PI42C_PONAB
ID PI42C_PONAB Reviewed; 421 AA.
AC Q5R488;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma {ECO:0000305};
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; Synonyms=PIP5K2C;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- PTM: Phosphorylated, phosphorylation is induced by EGF.
CC {ECO:0000250|UniProtKB:O88370}.
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DR EMBL; CR861368; CAH93428.1; -; mRNA.
DR RefSeq; NP_001127008.1; NM_001133536.1.
DR AlphaFoldDB; Q5R488; -.
DR SMR; Q5R488; -.
DR STRING; 9601.ENSPPYP00000005349; -.
DR GeneID; 100174032; -.
DR KEGG; pon:100174032; -.
DR CTD; 79837; -.
DR eggNOG; KOG0229; Eukaryota.
DR InParanoid; Q5R488; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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: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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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_0000285752"
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"
SQ SEQUENCE 421 AA; 47235 MW; B591B3E709EA4A16 CRC64;
MASSSVPPAT VSAATTGPGP GFGFASKTKK KHFVQQEVKV FRAADPLVGV FLWGVAHSIN
ELSQVPPPVM LLPDDFKASS KIKVNNHLFH RENLPSHFKF KEYCPQVFRN LRDRFGIDDQ
DYLVSLTRNP PSESEGSDGR FLICYDRTLV IKEVSSEDIA DMHSNLSNYH QYIVKCHGNT
LLPQFLGMYR VSVDNEDSYM LVMRNMFSHR LPVHRKYDLK GSLVSREASD KEKVKELPTL
KGMDFLNKNQ KVYIGEDEKK IFLEKLKRDV EFLVQLKIMD YSLLLGIHDI IRGSEPEEEG
PVREDESEVD GDCSLTGPPA LVGSYGTSPE GIGGYIHSHR PLGPGEFESF IDVHAIRSAE
GAPQKEVYFM GLIDILTQYD AKKKAAHAAK TVKHGAGAEI STVHPEQYAK RFLDFITNIF
A
