ID A0A091DHH0_FUKDA Unreviewed; 1045 AA.
AC A0A091DHH0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=H920_06965 {ECO:0000313|EMBL:KFO31579.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO31579.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO31579.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO31579.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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; KN122257; KFO31579.1; -; Genomic_DNA.
DR RefSeq; XP_010626365.1; XM_010628063.2.
DR AlphaFoldDB; A0A091DHH0; -.
DR STRING; 885580.ENSFDAP00000012960; -.
DR Ensembl; ENSFDAT00000025705; ENSFDAP00000012960; ENSFDAG00000020275.
DR GeneID; 104864846; -.
DR CTD; 5293; -.
DR eggNOG; KOG0904; Eukaryota.
DR OMA; CCEPQIT; -.
DR OrthoDB; 10350at2759; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:InterPro.
DR GO; GO:0046934; F:1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08693; C2_PI3K_class_I_beta_delta; 1.
DR CDD; cd05174; PI3Kc_IA_delta; 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; IPR037703; PI3Kdelta_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF35; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT DELTA ISOFORM; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL 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; 1.
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:KFO31579.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 16..105
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 187..278
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 319..476
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 498..675
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 746..1028
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 287..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1045 AA; 119849 MW; 9E025BA2FF99B69E CRC64;
MPPGVDCPME FWTEEENQNV VVDFLLPTGV YLNFPVSLNA NLSTIKQVLW HRAQYEPLFH
MLSGPEAYVF TCVNQTAEQQ ELEDEQRRLC DVRPFLPVLR VVAREGDRVK KLINSQISLL
IGKGLHEFDS LGDPEVNDFR AKMRQFCEEA AARRQQLGWE DWLQYSFPLQ LEPSARSWGP
GTLRVPNRAL LVNVKFEGSE ESFTFQVSTK DTPLALMACA LRKKATVFRQ PLVEQPEDYA
LQVNGRHEYL YGSYPLCQFQ YICSCLHNGL TPHLTMLHSS SILAMREEQG NPTSQVQKPR
PKPPPIPTKK PSSVSLWSLE QPFCIELIQG SKVNADERMK LVVQAGLFHG HEMLCKTVSS
LEVSVCSEPL WKQRLEFDIS ICDLPRMARL CFALYAVVEK AKKARSTKKK SKKADCPIAW
ANIMLFDYRD QLKTGERRLY MWPSVPDEKG ELLNPAGTVH GNPNTESAAA LVICLPEVAP
HPVYYPTLEK ILELGRHGEQ HGRITEEEQV QLREILERRG SSELYEHEKD LVWKMRHEVQ
EHFPDALSRL LLVTKWHKHE DVAQMLYLLC SWPELPVLSA LELLDFSFPD CHVGSFAIKS
LRKLTDDELF QYLLQLVQVL KYESYLDCEL TKFLLDRALA NRKIGHFLFW HLRSEMHVPS
VALRFGLIME AYCRGSTHHM KVLMKQGEAL SKLKALNDFV KVSSQKTTKP QTKELMHLCM
RQETYLEALS HLQSPLDPST LLEEVCVEQC TFMDSKMKPL WIMYSSEEAG TAGSVGIIFK
NGDDLRQDML TLQMIQLMDV LWKQEGLDLR MTPYGCLPTG DRTGLIEVVL HSDTIANIQL
NKSNMAATAA FNKDALLNWL KSKNPGEALE RAIEEFTLSC AGYCVATYVL GIGDRHSDNI
MIRESGQLFH IDFGHFLGNF KTKFGINRER VPFILTYDFV HVIQQGKTNN SEKFERFRGY
CERAYTILRR HGLLFLHLFA LMRAAGLPEL SCSKDIQYLK DSLALGKTEE EALKHFRVKF
NEALRESWKT KVNWLAHNVS KDNRQ
//
