PI5L1_MOUSE
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 03-AUG-2022, entry version 117.
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; Q6U7H8; -.
DR PRIDE; Q6U7H8; -.
DR ProteomicsDB; 301824; -. [Q6U7H8-1]
DR ProteomicsDB; 301825; -. [Q6U7H8-2]
DR ProteomicsDB; 301826; -. [Q6U7H8-3]
DR ProteomicsDB; 301827; -. [Q6U7H8-4]
DR Antibodypedia; 30919; 145 antibodies from 27 providers.
DR DNASU; 227733; -.
DR Ensembl; ENSMUST00000055304; ENSMUSP00000051282; ENSMUSG00000046854. [Q6U7H8-1]
DR Ensembl; ENSMUST00000100188; ENSMUSP00000097763; ENSMUSG00000046854. [Q6U7H8-3]
DR GeneID; 227733; -.
DR KEGG; mmu:227733; -.
DR UCSC; uc008jfv.1; mouse. [Q6U7H8-1]
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; PRHELHG; -.
DR OrthoDB; 779747at2759; -.
DR PhylomeDB; Q6U7H8; -.
DR TreeFam; TF354315; -.
DR BioGRID-ORCS; 227733; 2 hits in 74 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 74 other tissues.
DR Genevisible; Q6U7H8; MM.
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 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; 2.
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; 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
