQHV; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000018468; Linkage group LG14.
DR Bgee; ENSLOCG00000004421; Expressed in mesonephros and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:GO_Central.
DR GO; GO:0046934; F:1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IBA:GO_Central.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08693; C2_PI3K_class_I_beta_delta; 1.
DR CDD; cd00872; PI3Ka_I; 1.
DR CDD; cd05173; PI3Kc_IA_beta; 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; IPR037702; PI3Kbeta_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF33; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT BETA 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; 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; 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:UP000018468};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 24..113
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 188..279
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 326..493
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 522..699
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 776..1057
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1074 AA; 123027 MW; 1F43972B52329052 CRC64;
LFPTMPPAVM DTLDIWAVDS QLTNDVCVAV DFLLPTGIYI QMDVPREATI QHIKLLLWKQ
AQSYPLFSFL GEMESYMFEC VNQSAVHEEL EDETRRLCDV RPFLPVLKLV TRNCGRAEKL
LDSKIGVLIG KGLHELDALQ DPEVKDFRTK MFRISEDKMQ KLQMMTWMEW LQCYFSPVLD
STVPDGIQDK LNVTMHFSHS QDTASLAISP YMTPNDLTEQ AVKKWLTTHR SEEEVNSSEY
VLRVSTRLEF LFGEHPLIHY KYVKTCMMCN ESPHLTLVEC STVKEMFEKE ISAVGTVVNR
KSSNPPFPLP PKKRGVSQIS TCVWDVAEPF RITLIKGSKV NAEETVKVQV RAGLFHGTEL
LCKPAVSSET CGKNEHVWNK TLEFDINVCD MPRMTRLCFA VYAVMDKVKK QKSTKNIHAT
KYQTIRKAGK VHYPIAWVNT MVFDYRGQLK TGELILHGWS SFPDELEEML NPIGTVQTNP
YTENATALHI HFHECTKSAV IYPPFDKILE KAAEIARGSD CMPMVSRGSK KFHIELKEIM
ERDPLSQLCE NEKDLIWTLR YDCRENFPQS LPKLLLSVKW NKHEDMAQLQ ALLQIWPKLS
PRDALELLDF NYPDQYVREY AVNCLRDMSD EELSQYLLQL VQVLRYEPYY DCALSRFLLE
RAQANRKIGH FLFWHLRSEI HMPAVSVQFS LILEAYCRGS IPHIEVLKKQ VEALCKLKAV
NELIKLGTLK NARNKTKEAM LTKEAMMTCL RQTGFAETLS DLQSPLNPSI LLSGIHVERC
RYMDSKMKPL WVVYNNKLLA GDTLGIIFKN GDDLRQDMLT LQILRLMDML WKEANLDLRI
VPYGCLATGD RTGLIEVVSA SETIANIQLT SSNVAATAAF NKDALLNWLK EKNSGDALDR
AIEEFTLSCA GYCVATYVLG IGDRHSDNIM VRSTGQLFHI DFGHILGNFK SKFGIKRERV
PFILTYDFIH VIQQGKTGNT EKFGRFRQCC EDAYLILRKN GNLFITLFAL MLTAGLPELT
SVKDIQYLKD SLALGKTDED ALKQFRQKFD EALRESWTTK VNWMAHNVAK DNRS
//
