ID H2N969_PONAB Unreviewed; 1068 AA.
AC H2N969; A0A2J8US95;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010};
DE EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010};
GN Name=PIK3CD {ECO:0000313|Ensembl:ENSPPYP00000002213.3};
GN ORFNames=CR201_G0025751 {ECO:0000313|EMBL:PNJ48148.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000002213.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000002213.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ48148.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ48148.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000002213.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; NDHI03003447; PNJ48148.1; -; Genomic_DNA.
DR Ensembl; ENSPPYT00000002280.3; ENSPPYP00000002213.3; ENSPPYG00000001909.3.
DR eggNOG; KOG0904; Eukaryota.
DR GeneTree; ENSGT00940000159079; -.
DR HOGENOM; CLU_002191_1_3_1; -.
DR OMA; CCEPQIT; -.
DR TreeFam; TF102031; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0038089; P:positive regulation of cell migration by vascular endothelial growth factor signaling pathway; IEA:Ensembl.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:1905278; P:positive regulation of epithelial tube formation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0033031; P:positive regulation of neutrophil apoptotic process; IEA:Ensembl.
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};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
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 284..441
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 521..698
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 769..1051
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1068 AA; 121792 MW; 473D9BA48A72484F CRC64;
MPPGVDCPME FWTKEENQSV VVDFLLPTGV YLNFPVSRNA NLSTIKQLLW HRAQYEPLFH
MLSGPEAYVF TCINQTAEQQ ELEDEQRRLC DVQPFLPVLR LVAREGDRVK KLINSQISLL
IGKGLHEFDS LCDPEVNDFR AKMCQFCEEA AARRQQLGWE AWLQYSFPLQ LEPSARTWGP
GTLRLPNRAL LVNVKFEGSE ESFTFQVSTK DVPLALMACA LRKKATVFRQ PLVEQPEDYT
LQVNGRHEYL YGSYPLCQFQ VQKPRAKPPP IPAKKPSSVS LWSLEQPFCI ELIQGSKVNA
DERMKLVVQA GLFHGNEMLC KTVSSSEVSV CSEPVWKQRL EFDINICDLP RMARLCFALY
AVIEKAKKAR STKKKSKKAD CPIAWANLML FDYKDQLKTG ERCLYMWPSV PDEKGELLNP
TGTVRSNPNM DSAAALLICL PEVAPHPVYY PALEKLLGGM LLASRGWRPE LLWMCLHAQD
SAPSRTIGVA MPCLGVLPRL VQAPGDAECS CLLQILELGR HSECVHVTEE EQLQLREILE
RRGSGELYEH EKDLVWKLRH EVQEHFPEAL ARLLLVTKWN KHEDVAQDAL PAVSWPELPV
LSALELLDFS FPDCHVGSFA IKSLRKLTDD ELFQYLLQLV QVLKYESYLD CELTKFLLDR
ALANRKIGHF LFWHLRSEMH VPSVALRFGL ILEAYCRGST HHMKVLMKQG EALSKLKALN
DFVKLSSQKT PKPQTKELMH LCMRQEAYLE ALSHLQSPLD PSTLLAEVCV EQCTFMDSKM
KPLWIMYSNE EAGSGGSVGI IFKNGDDLRQ DMLTLQMIQL MDVLWKQEGL DLRMTPYGCL
PTGDRTGLIE VVLRSDTIAN IQLNKSNMAA TAAFNKDALL NWLKSKNPGE ALDRAIEEFT
LSCAGYCVAT YVLGIGDRHS DNIMIRESGQ LFHIDFGHFL GNFKTKFGIN RERVPFILTY
DFVHVIQQGK TNNSEKFERF RGYCERAYTI LRRHGLLFLH LFALMRAAGL PELSCSKDIQ
YLKDSLALGK TEEEALKHFR VKFNEALRES WKTKVNWLAH NVSKDNRQ
//
