ID A0A3N0Y0Y0_ANAGA Unreviewed; 1078 AA.
AC A0A3N0Y0Y0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 18-JUN-2025, entry version 32.
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=DPX16_2088 {ECO:0000313|EMBL:ROL01519.1};
OS Anabarilius grahami (Kanglang fish) (Barilius grahami).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Xenocyprididae; Xenocypridinae; Xenocypridinae incertae sedis; Anabarilius.
OX NCBI_TaxID=495550 {ECO:0000313|EMBL:ROL01519.1, ECO:0000313|Proteomes:UP000281406};
RN [1] {ECO:0000313|EMBL:ROL01519.1, ECO:0000313|Proteomes:UP000281406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-KIZ {ECO:0000313|EMBL:ROL01519.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:ROL01519.1};
RA Jiang W.;
RT "Genome assembly for a Yunnan-Guizhou Plateau 3E fish, Anabarilius grahami
RT (Regan), and its evolutionary and genetic applications.";
RL Submitted (OCT-2018) 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 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:ROL01519.1}.
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DR EMBL; RJVU01054669; ROL01519.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N0Y0Y0; -.
DR OrthoDB; 67688at2759; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000281406; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA.
DR GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; IEA:TreeGrafter.
DR GO; GO:0005944; C:phosphatidylinositol 3-kinase complex, class IB; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:TreeGrafter.
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; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:TreeGrafter.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:TreeGrafter.
DR CDD; cd08398; C2_PI3K_class_I_alpha; 1.
DR CDD; cd00872; PI3Ka_I; 1.
DR FunFam; 1.10.1070.11:FF:000006; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 2.60.40.150:FF:000041; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 3.10.20.90:FF:000055; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 3.10.20.90:FF:000074; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 3.30.1010.10:FF:000007; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 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; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 2.
DR Gene3D; 3.30.1010.10; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 4; 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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR PANTHER; PTHR10048:SF95; PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE 3-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; 2.
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, ECO:0000313|EMBL:ROL01519.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000281406};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 16..105
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 187..289
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 332..489
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 518..718
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 774..1060
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1078 AA; 124552 MW; 9461E8B35F2622C9 CRC64;
MAPRPSSGEL WGLHLMPPRI LVDCCLPNGI LVSLECLREA PLTSIKQQLF SEARKYPLYH
LLQEESCYIF VGVTQEAERE EFYDETRRLC DLRLFHPILK VIEPLGNREE KILNREIGFA
IGMPICEFEL VKDPEVQDFR RNILSVCREA VEEREGGGAH TQALYVYPPN VESSPDLPQH
IYSKLDKGRL IVTIWVIVSP SNSKQKYTLK IAHDSLPEQL IAEAIRKKTR SMHLSAQQLR
LCVQEYQGQY ILKVCGCDEY FLEKYPLSQY KYIRSCITLA RLPHLMLVSK DSLYSQLPAS
GFMAPSYSRR TPQPSPCPGG GDPGSPRSLW AFNTHLRVRL LCATYVNVNI RDIDKIYVRT
GIYHGGEPLC DNVNTQRVPC SNPRWNEWLS YDIYLTDVPR SARLCLSICS VKGRKGAKEE
HCPLAWGNIN LFDYKDTLVS GKVALGLWPV PHGLEDLLNP IGVSGSNPNK ETPCVELEFP
WFNQTVVFPD EQQIEEHANW SISRELGYSY CLGLSSRLAC DSTISQADAE QLRVLCSRDP
LYELSEQEKD FLWRHRHYCV NIPESLPKLL LSVKWNSRDE VSQVRISIST QLYPSIRSSL
IRVCAQIYCL LKDWPLMQPE SALELLDCNF PDPMVREFAL RCLIQGLTDD KLSQYLLQLV
QVLKYEMYLD NPLARFLIKK ALTNQRIGHF FFWHLKSEMH NKTVSRRFGL LLEAFCRACG
MYLKHLNRQV EAMDKLVNLT DTLKQEKKDE TQKTQMKFLV EHMSRPDYME ALQGLEECRI
MSSAKRPLWL NWENPDIMSE LLFTNNEIIF KNGDDLRQDM LTLQIIKIME NIWQNQGLDL
RMLPYGCLSI GDCVGLIEVV KNSHTIMQIQ CKGGLKGALQ FNSNTLHHWI KEKNKGEAYD
RAIDLFTRSC AGYCVATFIL GIGDRHNSNI MVKENGQLFH IDFGHFLDHK KKKFGYKRER
VPFVLTQDFL IVISKGVQEC SKTKEFERFQ EMCYKAYLAI RQHASLFINL FSLLLGCGMP
ELQSFDDIAY LRKTLALEKN QQDALEYFTK QMNDAHHGGW TTKMDWIFHT IRHMPNEH
//
