ID A0A3B4C1H7_PYGNA Unreviewed; 1667 AA.
AC A0A3B4C1H7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 alpha {ECO:0000313|Ensembl:ENSPNAP00000004810.1};
GN Name=PIK3C2A {ECO:0000313|Ensembl:ENSPNAP00000004810.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000004810.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000004810.1}
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-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000256|ARBA:ARBA00023985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000256|ARBA:ARBA00023985};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR Ensembl; ENSPNAT00000006443.1; ENSPNAP00000004810.1; ENSPNAG00000011238.1.
DR GeneTree; ENSGT00940000157813; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
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; cd04012; C2A_PI3K_class_II; 1.
DR CDD; cd08381; C2B_PI3K_class_II; 1.
DR CDD; cd07289; PX_PI3K_C2_alpha; 1.
DR Gene3D; 3.10.20.770; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
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 Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000008; C2_dom.
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; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR042133; PX_PI3K_C2_alpha.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF28; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 3-KINASE C2 DOMAIN-CONTAINING SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00168; C2; 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; PF00787; PX; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50004; C2; 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; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 438..526
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 669..827
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 846..1024
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1092..1370
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1409..1525
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1540..1659
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1667 AA; 187325 MW; 9FC5CC8202F2C757 CRC64;
MAQISSGNGY KLDRPSSPLG ARPKGVVGKE EALRMEAEAL AKLQREKRHT LPVPASSTKA
LPNTAASTAS TSRPEKDLIV FPESEAKKKE EKDAFADIDV EKLTNAELEK LLLDDNFGAS
KMTRPSSLLG CNLSASYPGG QAFSPSPFHW TPTLSTPSNS ALSTPTHPQA SVFPSAPFPK
PPCSFQNGFT PAMPPFVHLP AQQAPFLSFP HIQPPRPLVF QQPTVTPEMA KLFDKIASTS
EYLRNGKSSS LDADSTSMKS LEPVPQPPEP TSISRFDWLD LDPLSKRRVE VEEAPSAQGE
AVMEESAPAG DPWDAVLRDE TEVTGSNSPS AQVKDQHIVT SQQRRASTGT AVTRSHSLNI
PATSSHHNQS KQVSKGSGNI VTKYATLQGK EAQNLEVVAF CEDIAKLRSK FTHDDFSTNP
GYVISPVISQ RDIGGDRNSS VKVSIEISDS QQPVTFTCDV SSPVELLIMQ ALCWVHDDLS
QVDIGSYILK VCGQEEVLQN KHSLGSHEYV QNCRKWETEI KLQLLAQSTM RRDLARTVDD
DTSPIDLEKY LDHIERPFKE TSTQYKTVDQ VLQAVKKLCS ALGEVETPAI TDAVKRLKHS
VNLPKSRTPE YCFLFIDCSS PVEERMEALT NAVYDLAMLY LRSFCLASPD HVKQDPTEDE
RESKEASGTT EHVQFTVYAI HGISTAWVSS YEKYYLMCAL THNGRNLFKP VQSKKVGTYK
SFFYHIKWDE LINFPISVAL LPLETMLSLT LYGVLNQNAS NSPDSNKQRK GPELLGKVTM
PLFDFRRVLS RGTKLLNLWM TPQSSPSGAA GKRMNLAERI ILQVDFPSPA VDVLYVGPQE
TKCPDPQALE TPDPDIKRKI EKLCDHTLLS SHRLTRADKQ LLWDHRHHCR GYEHSLPKIL
SSAPSWDWGS MAEIHALLHH WSPLSPVSAL ELLDSKFADT EVRSMAVSWI ESCSDDELTD
YLPQLVQALK FESHLKNSLV IFLLSRAEGN INIAHYLYWL LKDAVQDPAF GQRYSHVLGA
LLCLCSARLR AELEKQTQLV HLLGALAEKV RQASSSNRQV VLQEGLERVQ SYFQRNNCRL
PLSPSLVAKE LNVKACSFFN SNAVPLKLAL VNADQLGEEI NVMFKAGEDL RQDMLALQMI
RIMDRIWLQE GLDLRIVNFK CISTGKDKGM VELVSSSETL RKIQVEYGVT GSFKDKPLAE
WLRKYNPAED EYEKASENFI YSCAGCCVAT YLLGICDRHN DNIMLRTTGH MFHIDFGKFL
GHAQMIGSFK RDRAPFVLTS DMAYVINGGE RPTSRFQLFI DLCSQAYNLI RKHSSLFLNL
LSLMTQSGLP ELTGAQDLKY VYDALQPQTT DAEATVFFTR LIESSLGSVA TKFNFFIHNL
AQLRFSGLPS NDEPILSFSP RTYTLKQDGR IRDAFVYSFQ KRYNPDKHYT YVVRVLREGQ
NEPQFVFRTF DEFQELHNKL TILFPLWKLP GFPNKMVLGR THIKDVASKR KVELNSYVHS
LMRSSTEVSQ CDLVYTFFHP IARDDKTEGL DGLPKIPGRV EGEVKLSVSY RNSTLFIMVM
HIKDLVSDDG TDPNPYVKTY LLPDPHKTSK RKTKISRKTR NPTFNEMLVY SGYSKETLKQ
RELQLSVLSA ESLRENCYLG GITLSLKDFD LSQETVKWYK LTAVPYF
//
