ID PI5L1_MOUSE Reviewed; 395 AA. AC Q6U7H8; A2ASY7; A2ASY9; Q3TNU0; Q3V0C8; Q52KH3; Q8K345; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 126. DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase-like protein 1; DE Short=PI(4)P 5-kinase-like protein 1; DE Short=PtdIns(4)P-5-kinase-like protein 1; DE AltName: Full=Phosphatidylinositol phosphate kinase homolog {ECO:0000303|PubMed:14701839}; DE Short=PIPKH {ECO:0000303|PubMed:14701839}; GN Name=Pip5kl1; Synonyms=Pipkh; 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, INTERACTION WITH PIP5K1A RP AND PIP5K1B, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF RP LYS-155 AND ASP-281. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=14701839; DOI=10.1074/jbc.m309721200; RA Chang J.D., Field S.J., Rameh L.E., Carpenter C.L., Cantley L.C.; RT "Identification and characterization of a phosphoinositide phosphate kinase RT homolog."; RL J. Biol. Chem. 279:11672-11679(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC STRAIN=C57BL/6J; TISSUE=Eye, and Testis; 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 4). RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland; 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). CC -!- FUNCTION: May act as a scaffold to localize and regulate type I CC phosphatidylinositol 4-phosphate 5-kinases to specific compartments CC within the cell, where they generate PI(4,5)P2 for actin nucleation, CC signaling and scaffold protein recruitment and conversion to CC PI(3,4,5)P3. {ECO:0000269|PubMed:14701839}. CC -!- SUBUNIT: Interacts with type I phosphatidylinositol 4-phosphate 5- CC kinases, including PIP5K1A and PIP5K1B. {ECO:0000269|PubMed:14701839}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14701839}. Membrane CC {ECO:0000269|PubMed:14701839}. Note=Localized to large cytoplasmic CC vesicular structures. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q6U7H8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6U7H8-2; Sequence=VSP_024905; CC Name=3; CC IsoId=Q6U7H8-3; Sequence=VSP_024906, VSP_024909; CC Name=4; CC IsoId=Q6U7H8-4; Sequence=VSP_024907, VSP_024908; CC -!- TISSUE SPECIFICITY: Highly expressed in brain and testis, relatively to CC heart, spleen, lung, liver, skeletal muscle and kidney. CC {ECO:0000269|PubMed:14701839}. CC -!- CAUTION: In spite of its similarity to other phosphatidylinositol CC kinases, lacks intrinsic lipid kinase activity. CC {ECO:0000269|PubMed:14701839}. 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; AY376879; AAQ92365.1; -; mRNA. DR EMBL; AK133244; BAE21576.1; -; mRNA. DR EMBL; AK164998; BAE37997.1; -; mRNA. DR EMBL; AL928710; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC028795; AAH28795.1; -; mRNA. DR EMBL; BC094346; AAH94346.1; -; mRNA. DR EMBL; BC117018; AAI17019.1; -; mRNA. DR EMBL; BC119037; AAI19038.1; -; mRNA. DR CCDS; CCDS15920.1; -. [Q6U7H8-1] DR RefSeq; NP_937834.1; NM_198191.3. [Q6U7H8-1] DR AlphaFoldDB; Q6U7H8; -. DR SMR; Q6U7H8; -. DR BioGRID; 230677; 1. DR IntAct; Q6U7H8; 1. DR STRING; 10090.ENSMUSP00000051282; -. DR PhosphoSitePlus; Q6U7H8; -. DR PaxDb; 10090-ENSMUSP00000051282; -. DR ProteomicsDB; 301824; -. [Q6U7H8-1] DR ProteomicsDB; 301825; -. [Q6U7H8-2] DR ProteomicsDB; 301826; -. [Q6U7H8-3] DR ProteomicsDB; 301827; -. [Q6U7H8-4] DR Antibodypedia; 30919; 160 antibodies from 27 providers. DR DNASU; 227733; -. DR Ensembl; ENSMUST00000055304.14; ENSMUSP00000051282.8; ENSMUSG00000046854.17. [Q6U7H8-1] DR Ensembl; ENSMUST00000100188.3; ENSMUSP00000097763.3; ENSMUSG00000046854.17. [Q6U7H8-3] DR GeneID; 227733; -. DR KEGG; mmu:227733; -. DR UCSC; uc008jfv.1; mouse. [Q6U7H8-1] DR AGR; MGI:2448520; -. DR CTD; 138429; -. DR MGI; MGI:2448520; Pip5kl1. DR VEuPathDB; HostDB:ENSMUSG00000046854; -. DR eggNOG; KOG0229; Eukaryota. DR GeneTree; ENSGT00940000158633; -. DR HOGENOM; CLU_043959_0_0_1; -. DR InParanoid; Q6U7H8; -. DR OMA; EFYGLTC; -. DR OrthoDB; 2958279at2759; -. DR PhylomeDB; Q6U7H8; -. DR TreeFam; TF354315; -. DR BioGRID-ORCS; 227733; 2 hits in 79 CRISPR screens. DR ChiTaRS; Pip5kl1; mouse. DR PRO; PR:Q6U7H8; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; Q6U7H8; Protein. DR Bgee; ENSMUSG00000046854; Expressed in lens of camera-type eye and 77 other cell types or tissues. DR GO; GO:0042995; C:cell projection; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. 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:0030336; P:negative regulation of cell migration; ISO:MGI. DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISS:UniProtKB. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI. DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB. DR CDD; cd17304; PIPKc_PIP5KL1; 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:SF46; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 5-KINASE-LIKE PROTEIN 1; 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. DR Genevisible; Q6U7H8; MM. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Lipid metabolism; KW Membrane; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..395 FT /note="Phosphatidylinositol 4-phosphate 5-kinase-like FT protein 1" FT /id="PRO_0000285759" FT DOMAIN 37..394 FT /note="PIPK" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..10 FT /note="MATPSLRSHE -> MLFVSCASSHQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_024905" FT VAR_SEQ 10 FT /note="E -> EVGADQRGDKKGKGESLAITLARGLNTPPPRLCSGKIKTRPTE (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_024906" FT VAR_SEQ 201..216 FT /note="KYFIIMQCIFYPTSRI -> VSVADRGGSAVGAAGG (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024907" FT VAR_SEQ 217..395 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024908" FT VAR_SEQ 308..395 FT /note="SIQGVSKSKGTGDQNCRMLPDLPNALHILDGPDQRYFLGLVDMTTVYGFRKR FT LEHVWKMVRYPGQSVSTVSPAHYARRLCRWAEVHTE -> RTVTPAMLAMALTETTH FT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_024909" FT MUTAGEN 155 FT /note="K->R: No effect on lipid kinase activity when the FT protein is purified from mammalian cell extracts. No effect FT on lipid kinase activity when the protein is purified from FT mammalian cell extracts; when associated with A-281." FT /evidence="ECO:0000269|PubMed:14701839" FT MUTAGEN 281 FT /note="D->A: No effect on lipid kinase activity observed FT when the protein is purified from mammalian cell extracts; FT when associated with R-155." FT /evidence="ECO:0000269|PubMed:14701839" FT CONFLICT 215..218 FT /note="RISE -> VLPP (in Ref. 4; AAH28795)" FT /evidence="ECO:0000305" FT CONFLICT 265 FT /note="R -> Q (in Ref. 4; AAH28795)" FT /evidence="ECO:0000305" SQ SEQUENCE 395 AA; 45293 MW; 22AA0A86324972AB CRC64; MATPSLRSHE IPAHSQEAGN KSISSGSRRG LLWHLRARQS RVGLFEVGPG HELHRMTRMM QEGLWAATQV SKNNPPTGPT TQKDYLEVMT QVHEEGFELG TLAGPAFARL RKSIGLTEED YQATLGPGDP YLQFFSTSKS KASFFLTHDQ RFFVKTQRRH EVHVLLAHLP RYVEHLQQYP HSLLARLLGV YSLRVAQGKK KYFIIMQCIF YPTSRISERY DIKGCNISRW VDPAPEGSPL VLVLKDLNFQ EKTMRLGAQR SWFLRQMELD TAFLREVNVL DYSLLVAIQF LHEDEKGIHH SVFSTFKSIQ GVSKSKGTGD QNCRMLPDLP NALHILDGPD QRYFLGLVDM TTVYGFRKRL EHVWKMVRYP GQSVSTVSPA HYARRLCRWA EVHTE //