ID A0A3B4XYX8_SERLL Unreviewed; 1085 AA.
AC A0A3B4XYX8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010};
DE EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000022162.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000022162.1}
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}.
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DR AlphaFoldDB; A0A3B4XYX8; -.
DR STRING; 1841481.ENSSLDP00000022162; -.
DR Ensembl; ENSSLDT00000022882.1; ENSSLDP00000022162.1; ENSSLDG00000017243.1.
DR GeneTree; ENSGT00940000156858; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000261360; Unplaced.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 26..127
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 209..301
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 349..508
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 523..705
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 779..1062
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1085 AA; 124973 MW; C4F0FC19EA7A060C CRC64;
MKPKVLREDT RRRRRKKAIT SPSGTSMDQI TVEFVLPTVA RGGSGPDSLL LEVAGNWTVE
QVKAQVWLKA VTSNLCPEFY QRFSPDHCIL LYQKKGNVCE IYDKHQVFQT LDCIRYWRAL
KKDVGRIQLV PRPQPSDESL QYQRYLNYLI GYDVTDVSNV HDDELEFTRR KLLTPRRIEL
SDRDPKLYSM DPWVTRKLLP EHLLSKVSNG HILVVIHITT ASQTIKVSID DTPAQVLASF
FAKTANKRPL LGIPENMCEA DYVLRVCGRE EYLYGDKPLQ NFNWIRQCLK NGEEIHLVLE
MPPDPDQDLV QREDWAQVDD CTGVAGTHEQ LTIDEKDHER VFTISMWDCN RKFRVKVLGI
DIPSLPKIPE FIVFIEASIF HGQQLLAQER TTSKTFNEEV LWNCWLEFNI KIKDLPKGAR
LNLQAYLCLF VLVSGKTKSR LLYYVNLLLI DHRSLLRQGE FILHMWKMPE KSEESSSSIN
ADKLTSATNP DKASSMAIAI LLDKYCYPVV LPKSRDVSRD VSRDAVREMP NHLKKQFGAI
VATDPLHPLS PEDKELLWHF RQECMRDPRA YPKLLGSVRW GKQEDVLATH RLLERSSAWD
SSGLDVGLAM QLLDCHYSDA QVRSMAVRKL ETLEDDDVLR YLLQLVQAVK FEPYHDSALV
RFLLKRALRS KRIGHFLFWF LRSEIAQSMH YQQRYAVLLE AYLRGCGEAM LQDYRKQVEM
TEALQKVTRE MKAMSADKYD VTAQVVFQLR QKLETLQLSG LPESFRVPYD PGLRAGALLI
EQCKVMASKK KPLWLQFKRA DPTTLSKDPI GIIFKDGDDL RQDMLILQIL LIMESIWETE
SLDLCLLPYG CISTGNRIGM IEIVKDATTI ANIQQSVVGS TGAFKDEILY QWLRDKCVSE
DKFQQAVERF LYSCGGYCVA TYVLGIGDRH NDNIMITESG NLFHIDFGHI LGNYKSFMGI
SKEWVPFVLT PDFLYVMGTS GKKSSPHFQK FQDVCVKAYL ALRHHTNLLI ILFSMMLMTG
MPQLTSKEDI EYIREALTVG RSEDDAQRHL LDQIEICREK GWMVQINWFV HLVLGIKQGV
EKRST
//
