PI42C_RAT
ID PI42C_RAT Reviewed; 420 AA.
AC O88370;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma {ECO:0000305};
DE EC=2.7.1.149 {ECO:0000269|PubMed:9685379};
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|RGD:621711}; Synonyms=Pip5k2c;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, TISSUE SPECIFICITY, FUNCTION,
RP AND CATALYTIC ACTIVITY.
RX PubMed=9685379; DOI=10.1074/jbc.273.32.20292;
RA Itoh T., Ijuin T., Takenawa T.;
RT "A novel phosphatidylinositol-5-phosphate 4-kinase (phosphatidylinositol-
RT phosphate kinase IIgamma) is phosphorylated in the endoplasmic reticulum in
RT response to mitogenic signals.";
RL J. Biol. Chem. 273:20292-20299(1998).
CC -!- FUNCTION: Phosphatidylinositol 5-phosphate 4-kinase with low enzymatic
CC activity (PubMed:9685379). May be a GTP sensor, has higher GTP-
CC dependent kinase activity than ATP-dependent kinase activity (By
CC similarity). PIP4Ks negatively regulate insulin signaling through a
CC catalytic-independent mechanism. They interact with PIP5Ks and suppress
CC PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-dependent conversion
CC to PtdIns(3,4,5)P3 (By similarity). {ECO:0000250|UniProtKB:Q8TBX8,
CC ECO:0000269|PubMed:9685379}.
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:0000269|PubMed:9685379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12281;
CC Evidence={ECO:0000305|PubMed:9685379};
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:0000269|PubMed:9685379}. Cytoplasm {ECO:0000269|PubMed:9685379}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with the most abundant expression
CC in kidney. {ECO:0000269|PubMed:9685379}.
CC -!- PTM: Phosphorylated, phosphorylation is induced by EGF.
CC {ECO:0000269|PubMed:9685379}.
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DR EMBL; AF030558; AAC40202.1; -; mRNA.
DR RefSeq; NP_536728.2; NM_080480.2.
DR AlphaFoldDB; O88370; -.
DR SMR; O88370; -.
DR STRING; 10116.ENSRNOP00000061758; -.
DR iPTMnet; O88370; -.
DR PhosphoSitePlus; O88370; -.
DR jPOST; O88370; -.
DR PaxDb; O88370; -.
DR PRIDE; O88370; -.
DR GeneID; 140607; -.
DR KEGG; rno:140607; -.
DR UCSC; RGD:621711; rat.
DR CTD; 79837; -.
DR RGD; 621711; Pip4k2c.
DR VEuPathDB; HostDB:ENSRNOG00000005138; -.
DR eggNOG; KOG0229; Eukaryota.
DR InParanoid; O88370; -.
DR OrthoDB; 1562683at2759; -.
DR PhylomeDB; O88370; -.
DR Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-RNO-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-RNO-8847453; Synthesis of PIPs in the nucleus.
DR PRO; PR:O88370; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000005138; Expressed in adult mammalian kidney and 19 other tissues.
DR ExpressionAtlas; O88370; baseline and differential.
DR Genevisible; O88370; RN.
DR GO; GO:0005776; C:autophagosome; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0043229; C:intracellular organelle; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IDA:RGD.
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:RGD.
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:0006661; P:phosphatidylinositol biosynthetic process; NAS:RGD.
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:RGD.
DR GO; GO:0010506; P:regulation of autophagy; ISO:RGD.
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..420
FT /note="Phosphatidylinositol 5-phosphate 4-kinase type-2
FT gamma"
FT /id="PRO_0000285753"
FT DOMAIN 43..419
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"
SQ SEQUENCE 420 AA; 47049 MW; BDB07F67FA81E943 CRC64;
MASSSVPPAT APAAAGGPGP GFGFASKTKK KHFVQQKVKV FRAADPLVGV FLWGVAHSIN
ELSQVPPPVM LLPDDFKASS KIKVNNHLFH RENLPSHFKF KEYCPQVFRN LRDRFAIDDH
DYLVSLTRSP PSETEGSDGR FLISYDRTLV IKEVSSEDIA DMHSNLSNYH QYIVKCHGNT
LLPQFLGMYR VSVENEDSYM LVMRNMFSHR LPVHRKYDLK GSLVSREASD KEKVKELPTL
KDMDFLNKNQ KVYIGEEEKK VFLEKLKRDV EFLVQLKIMD YSLLLGIHDI IRGSEPEEEG
PVREEESEWD GDCNLTGPPA LVGSYGTSPE GIGGYIHSHR PLGPGEFESF IDVYAIRSAE
GAPEGGVFHG LIDILTQYDA KKKAAHAAKT VKHGAGAEIS TVHPEQYAKR FLDFISNIFA
