PI42C_XENTR
ID PI42C_XENTR Reviewed; 419 AA.
AC Q6GL14; Q28EX3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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; ORFNames=TGas097l11.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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. {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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAJ83604.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR762295; CAJ83604.1; ALT_INIT; mRNA.
DR EMBL; BC074705; AAH74705.1; -; mRNA.
DR RefSeq; NP_001005670.1; NM_001005670.1.
DR AlphaFoldDB; Q6GL14; -.
DR SMR; Q6GL14; -.
DR STRING; 8364.ENSXETP00000013678; -.
DR PaxDb; Q6GL14; -.
DR DNASU; 448167; -.
DR GeneID; 448167; -.
DR KEGG; xtr:448167; -.
DR CTD; 79837; -.
DR Xenbase; XB-GENE-964849; pip4k2c.
DR eggNOG; KOG0229; Eukaryota.
DR InParanoid; Q6GL14; -.
DR OrthoDB; 1562683at2759; -.
DR Reactome; R-XTR-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-XTR-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-XTR-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-XTR-8847453; Synthesis of PIPs in the nucleus.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
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 ATP-binding; Cytoplasm; Endoplasmic reticulum; Kinase; Lipid metabolism;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..419
FT /note="Phosphatidylinositol 5-phosphate 4-kinase type-2
FT gamma"
FT /id="PRO_0000285756"
FT DOMAIN 46..418
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 299..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 419 AA; 47642 MW; 5F39589CF7868E2A CRC64;
MSSSGAMPAV SSASSSAAVG ILSATTAKTK TKKKHFVQQK VKVFRASDPL ISVFMWGVNH
SVNELIQVPV PVMLLPDDFK ANSKIKVTNH LFNRENLPSH FKFKDYCPQV FRNLRERFGI
DDQDFQASLT RSSPYCESEG HDGRFLLSYD KTLVIKEISS EDVADMHNIL SHYHQHIVKC
HGNTLLPQFL GMYRLSVDNE DSYIMVMRNM FSHRLTVHRK YDLKGSLVSR EASDKEKIKE
LPTLKDMDFL NKSQKVYVDE EQKKNFMEKL KRDVDFLVQL KLMDYSLLLG IHEVFRAEQE
EEEDLEEDHT ENESSPHMNV GSYGTSPEGI AGYLNSHKPL GPGEFEPIID VYAIKSSDNA
PQKEVYFMGL IDILTHYDAK KKAAHAAKTV KHGAGAEIST VHPDQYGKRF LEFVTNIFA
