PI42C_MOUSE
ID PI42C_MOUSE Reviewed; 421 AA.
AC Q91XU3; Q3UFU5; Q99K02;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma;
DE EC=2.7.1.149 {ECO:0000250|UniProtKB:Q8TBX8};
DE AltName: Full=Phosphatidylinositol 5-phosphate 4-kinase type II gamma;
DE Short=PI(5)P 4-kinase type II gamma;
DE Short=PIP4KII-gamma;
GN Name=Pip4k2c {ECO:0000312|MGI:MGI:2152214}; Synonyms=Pip5k2c;
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], AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15018809; DOI=10.1016/s1567-133x(01)00023-0;
RA Akiba Y., Suzuki R., Saito-Saino S., Owada Y., Sakagami H., Watanabe M.,
RA Kondo H.;
RT "Localization of mRNAs for phosphatidylinositol phosphate kinases in the
RT mouse brain during development.";
RL Gene Expr. Patterns 1:123-133(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Kidney, 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
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 -!- FUNCTION: Phosphatidylinositol 5-phosphate 4-kinase with low enzymatic
CC activity. May be a GTP sensor, has higher GTP-dependent kinase activity
CC than ATP-dependent kinase activity. PIP4Ks negatively regulate insulin
CC signaling through a catalytic-independent mechanism. They interact with
CC PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-
CC dependent conversion to PtdIns(3,4,5)P3.
CC {ECO:0000250|UniProtKB:Q8TBX8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:12280,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57795,
CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.149;
CC Evidence={ECO:0000250|UniProtKB:Q8TBX8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12281;
CC Evidence={ECO:0000250|UniProtKB:Q8TBX8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-
CC phosphate) + ATP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:55992,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:83423,
CC ChEBI:CHEBI:84968, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q8TBX8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55993;
CC Evidence={ECO:0000250|UniProtKB:Q8TBX8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-
CC phosphate) + GTP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + GDP + H(+); Xref=Rhea:RHEA:55964,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:83423, ChEBI:CHEBI:84968;
CC Evidence={ECO:0000250|UniProtKB:Q8TBX8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55965;
CC Evidence={ECO:0000250|UniProtKB:Q8TBX8};
CC -!- SUBUNIT: Interacts with PIP5K1A; the interaction inhibits PIP5K1A
CC kinase activity. {ECO:0000250|UniProtKB:Q8TBX8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:O88370}. Cytoplasm
CC {ECO:0000250|UniProtKB:O88370}.
CC -!- DEVELOPMENTAL STAGE: No significant expression was discerned throughout
CC the prenatal brains except for the olfactory mantle zone, which
CC exhibited the expression signals weakly. On P0 and P7, the expression
CC was weakly positive in the gray matter throughout the brain, with
CC higher expression in the olfactory mitral cell layer. In the
CC cerebellum, the expression was evenly positive in external and internal
CC granule cell layers. On P21 and P56, the expression in non-cortical
CC brain parenchyma was negligible. However, the expression was evident in
CC the olfactory mitral cell layer, the piriform cortex, the hippocampal
CC pyramidal CA1-3, and the cerebellar Purkinje cell layer, although much
CC less distinct in the dentate granule cell layer and the cerebellar
CC granule cell layer. In the cerebral cortex, the expression was weaker
CC in layer V than the other layers. No significant expression was seen in
CC the white matter. {ECO:0000269|PubMed:15018809}.
CC -!- PTM: Phosphorylated, phosphorylation is induced by EGF.
CC {ECO:0000250|UniProtKB:O88370}.
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DR EMBL; AB054591; BAB62096.1; -; mRNA.
DR EMBL; AK148299; BAE28464.1; -; mRNA.
DR EMBL; BC005539; AAH05539.1; -; mRNA.
DR EMBL; BC021383; AAH21383.1; -; mRNA.
DR CCDS; CCDS24232.1; -.
DR RefSeq; NP_473438.1; NM_054097.3.
DR RefSeq; XP_017169257.1; XM_017313768.1.
DR AlphaFoldDB; Q91XU3; -.
DR SMR; Q91XU3; -.
DR BioGRID; 228173; 32.
DR IntAct; Q91XU3; 15.
DR MINT; Q91XU3; -.
DR STRING; 10090.ENSMUSP00000013970; -.
DR iPTMnet; Q91XU3; -.
DR PhosphoSitePlus; Q91XU3; -.
DR EPD; Q91XU3; -.
DR jPOST; Q91XU3; -.
DR MaxQB; Q91XU3; -.
DR PaxDb; Q91XU3; -.
DR PeptideAtlas; Q91XU3; -.
DR PRIDE; Q91XU3; -.
DR ProteomicsDB; 288205; -.
DR Antibodypedia; 28802; 114 antibodies from 25 providers.
DR DNASU; 117150; -.
DR Ensembl; ENSMUST00000013970; ENSMUSP00000013970; ENSMUSG00000025417.
DR GeneID; 117150; -.
DR KEGG; mmu:117150; -.
DR UCSC; uc007hiq.2; mouse.
DR CTD; 79837; -.
DR MGI; MGI:2152214; Pip4k2c.
DR VEuPathDB; HostDB:ENSMUSG00000025417; -.
DR eggNOG; KOG0229; Eukaryota.
DR GeneTree; ENSGT00940000156890; -.
DR HOGENOM; CLU_004312_7_0_1; -.
DR InParanoid; Q91XU3; -.
DR OMA; SEWDGDC; -.
DR OrthoDB; 1562683at2759; -.
DR PhylomeDB; Q91XU3; -.
DR TreeFam; TF354315; -.
DR BRENDA; 2.7.1.149; 3474.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-MMU-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-8847453; Synthesis of PIPs in the nucleus.
DR BioGRID-ORCS; 117150; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Pip4k2c; mouse.
DR PRO; PR:Q91XU3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q91XU3; protein.
DR Bgee; ENSMUSG00000025417; Expressed in pigmented layer of retina and 274 other tissues.
DR Genevisible; Q91XU3; MM.
DR GO; GO:0005776; C:autophagosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0043229; C:intracellular organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; ISS:UniProtKB.
DR GO; GO:0016309; F:1-phosphatidylinositol-5-phosphate 4-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:1902635; P:1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0090217; P:negative regulation of 1-phosphatidylinositol-4-phosphate 5-kinase activity; ISS:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; ISO:MGI.
DR GO; GO:0010506; P:regulation of autophagy; ISO:MGI.
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 Acetylation; ATP-binding; Cytoplasm; Endoplasmic reticulum; Kinase;
KW Lipid metabolism; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8TBX8"
FT CHAIN 2..421
FT /note="Phosphatidylinositol 5-phosphate 4-kinase type-2
FT gamma"
FT /id="PRO_0000285751"
FT DOMAIN 43..420
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 69..75
FT /note="Required for interaction with PIP5K1A"
FT /evidence="ECO:0000250|UniProtKB:Q8TBX8"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8TBX8"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TBX8"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TBX8"
FT CONFLICT 90
FT /note="H -> R (in Ref. 2; BAE28464)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 47336 MW; 368C9CE0C9EA83D4 CRC64;
MASSSVPPAT APAAAGGPGP GFGFASKTKK KHFVQQKVKV FRAADPLVGV FLWGVAHSIN
ELSQVPPPVM LLPDDFKASS KIKVNNHFFH RENLPSHFKF KEYCPQVFRN LRDRFAIDDH
DYLVSLTRSP PSETEGSDGR FLISYDRTLV IKEVSSEDIA DMHSNLSNYH QYIVKCHGNT
LLPQFLGMYR VSVENEDSYM LVMRNMFSHR LPVHRKYDLK GSLVSREASD KEKVKELPTL
KDMDFLNKNQ KVYIGEEEKK VFLEKLKRDV EFLVQLKIMD YSLLLGIHDI IRGSEPEEEG
PVREEESEWD GDCNLAGPPA LVGSYGTSPE GIGGYIHSHR PLGPGEFESF IDVYAIRSAE
GAPQKEVYFM GLIDILTQYD AKKKAAHAAK TVKHGAGAEI STVHPEQYAK RFLDFIANIF
A
