PI51A_MOUSE
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 03-AUG-2022, entry version 156.
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}.
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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_001293707.1. [P70182-3]
DR RefSeq; NP_032873.2; NM_008847.3. [P70182-1]
DR AlphaFoldDB; P70182; -.
DR SMR; P70182; -.
DR BioGRID; 202172; 9.
DR STRING; 10090.ENSMUSP00000102852; -.
DR BindingDB; P70182; -.
DR iPTMnet; P70182; -.
DR PhosphoSitePlus; P70182; -.
DR EPD; P70182; -.
DR jPOST; P70182; -.
DR MaxQB; P70182; -.
DR PaxDb; P70182; -.
DR PeptideAtlas; P70182; -.
DR PRIDE; P70182; -.
DR ProteomicsDB; 289568; -. [P70182-1]
DR ProteomicsDB; 289569; -. [P70182-2]
DR ProteomicsDB; 289570; -. [P70182-3]
DR Antibodypedia; 34058; 197 antibodies from 29 providers.
DR DNASU; 18720; -.
DR Ensembl; ENSMUST00000107233; ENSMUSP00000102852; ENSMUSG00000028126. [P70182-3]
DR Ensembl; ENSMUST00000107236; ENSMUSP00000102855; ENSMUSG00000028126. [P70182-1]
DR GeneID; 18720; -.
DR KEGG; mmu:18720; -.
DR UCSC; uc008qhx.3; mouse. [P70182-1]
DR UCSC; uc008qhy.3; mouse. [P70182-3]
DR CTD; 8394; -.
DR MGI; MGI:107929; Pip5k1a.
DR VEuPathDB; HostDB:ENSMUSG00000028126; -.
DR eggNOG; KOG0229; Eukaryota.
DR GeneTree; ENSGT00940000154703; -.
DR InParanoid; P70182; -.
DR OMA; NIRLVAM; -.
DR OrthoDB; 1562683at2759; -.
DR PhylomeDB; P70182; -.
DR TreeFam; TF319618; -.
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; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Pip5k1a; mouse.
DR PRO; PR:P70182; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P70182; protein.
DR Bgee; ENSMUSG00000028126; Expressed in placenta labyrinth and 278 other tissues.
DR ExpressionAtlas; P70182; baseline and differential.
DR Genevisible; P70182; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS: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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISO:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0097178; P:ruffle assembly; ISS:UniProtKB.
DR Gene3D; 3.30.800.10; -; 1.
DR InterPro; IPR023610; PInositol-4-P-5-kinase.
DR InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR PANTHER; PTHR23086; PTHR23086; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00330; PIPKc; 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 448..475
FT /note="Polar residues"
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
