ID PI51A_MOUSE Reviewed; 546 AA. AC P70182; F8WIX5; Q3U917; Q8K0D3; Q99L80; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 2. DT 02-SEP-2026, entry version 175. DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha {ECO:0000305|PubMed:18772378, ECO:0000305|PubMed:8798574}; DE Short=PIP5K1-alpha {ECO:0000305|PubMed:18772378, ECO:0000305|PubMed:8798574}; DE Short=PtdIns(4)P-5-kinase 1 alpha {ECO:0000305|PubMed:18772378, ECO:0000305|PubMed:8798574}; DE EC=2.7.1.68 {ECO:0000269|PubMed:9535851}; DE AltName: Full=68 kDa type I phosphatidylinositol 4-phosphate 5-kinase alpha {ECO:0000303|PubMed:8798574}; DE AltName: Full=Phosphatidylinositol 4-phosphate 5-kinase type I alpha {ECO:0000305|PubMed:18772378, ECO:0000305|PubMed:8798574}; DE Short=PIP5KIalpha {ECO:0000303|PubMed:18772378, ECO:0000305|PubMed:8798574}; DE AltName: Full=Phosphatidylinositol 4-phosphate 5-kinase type I beta {ECO:0000312|EMBL:BAA13031.1, ECO:0000312|EMBL:BAE29943.1, ECO:0000312|EMBL:BAE30850.1, ECO:0000312|EMBL:BAE34344.1}; DE Short=PI4P5KIbeta; GN Name=Pip5k1a {ECO:0000312|MGI:MGI:107929}; 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; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, RP ACTIVITY REGULATION, AND TISSUE SPECIFICITY. RC TISSUE=Insulinoma; RX PubMed=8798574; DOI=10.1074/jbc.271.39.23611; RA Ishihara H., Shibasaki Y., Kizuki N., Katagiri H., Yazaki Y., Asano T., RA Oka Y.; RT "Cloning of cDNAs encoding two isoforms of 68-kDa type I RT phosphatidylinositol 4-phosphate 5-kinase."; RL J. Biol. Chem. 271:23611-23614(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC STRAIN=C57BL/6J; TISSUE=Inner ear, and Macrophage; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Eye, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; 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 [5] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=9535851; DOI=10.1074/jbc.273.15.8741; RA Ishihara H., Shibasaki Y., Kizuki N., Wada T., Yazaki Y., Asano T., Oka Y.; RT "Type I phosphatidylinositol-4-phosphate 5-kinases. Cloning of the third RT isoform and deletion/substitution analysis of members of this novel lipid RT kinase family."; RL J. Biol. Chem. 273:8741-8748(1998). RN [6] RP FUNCTION, AND INTERACTION WITH RAC1. RX PubMed=10679324; DOI=10.1016/s0960-9822(00)00315-8; RA Tolias K.F., Hartwig J.H., Ishihara H., Shibasaki Y., Cantley L.C., RA Carpenter C.L.; RT "Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac- RT dependent actin assembly."; RL Curr. Biol. 10:153-156(2000). RN [7] RP FUNCTION IN PLATELETS, AND DISRUPTION PHENOTYPE. RX PubMed=18772378; DOI=10.1073/pnas.0804139105; RA Wang Y., Chen X., Lian L., Tang T., Stalker T.J., Sasaki T., Kanaho Y., RA Brass L.F., Choi J.K., Hartwig J.H., Abrams C.S.; RT "Loss of PIP5KIbeta demonstrates that PIP5KI isoform-specific PIP2 RT synthesis is required for IP3 formation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:14064-14069(2008). RN [8] RP FUNCTION IN PHAGOCYTOSIS, AND DISRUPTION PHENOTYPE. RX PubMed=19153220; DOI=10.1083/jcb.200806121; RA Mao Y.S., Yamaga M., Zhu X., Wei Y., Sun H.-Q., Wang J., Yun M., Wang Y., RA Di Paolo G., Bennett M., Mellman I., Abrams C.S., De Camilli P., Lu C.Y., RA Yin H.L.; RT "Essential and unique roles of PIP5K-gamma and -alpha in Fcgamma receptor- RT mediated phagocytosis."; RL J. Cell Biol. 184:281-296(2009). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Spleen; 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). RN [10] RP FUNCTION IN EMBRYOGENESIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE. RX PubMed=20622009; DOI=10.1074/jbc.m110.132191; RA Volpicelli-Daley L.A., Lucast L., Gong L.-W., Liu L., Sasaki J., Sasaki T., RA Abrams C.S., Kanaho Y., De Camilli P.; RT "Phosphatidylinositol-4-phosphate 5-kinases and phosphatidylinositol 4,5- RT bisphosphate synthesis in the brain."; RL J. Biol. Chem. 285:28708-28714(2010). RN [11] RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH DGKZ AND IRS1. RX PubMed=27739494; DOI=10.1038/srep35438; RA Liu T., Yu B., Kakino M., Fujimoto H., Ando Y., Hakuno F., Takahashi S.I.; RT "A novel IRS-1-associated protein, DGKzeta regulates GLUT4 translocation in RT 3T3-L1 adipocytes."; RL Sci. Rep. 6:35438-35438(2016). CC -!- FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4- CC phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5- CC bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that CC regulates several cellular processes such as signal transduction, CC vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and CC cell motility (PubMed:8798574, PubMed:9535851). PtdIns(4,5)P2 can CC directly act as a second messenger or can be utilized as a precursor to CC generate other second messengers: inositol 1,4,5-trisphosphate (IP3), CC diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate CC (PtdIns(3,4,5)P3/PIP3) (By similarity). PIP5K1A-mediated CC phosphorylation of PtdIns(4)P is the predominant pathway for CC PtdIns(4,5)P2 synthesis (PubMed:18772378). Can also use CC phosphatidylinositol (PtdIns) as substrate in vitro (By similarity). CC Together with PIP5K1C, is required for phagocytosis, both enzymes CC regulating different types of actin remodeling at sequential steps CC (PubMed:19153220). Promotes particle ingestion by activating the WAS CC GTPase-binding protein that induces Arp2/3 dependent actin CC polymerization at the nascent phagocytic cup (PubMed:19153220). CC Together with PIP5K1B, is required, after stimulation by G protein CC coupled receptors, for the synthesis of IP3 that will induce stable CC platelet adhesion (PubMed:18772378). Recruited to the plasma membrane CC by the E-cadherin/beta-catenin complex where it provides the substrate CC PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, IP3 and DAG, that CC will mobilize internal calcium and drive keratinocyte differentiation CC (By similarity). Positively regulates insulin-induced translocation of CC SLC2A4 to the cell membrane in adipocytes (PubMed:27739494). Together CC with PIP5K1C has a role during embryogenesis (PubMed:20622009). CC Independently of its catalytic activity, is required for membrane CC ruffling formation, actin organization and focal adhesion formation CC during directional cell migration by controlling integrin-induced CC translocation of the small GTPase RAC1 to the plasma membrane CC (PubMed:10679324). Also functions in the nucleus where it acts as an CC activator of TUT1 adenylyltransferase activity in nuclear speckles, CC thereby regulating mRNA polyadenylation of a select set of mRNAs (By CC similarity). {ECO:0000250|UniProtKB:Q99755, CC ECO:0000269|PubMed:10679324, ECO:0000269|PubMed:18772378, CC ECO:0000269|PubMed:19153220, ECO:0000269|PubMed:20622009, CC ECO:0000269|PubMed:27739494, ECO:0000269|PubMed:8798574, CC ECO:0000269|PubMed:9535851, ECO:0000303|PubMed:18772378}. 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-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178, CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68; CC Evidence={ECO:0000269|PubMed:8798574, ECO:0000269|PubMed:9535851}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14426; CC Evidence={ECO:0000305|PubMed:8798574, ECO:0000305|PubMed:9535851}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero- CC 3-phospho-1D-myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2- CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol CC 4,5-bisphosphate + ADP + H(+); Xref=Rhea:RHEA:40363, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77136, CC ChEBI:CHEBI:77137, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:Q99755}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40364; CC Evidence={ECO:0000250|UniProtKB:Q99755}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4- CC phosphate) + ATP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo- CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:65356, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:83423, CC ChEBI:CHEBI:83436, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:Q99755}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65357; CC Evidence={ECO:0000250|UniProtKB:Q99755}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D- CC myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl- CC sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ADP + H(+); CC Xref=Rhea:RHEA:40367, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:77139, ChEBI:CHEBI:77140, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:Q99755}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40368; CC Evidence={ECO:0000250|UniProtKB:Q99755}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D- CC myo-inositol + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3- CC phospho-1D-myo-inositol 5-phosphate + ADP + H(+); CC Xref=Rhea:RHEA:40379, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:77163, ChEBI:CHEBI:77164, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:Q99755}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40380; CC Evidence={ECO:0000250|UniProtKB:Q99755}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3- CC phospho-1D-myo-inositol + ATP = 1-octadecanoyl-2-(9Z,12Z)- CC octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + CC ADP + H(+); Xref=Rhea:RHEA:40383, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77158, ChEBI:CHEBI:77159, CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q99755}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40384; CC Evidence={ECO:0000250|UniProtKB:Q99755}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phospho-(1D-myo-inositol) + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)- CC eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + CC ADP + H(+); Xref=Rhea:RHEA:40375, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77160, ChEBI:CHEBI:133606, CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q99755}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40376; CC Evidence={ECO:0000250|UniProtKB:Q99755}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-di-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo- CC inositol + ATP = 1,2-di(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho- CC 1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40387, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77165, CC ChEBI:CHEBI:77167, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:Q99755}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40388; CC Evidence={ECO:0000250|UniProtKB:Q99755}; CC -!- ACTIVITY REGULATION: Activated by phosphatidic acid. CC {ECO:0000269|PubMed:8798574, ECO:0000269|PubMed:9535851}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=26 uM for phosphatidylinositol-4-phosphate/PtdIns(4)P CC {ECO:0000269|PubMed:9535851}; CC KM=33 uM for ATP {ECO:0000269|PubMed:9535851}; CC -!- SUBUNIT: Interacts with RAC1 (PubMed:10679324). Interacts with TUT1 (By CC similarity). Forms a complex with CDH1/E-cadherin, CTNNB1/beta-catenin CC and CTNND1 at the plasma membrane upon calcium stimulation (By CC similarity). Found in a ternary complex with IRS1 and DGKZ in the CC absence of insulin stimulation (PubMed:27739494). Interacts with DGKZ CC (By similarity). Interacts with PIP4K2C; the interaction inhibits CC PIP5K1A kinase activity (By similarity). {ECO:0000250|UniProtKB:Q99755, CC ECO:0000269|PubMed:10679324, ECO:0000269|PubMed:27739494}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20622009}. CC Cytoplasm {ECO:0000269|PubMed:20622009}. Nucleus CC {ECO:0000250|UniProtKB:Q99755}. Nucleus speckle CC {ECO:0000250|UniProtKB:Q99755}. Cell projection, ruffle CC {ECO:0000250|UniProtKB:Q99755}. Cell projection, lamellipodium CC {ECO:0000250|UniProtKB:Q99755}. Note=Colocalizes with RAC1 at actin- CC rich membrane ruffles (By similarity). Localizes to nuclear speckles CC and associates with TUT1 to regulate polyadenylation of selected mRNAs CC (By similarity). {ECO:0000250|UniProtKB:Q99755}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P70182-1; Sequence=Displayed; CC Name=2; CC IsoId=P70182-2; Sequence=VSP_053437, VSP_016009; CC Name=3; CC IsoId=P70182-3; Sequence=VSP_053437; CC -!- TISSUE SPECIFICITY: Highest expression in brain. Also detected in CC skeletal muscle, testis, brain and lung. {ECO:0000269|PubMed:20622009, CC ECO:0000269|PubMed:8798574}. CC -!- DEVELOPMENTAL STAGE: Expression is highest during early embryogenesis CC and slightly decreases over time. {ECO:0000269|PubMed:20622009}. CC -!- DISRUPTION PHENOTYPE: Survive to adulthood, but bred poorly and display CC reduced fertility. Failed to form any vessel occlusion after chemical- CC induced carotid injury. Platelets have defective aggregation. Bone CC marrow-derived macrophages are defective in actin polymerization during CC phagocytosis. PIP5K1A and PIP5K1C double mutant mice are embryonic CC lethal. {ECO:0000269|PubMed:18772378, ECO:0000269|PubMed:19153220, CC ECO:0000269|PubMed:20622009}. CC -!- CAUTION: There is confusion in the literature with phosphatidylinositol CC 4-phosphate 5-kinase type I nomenclature due to the fact that CC frequently mouse PIP5K1B is named Phosphatidylinositol 4-phosphate 5- CC kinase type I alpha. {ECO:0000305}. 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; D86177; BAA13031.1; -; mRNA. DR EMBL; AK150898; BAE29943.1; -; mRNA. DR EMBL; AK151984; BAE30850.1; -; mRNA. DR EMBL; AK158062; BAE34344.1; -; mRNA. DR EMBL; AC087062; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC131769; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC003763; AAH03763.1; -; mRNA. DR EMBL; BC031774; AAH31774.1; -; mRNA. DR CCDS; CCDS38542.1; -. [P70182-1] DR CCDS; CCDS79980.1; -. [P70182-3] DR RefSeq; NP_001280636.1; NM_001293707.2. [P70182-3] DR RefSeq; NP_032873.2; NM_008847.4. [P70182-1] DR AlphaFoldDB; P70182; -. DR SMR; P70182; -. DR BioGRID; 202172; 10. DR FunCoup; P70182; 3317. DR STRING; 10090.ENSMUSP00000102852; -. DR BindingDB; P70182; -. DR GlyGen; P70182; 1 site, 1 N-linked glycan (1 site). DR iPTMnet; P70182; -. DR PhosphoSitePlus; P70182; -. DR jPOST; P70182; -. DR PaxDb; 10090-ENSMUSP00000102852; -. DR PeptideAtlas; P70182; -. DR ProteomicsDB; 289568; -. [P70182-1] DR ProteomicsDB; 289569; -. [P70182-2] DR ProteomicsDB; 289570; -. [P70182-3] DR Pumba; P70182; -. DR Antibodypedia; 34058; 202 antibodies from 30 providers. DR DNASU; 18720; -. DR Ensembl; ENSMUST00000107233.9; ENSMUSP00000102852.3; ENSMUSG00000028126.17. [P70182-3] DR Ensembl; ENSMUST00000107236.9; ENSMUSP00000102855.3; ENSMUSG00000028126.17. [P70182-1] DR GeneID; 18720; -. DR KEGG; mmu:18720; -. DR UCSC; uc008qhx.3; mouse. [P70182-1] DR UCSC; uc008qhy.3; mouse. [P70182-3] DR AGR; MGI:107929; -. DR CTD; 8394; -. DR MGI; MGI:107929; Pip5k1a. DR VEuPathDB; HostDB:ENSMUSG00000028126; -. DR eggNOG; KOG0229; Eukaryota. DR GeneTree; ENSGT00940000154703; -. DR InParanoid; P70182; -. DR OMA; CIFYADD; -. DR PhylomeDB; P70182; -. DR BRENDA; 2.7.1.68; 3474. DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane. DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR SABIO-RK; P70182; -. DR BioGRID-ORCS; 18720; 7 hits in 79 CRISPR screens. DR PRO; PR:P70182; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; P70182; protein. DR Bgee; ENSMUSG00000028126; Expressed in placenta labyrinth and 281 other cell types or tissues. DR ExpressionAtlas; P70182; baseline and differential. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0030027; C:lamellipodium; ISO:GO_Central. DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:GO_Central. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. DR GO; GO:0032587; C:ruffle membrane; IDA:MGI. DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IDA:MGI. DR GO; GO:0019900; F:kinase binding; ISO:GO_Central. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0090630; P:activation of GTPase activity; ISO:GO_Central. DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB. DR GO; GO:0010761; P:fibroblast migration; IMP:MGI. DR GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB. DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IGI:MGI. DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:MGI. DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISO:GO_Central. DR GO; GO:0008654; P:phospholipid biosynthetic process; ISO:GO_Central. DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB. DR GO; GO:0097178; P:ruffle assembly; ISS:UniProtKB. DR CDD; cd17306; PIPKc_PIP5K1A_like; 1. DR FunFam; 3.30.800.10:FF:000001; phosphatidylinositol 4-phosphate 5-kinase type-1 gamma; 1. DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1. DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1. DR InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf. DR InterPro; IPR002498; PInositol-4-P-4/5-kinase_core. DR InterPro; IPR027484; PInositol-4-P-5-kinase_N. DR InterPro; IPR023610; PInositol-4/5-P-5/4-kinase. DR PANTHER; PTHR23086:SF54; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 5-KINASE TYPE-1 ALPHA; 1. DR PANTHER; PTHR23086; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; 1. DR Pfam; PF01504; PIP5K; 1. DR SMART; SM00330; PIPKc; 1. DR SUPFAM; SSF56104; SAICAR synthase-like; 1. DR PROSITE; PS51455; PIPK; 1. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cell membrane; Cell projection; KW Cytoplasm; Isopeptide bond; Kinase; Lipid metabolism; Membrane; KW Nucleotide-binding; Nucleus; Reference proteome; Transferase; KW Ubl conjugation. FT CHAIN 1..546 FT /note="Phosphatidylinositol 4-phosphate 5-kinase type-1 FT alpha" FT /id="PRO_0000185457" FT DOMAIN 66..434 FT /note="PIPK" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781" FT REGION 442..475 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 491..518 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 450..462 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 509..518 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CROSSLNK 88 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q99755" FT VAR_SEQ 27 FT /note="A -> AA (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_053437" FT VAR_SEQ 238..431 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_016009" FT CONFLICT 107 FT /note="P -> R (in Ref. 2; BAE29943/BAE30850)" FT /evidence="ECO:0000305" FT CONFLICT 120 FT /note="N -> S (in Ref. 4; AAH03763)" FT /evidence="ECO:0000305" FT CONFLICT 258 FT /note="E -> D (in Ref. 1; BAA13031)" FT /evidence="ECO:0000305" SQ SEQUENCE 546 AA; 60485 MW; 6E895F22A75B7140 CRC64; MASASSGPAA AGFSSLDAGA PAGTAAASGI KRATVSEGPS ASVMPVKKIG HRSVDSSGET TYKKTTSSAL KGAIQLGITH TVGSLSTKPE RDVLMQDFYV VESIFFPSEG SNLTPAHHYN DFRFKTYAPV AFRYFRELFG IRPDDYLYSL CSEPLIELSN SGASGSLFYV SSDDEFIIKT VQHKEAEFLQ KLLPGYYMNL NQNPRTLLPK FYGLYCVQAG GKNIRIVVMN NLLPRSVKMH MKYDLKGSTY KRRASQKERE KTLPTFKDLD FLQDIPDGLF LDADMYSALC KTLQRDCLVL QSFKIMDYSL LMSIHNMDHA QREPTSNDTQ YSADTRRPAP QKALYSTAME SIQGEARRGG TVETEDHMGG IPARNNKGER LLLYIGIIDI LQSYRFVKKL EHSWKALVHD GDTVSVHRPG FYAERFQRFM CNTVFKKIPL KPSPTKKFRS GPSFSRRSGP SGNSCTSQLM ASGEHRAQVT TKAEVEPDVH LGRPDVLPQT PPLEEISEGS PVPGPSFSPV VGQPLQILNL SSTLEKLDVA ESEFTH //