ID A0A1L8GTX9_XENLA Unreviewed; 1115 AA.
AC A0A1L8GTX9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=pik3cg.S {ECO:0000313|RefSeq:XP_018111272.1,
GN ECO:0000313|Xenbase:XB-GENE-6487000};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018111272.1};
RN [1] {ECO:0000313|RefSeq:XP_018111272.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018111272.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018111272.1};
RG RefSeq;
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 RefSeq; XP_018111272.1; XM_018255783.2.
DR AlphaFoldDB; A0A1L8GTX9; -.
DR STRING; 8355.A0A1L8GTX9; -.
DR MaxQB; A0A1L8GTX9; -.
DR PaxDb; 8355-A0A1L8GTX9; -.
DR GeneID; 108713077; -.
DR KEGG; xla:108713077; -.
DR AGR; Xenbase:XB-GENE-6487000; -.
DR CTD; 108713077; -.
DR Xenbase; XB-GENE-6487000; pik3cg.S.
DR OMA; WDCDRRF; -.
DR OrthoDB; 10350at2759; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 108713077; Expressed in spleen and 18 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; 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; 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:UP000186698};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 39..146
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 222..314
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 362..529
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 549..731
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 809..1092
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1115 AA; 128766 MW; 9F0067C94B124FDD CRC64;
MLSSGMELDN YEQPVVLRDE NQRRRRRMRP HSATTSVFSM DLIPIEFIMP TINRCSKVQE
TMLLEVAGNC SVEQMKAQVW MHAIEKSHNS DFYQRLTPDQ FLLQYQKKGQ WYEIYDKHQV
IQTLDCIMYW KVLQKTVGKI HIVQKEKTPE EMIEYQKTLN YLIGYDVTDV SNVHDDELEF
TRRRLVTPRM IELSRRDARL YSMDPWVTSK PLPEYLCQRI TSNSIFIIIH KGMTSHTIRV
SIDDTPDVIL HSFFTKMAKK KSLLEISEEN SELDFVLRVC GRDEYIIGNA PIKDFHWIRQ
CIKNGQEIHL VLEKPPNALK DDVQKEEWPL VDDCTGVTGY HEQLTIEGKD HEKIFTISLW
DCNRKFRVKI IGIDIPVLPK NTEIIVFVEA NIQHGQQVLS QRRTTCKPFT EEVLWNSWLE
FDLKIKDLPK GALLNLQIFC GKAPNVSIKS NALSPESAAS DSKFKNQLLY YVNLLLIDHR
FLLRQGEYVL HMWKIPGKGE EQGSINADKL TSATNPDKET SMAISISLDK YCHPVALPKH
KLVSDPELER PRTEMPNQLR KQLEEIIATD PLHPLTPEDK ELLWHFRSEI IKHPEAYPKL
LSSVKWGQQE MVAKTYQLLS KREAWDDCIL DVGLTIQLLD CNFSDENVRA MAVQKLESLQ
DDDVLHYLLQ LVQAVKFEPY HDSALSRFLV KRALQSKRIG HFLFWFLRSE IAQSMHYQQR
FAVILEAYLR GCGKAMLDDF TKQVQVTEIL HKVTMEIKSV SAEKYDVTSQ VITQLRQKLE
KLQNAKHPDK LPDSFRVPYD PGLRAGSLVV EKCKVMASKK KPLWLEFKCS DTTALSNETI
GIIFKHGDDL RQDMLILQIL RIMGSIWEAE SLDLYLLPYG CISTGNKIGM IEIVKDATTI
AQIQQSTVGN TGAFKDEVLS QWLKEKCPIE EKFSAAVERF VYSCAGYCVA TFVLGIGDRH
NDNIMVTESG NLFHIDFGHI LGNYKSFLGI NKERVPFVLT PDFLYVMGTS GKKTSQYFNT
FQDVCVKAYL ALRHHTNLMI ILFSMMLMTG MPQLTSKEDI EYIRDSLTVG KNDESAKKHF
LDQIEVCRDK GWTVQFNWFL HLVLGIKQGV EKHSA
//
