ID Q8CI98_MOUSE Unreviewed; 1045 AA. AC Q8CI98; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2004, sequence version 2. DT 02-SEP-2026, entry version 176. DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform {ECO:0000256|ARBA:ARBA00067682}; DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073}; DE EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010}; DE AltName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta {ECO:0000256|ARBA:ARBA00075758}; GN Name=Pik3cd {ECO:0000313|EMBL:AAH35203.2, GN ECO:0000313|MGI:MGI:1098211}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH35203.2}; RN [1] {ECO:0000313|EMBL:AAH35203.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N {ECO:0000313|EMBL:AAH35203.2}; RC TISSUE=Salivary gland {ECO:0000313|EMBL:AAH35203.2}; 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., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., 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., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] {ECO:0000313|EMBL:CAJ18557.1} RP NUCLEOTIDE SEQUENCE. RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., RA Wiemann S., Schick M., Korn B.; RT "Cloning of mouse full open reading frames in Gateway(R) system entry RT vector (pDONR201)."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero- CC 3-phospho-1D-myo-inositol 4,5-bisphosphate + ATP = 1-octadecanoyl-2- CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo- CC inositol 3,4,5-triphosphate) + ADP + H(+); Xref=Rhea:RHEA:43396, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77137, CC ChEBI:CHEBI:83243, ChEBI:CHEBI:456216; CC Evidence={ECO:0000256|ARBA:ARBA00051347}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43397; CC Evidence={ECO:0000256|ARBA:ARBA00051347}; 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 -!- 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: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}. CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate CC biosynthesis. {ECO:0000256|ARBA:ARBA00004805}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K CC subfamily. {ECO:0000256|ARBA:ARBA00006209}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00269}. 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; BC035203; AAH35203.2; -; mRNA. DR EMBL; CT010349; CAJ18557.1; -; mRNA. DR RefSeq; NP_001157522.1; NM_001164050.1. DR RefSeq; XP_006538713.1; XM_006538650.5. DR AlphaFoldDB; Q8CI98; -. DR SMR; Q8CI98; -. DR jPOST; Q8CI98; -. DR ProteomicsDB; 332688; -. DR Antibodypedia; 4215; 603 antibodies from 42 providers. DR DNASU; 18707; -. DR GeneID; 18707; -. DR UCSC; uc008vwu.2; mouse. DR AGR; MGI:1098211; -. DR CTD; 5293; -. DR MGI; MGI:1098211; Pik3cd. DR VEuPathDB; HostDB:ENSMUSG00000039936; -. DR GeneTree; ENSGT00940000159079; -. DR OrthoDB; 67688at2759; -. DR UniPathway; UPA00220; -. DR BioGRID-ORCS; 18707; 1 hit in 80 CRISPR screens. DR Bgee; ENSMUSG00000039936; Expressed in granulocyte and 170 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA. DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-EC. DR GO; GO:0046934; F:1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC. DR GO; GO:0042113; P:B cell activation; IEA:UniProtKB-ARBA. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProtKB-ARBA. DR GO; GO:0006952; P:defense response; IEA:UniProtKB-ARBA. 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:0051094; P:positive regulation of developmental process; IEA:UniProtKB-ARBA. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:UniProtKB-ARBA. DR GO; GO:0051240; P:positive regulation of multicellular organismal process; IEA:UniProtKB-ARBA. DR GO; GO:0022603; P:regulation of anatomical structure morphogenesis; IEA:UniProtKB-ARBA. DR GO; GO:2000026; P:regulation of multicellular organismal development; IEA:UniProtKB-ARBA. DR GO; GO:0051707; P:response to other organism; IEA:UniProtKB-ARBA. DR CDD; cd08693; C2_PI3K_class_I_beta_delta; 1. DR CDD; cd05174; PI3Kc_IA_delta; 1. DR FunFam; 1.10.1070.11:FF:000001; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1. DR FunFam; 1.25.40.70:FF:000008; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1. DR FunFam; 2.60.40.150:FF:000046; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1. DR FunFam; 3.10.20.770:FF:000002; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1. DR FunFam; 3.30.1010.10:FF:000005; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta; 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; 3.30.1010.10; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 4; 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; IPR037703; PI3-kinase_delta_cat. DR InterPro; IPR015433; PI3/4_kinase. 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; 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 1: Evidence at protein level; KW Adaptive immunity {ECO:0000256|ARBA:ARBA00023130}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Differentiation {ECO:0000256|ARBA:ARBA00022782}; KW Immunity {ECO:0000256|ARBA:ARBA00022859}; KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198}; KW Innate immunity {ECO:0000256|ARBA:ARBA00022588}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE- KW ProRule:PRU00269}; Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU00269}. 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 497..674 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" FT REGION 752..758 FT /note="G-loop" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00269" FT REGION 891..899 FT /note="Catalytic loop" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00269" SQ SEQUENCE 1045 AA; 119928 MW; 92CAF2C429142B17 CRC64; MPPGVDCPME FWTKEESQSV VVDFLLPTGV YLNFPVSRNA NLSTIKQVLW HRAQYEPLFH MLSDPEAYVF TCVNQTAEQQ ELEDEQRRLC DIQPFLPVLR LVAREGDRVK KLINSQISLL IGKGLHEFDS LRDPEVNDFR TKMRQFCEEA AAHRQQLGWV EWLQYSFPLQ LEPSARGWRA GLLRVSNRAL LVNVKFEGSE ESFTFQVSTK DMPLALMACA LRKKATVFRQ PLVEQPEEYA LQVNGRHEYL YGNYPLCHFQ YICSCLHSGL TPHLTMVHSS SILAMRDEQS NPAPQVQKPR AKPPPIPAKK PSSVSLWSLE QPFSIELIEG RKVNADERMK LVVQAGLFHG NEMLCKTVSS SEVNVCSEPV WKQRLEFDIS VCDLPRMARL CFALYAVVEK AKKARSTKKK SKKADCPIAW ANLMLFDYKD QLKTGERCLY MWPSVPDEKG ELLNPAGTVR GNPNTESAAA LVIYLPEVAP HPVYFPALEK ILELGRHGER GRITEEEQLQ LREILERRGS GELYEHEKDL VWKMRHEVQE HFPEALARLL LVTKWNKHED VAQMLYLLCS WPELPVLSAL ELLDFSFPDC YVGSFAIKSL RKLTDDELFQ YLLQLVQVLK YESYLDCELT KFLLGRALAN RKIGHFLFWH LRSEMHVPSV ALRFGLIMEA YCRGSTHHMK VLMKQGEALS KLKALNDFVK VSSQKTTKPQ TKEMMHMCMR QETYMEALSH LQSPLDPSTL LEEVCSVEQC TFMDSKMKPL WIMYSSEEAG SAGNVGIIFK NGDDLRQDML TLQMIQLMDV LWKQEGLDLR MTPYGCLPTG DRTGLIEVVL HSDTIANIQL NKSNMAATAA FNKDALLNWL KSKNPGEALD RAIEEFTLSC AGYCVATYVL GIGDRHSDNI MIRESGQLFH IDFGHFLGNF KTKFGINRER VPFILTYDFV HVIQQGKTNN SEKFERFRGY CERAYTILRR HGLLFLHLFA LMRAAGLPEL SCSKDIQYLK DSLALGKTEE EALKHFRVKF NEALRESWKT KVNWLAHNVS KDNRQ //