ID B4DG55_HUMAN Unreviewed; 1306 AA.
AC B4DG55;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=cDNA FLJ53905, highly similar to Phosphatidylinositol-4-phosphate 3-kinase C2domain-containing alpha polypeptide {ECO:0000313|EMBL:BAG57666.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG57666.1};
RN [1] {ECO:0000313|EMBL:BAG57666.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Amygdala {ECO:0000313|EMBL:BAG57666.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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 EMBL; AK294416; BAG57666.1; -; mRNA.
DR RefSeq; NP_001308309.1; NM_001321380.1.
DR PeptideAtlas; B4DG55; -.
DR DNASU; 5286; -.
DR GeneID; 5286; -.
DR CTD; 5286; -.
DR OrthoDB; 10350at2759; -.
DR BioGRID-ORCS; 5286; 19 hits in 1172 CRISPR screens.
DR GenomeRNAi; 5286; -.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:InterPro.
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: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; cd00869; PI3Ka_II; 1.
DR CDD; cd05176; PI3Kc_C2_alpha; 1.
DR CDD; cd07289; PX_PI3K_C2_alpha; 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; IPR037705; PI3K-C2-alpha_dom.
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; 2.
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 2: Evidence at transcript level;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAG57666.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 41..129
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 302..461
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 481..657
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 725..1003
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1042..1158
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1175..1298
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 238..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1306 AA; 148375 MW; C52FECFB0957796C CRC64;
MAAFCRSITK LKTKFPYTNH RTNPGYLLSP VTAQRNICGE NASVKVSIDI EGFQLPVTFT
CDVSSTVEII IMQALCWVHD DLNQVDVGSY VLKVCGQEEV LQNNHCLGSH EHIQNCRKWD
TEIRLQLLTF SAMCQNLART AEDDETPVDL NKHLYQIEKP CKEAMTRHPV EELLDSYHNQ
VELALQIENQ HRAVDQVIKA VRKICSALDG VETLAITESV KKLKRAVNLP RSKTADVTSL
FGGEDTSRSS TRGSLNPENP VQVSINQLTA AIYDLLRLHA NSGRSPTDCA QSSKSVKEAW
TTTEQLQFTI FAAHGISSNW VSNYEKYYLI CSLSHNGKDL FKPIQSKKVG TYKNFFYLIK
WDELIIFPIQ ISQLPLESVL HLTLFGILNQ SSGSSPDSNK QRKGPEALGK VSLPLFDFKR
FLTCGTKLLY LWTSSHTNSV PGTVTKKGYV MERIVLQVDF PSPAFDIIYT TPQVDRSIIQ
QHNLETLEND IKGKLLDILH KDSSLGLSKE DKAFLWEKRY YCFKHPNCLP KILASAPNWK
WVNLAKTYSL LHQWPALYPL IALELLDSKF ADQEVRSLAV TWIEAISDDE LTDLLPQFVQ
ALKYEIYLNS SLVQFLLSRA LGNIQIAHNL YWLLKDALHD VQFSTRYEHV LGALLSVGGK
RLREELLKQT KLVQLLGGVA EKVRQASGSA RQVVLQRSME RVQSFFQKNK CRLPLKPSLV
AKELNIKSCS FFSSNAVPLK VTMVNADPMG EEINVMFKVG EDLRQDMLAL QMIKIMDKIW
LKEGLDLRMV IFKCLSTGRD RGMVELVPAS DTLRKIQVEY GVTGSFKDKP LAEWLRKYNP
SEEEYEKASE NFIYSCAGCC VATYVLGICD RHNDNIMLRS TGHMFHIDFG KFLGHAQMFG
SFKRDRAPFV LTSDMAYVIN GGEKPTIRFQ LFVDLCCQAY NLIRKQTNLF LNLLSLMIPS
GLPELTSIQD LKYVRDALQP QTTDAEATIF FTRLIESSLG SIATKFNFFI HNLAQLRFSG
LPSNDEPILS FSPKTYSFRQ DGRIKEVSVF TYHKKYNPDK HYIYVVRILR EGQIEPSFVF
RTFDEFQELH NKLSIIFPLW KLPGFPNRMV LGRTHIKDVA AKRKIELNSY LQSLMNASTD
VAECDLVCTF FHPLLRDEKA EGIARSADAG SFSPTPGQIG GAVKLSISYR NGTLFIMVMH
IKDLVTEDGA DPNPYVKTYL PPDNHKTSKR KTKISRKTRN PTFNEMLVYS GYSKETLRQR
ELQLSVLSAE SLRENFFLGG VTLPLKDFNL SKETVKWYQL TAATYL
//
