ID A7E2E0_HUMAN Unreviewed; 1044 AA. AC A7E2E0; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 16-JAN-2019, entry version 88. DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit {ECO:0000256|PIRNR:PIRNR000587}; DE EC=2.7.1.153 {ECO:0000256|PIRNR:PIRNR000587}; GN Name=PIK3CD {ECO:0000313|EMBL:AAI50298.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAI50298.1}; RN [1] {ECO:0000313|EMBL:AAI50298.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., RA Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., RA Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., RA Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., RA Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., RA Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., RA Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., RA Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., RA Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., RA Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., RA Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., RA Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., RA Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., RA Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., RA Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., RA Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., RA Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., RA Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., RA Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). 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(+); CC Xref=Rhea:RHEA:21292, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57836, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; CC EC=2.7.1.153; Evidence={ECO:0000256|PIRNR:PIRNR000587}; CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. CC {ECO:0000256|PIRNR:PIRNR000587, ECO:0000256|PROSITE- CC ProRule:PRU00877, ECO:0000256|SAAS:SAAS01097356}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC150297; AAI50298.1; -; mRNA. DR UniGene; Hs.518451; -. DR PeptideAtlas; A7E2E0; -. DR PRIDE; A7E2E0; -. DR DNASU; 5293; -. DR PharmGKB; PA33310; -. DR eggNOG; KOG0904; Eukaryota. DR eggNOG; COG5032; LUCA. DR HOVERGEN; HBG052721; -. DR ChiTaRS; PIK3CD; human. DR Genevisible; A7E2E0; HS. DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC. DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IEA:InterPro. DR CDD; cd05174; PI3Kc_IA_delta; 1. DR Gene3D; 1.10.1070.11; -; 1. DR Gene3D; 2.60.40.150; -; 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; IPR003113; PI3K_adapt-bd_dom. DR InterPro; IPR002420; PI3K_C2_dom. DR InterPro; IPR000341; PI3K_Ras-bd_dom. DR InterPro; IPR008290; PI3K_Vps34. DR InterPro; IPR037703; PI3Kdelta_dom. DR InterPro; IPR015433; PI_Kinase. DR InterPro; IPR001263; PInositide-3_kin_accessory_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR10048; PTHR10048; 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 PIRSF; PIRSF000587; PI3K_Vps34; 3. 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; SSF48371; 1. DR SUPFAM; SSF54236; SSF54236; 1. DR SUPFAM; SSF56112; SSF56112; 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; PS51547; PI3K_C2; 1. DR PROSITE; PS51546; PI3K_RBD; 1. DR PROSITE; PS51545; PIK_HELICAL; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|PIRNR:PIRNR000587, KW ECO:0000256|SAAS:SAAS01019120}; KW Kinase {ECO:0000256|PIRNR:PIRNR000587, ECO:0000256|PROSITE- KW ProRule:PRU00269, ECO:0000256|SAAS:SAAS00936663, KW ECO:0000313|EMBL:AAI50298.1}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000587, KW ECO:0000256|SAAS:SAAS01019260}; KW Transferase {ECO:0000256|PIRNR:PIRNR000587, ECO:0000256|PROSITE- KW ProRule:PRU00269, ECO:0000256|SAAS:SAAS00936588}. FT DOMAIN 16 105 PI3K-ABD. {ECO:0000259|PROSITE:PS51544}. FT DOMAIN 187 278 PI3K-RBD. {ECO:0000259|PROSITE:PS51546}. FT DOMAIN 319 476 C2 PI3K-type. {ECO:0000259|PROSITE: FT PS51547}. FT DOMAIN 497 674 PIK helical. {ECO:0000259|PROSITE: FT PS51545}. FT DOMAIN 774 1024 PI3K/PI4K. {ECO:0000259|PROSITE:PS50290}. SQ SEQUENCE 1044 AA; 119495 MW; 65287228E244C13D CRC64; MPPGVDCPME FWTKEENQSV VVDFLLPTGV YLNFPVSRNA NLSTIKQLLW HRAQYEPLFH MLSGPEAYVF TCINQTAEQQ ELEDEQRRLC DVQPFLPVLR LVAREGDRVK KLINSQISLL IGKGLHEFDS LCDPEVNDFR AKMCQFCEEA AARRQQLGWE AWLQYSFPLQ LEPSAQTWGP GTLRLPNRAL LVNVKFEGSE ESFTFQVSTK DVPLALMACA LRKKATVFRQ PLVEQPEDYT LQVNGRHEYL YGSYPLCQFQ YICSCLHSGL TPHLTMVHSS SILAMRDEQS NPAPQVQKPR AKPPPIPAKK PCSVSLWSLE QPFRIELIQG SKVNADERMK LVVQAGLFHG NEMLCKTVSS SEVSVCSEPV WKQRLEFDIN ICDLPRMARL CFALYAVIEK AKKARSTKKK SKKADCPIAW ANLMLFDYKD QLKTGERCLY MWPSVPDEKG ELLNPTGTVR SNPNTDSAAA LLICLPEVAP HPVYYPALEK ILELGRHSEC VHVTEEEQLQ LREILERRGS GELYEHEKDL VWKLRHEVQE HFPEALARLL LVTKWNKHED VAQMLYLLCS WPELPVLSAL ELLDFSFPDC HVGSFAIKSL RKLTDDELFQ YLLQLVQVLK YESYLDCELT KFLLDRALAN RKIGHFLFWH LRSEMHVPSV ALRFGLILEA YCRGSTHHMK VLMKQGEALS KLKALNDFVK LSSQKTPKPQ TKELMHLCMR QEAYLEALSH LQSPLDPSTL LAEVCVEQCT FMDSKMKPLW IMYSNEEAGS GGSVGIIFKN GDDLRQDMLT LQMIQLMDVL WKQEGLDLRM TPYGCLPTGD RTGLIEVVLR SDTIANIQLN KSNMAATAAF NKDALLNWLK SKNPGEALDR AIEEFTLSCA GYCVATYVLG IGDRHSDNIM IRESGQLFHI DFGHFLGNFK TKFGINRERV PFILTYDFVH VIQQGKTNNS EKFERFRGYC ERAYTILRRH GLLFLHLFAL MRAAGLPELS CSKDIQYLKD SLALGKTEEE ALKHFRVKFN EALRESWKTK VNWLAHNVSK DNRQ //