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Database: UniProt
Entry: A0A087VDW5_BALRE
LinkDB: A0A087VDW5_BALRE
Original site: A0A087VDW5_BALRE 
ID   A0A087VDW5_BALRE        Unreviewed;      1106 AA.
AC   A0A087VDW5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 60.
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=N312_05194 {ECO:0000313|EMBL:KFO10807.1};
OS   Balearica regulorum gibbericeps (East African grey crowned-crane).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX   NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO10807.1, ECO:0000313|Proteomes:UP000053309};
RN   [1] {ECO:0000313|EMBL:KFO10807.1, ECO:0000313|Proteomes:UP000053309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO10807.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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}.
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DR   EMBL; KL489669; KFO10807.1; -; Genomic_DNA.
DR   RefSeq; XP_010300615.1; XM_010302313.1.
DR   AlphaFoldDB; A0A087VDW5; -.
DR   GeneID; 104635481; -.
DR   KEGG; breg:104635481; -.
DR   CTD; 5294; -.
DR   OrthoDB; 10350at2759; -.
DR   UniPathway; UPA00220; -.
DR   Proteomes; UP000053309; Unassembled WGS sequence.
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, ECO:0000313|EMBL:KFO10807.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053309};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          34..141
FT                   /note="PI3K-ABD"
FT                   /evidence="ECO:0000259|PROSITE:PS51544"
FT   DOMAIN          217..309
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          357..524
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          544..726
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          800..1083
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1106 AA;  128138 MW;  614C66FF1AEA2A9B CRC64;
     MELGDYEQPV VMREENKRRR RRMKPHCTSS NLSSMELISI EFILPTSNKH TKVPEMMLLE
     IAGNCTVEQM KAQIWMRAIE MSQTADFYHT FTPDQFILQY QKKGQWYEIY DKHQVLQTLD
     CILYWKVLQK KVGKIYVVQK QKPSEEVQEF QRQLNNLIGY DVTDVSNVHD DELEFTRRRL
     VTPRMIEVAC RDPKLYAMHP WTTSKPLPEY LFKKITNNNI FIIIHRGTTS QKIKVSIDDT
     PDMILHSFFT KMAKKKSLMD IPEDHSELDF VLRICGRDEY ITGETPIKDF HWIRQCLKNG
     EEIHLVLDNP PDPNEDEVQK EEWPLVDDCT GVTGYHEQLT IDGKDHERVF TISLWDCNRK
     FRVKIIGIDI PVLPRNTDLT VFVEANIQHG QQLLSQRRTS SKPFTEEVLW NIWLEFDIKI
     KDLPKGALLN LQIYCGKTQG LSTKTNLQSH ESPNSDSKCK TQLLYYVNLL LIDHRFLLRS
     GEYVLHMWKI PGKGEEQGSI NADKLTSATN PDKENSMAIS IVLDKYCHPI ALPKHRITSD
     PQGDRTRAEM PNQLRKQLEE IIATDPLNPL SPEDKELLWH FRYESIKHPK AYPKLLSSVK
     WGQQEIVAKT YQLLAKKEVW DQSTLDVGLT MQLLDCNFSD ENVRAMAVQK LESLEDDDVL
     HYLLQLVQAV KFEPYHDSAL ARFLLKRGLR NKRIGHFLFW FLRSEIAQSM HYQQRFAVIL
     EAYLRGCGKA MLHDFMKQVQ VIELLHKVTM EIKSVSAEKY DVTSQVIAQL RQKLEKLQSS
     KLPESFRVPY DPGLRAGALV IEKCKVMASK KKPLWLEFKC ADPTALSNET IGIIFKHGDD
     LRQDMLILQI LRIMESIWEA ESLDLCLLPY GCISTGNKIG MIEIVKDATT IAKIQQSTVG
     NTGAFKDEIL NQWLKERCMI EEKFQAAVER FVYSCAGYCV ATFVLGIGDR HNDNIMITET
     GNLFHIDFGH ILGNYKSFLG INKERVPFVL TPDFLFVMGT SGKKTSLHFH KFQDVCVKAY
     LALRHHTNLL IILFSMMLMT GMPQLTSKED IEYIRDALTV GKSEEDAKKY FLDQIEVCRD
     KGWTVQFNWF LHLVLGIKQG VEKHSA
//
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