PI42C_XENLA
ID PI42C_XENLA Reviewed; 419 AA.
AC Q5PQ01;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-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}.
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DR EMBL; BC087421; AAH87421.1; -; mRNA.
DR RefSeq; NP_001088764.1; NM_001095295.1.
DR AlphaFoldDB; Q5PQ01; -.
DR SMR; Q5PQ01; -.
DR DNASU; 496028; -.
DR GeneID; 496028; -.
DR KEGG; xla:496028; -.
DR CTD; 496028; -.
DR Xenbase; XB-GENE-964855; pip4k2c.S.
DR OrthoDB; 1562683at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 496028; Expressed in testis and 18 other tissues.
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: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_0000285755"
FT DOMAIN 46..418
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
SQ SEQUENCE 419 AA; 47651 MW; F4F138473C7B215A CRC64;
MSSSGAMPAV SSTSSSAAVG ILSATTAKTK TKKKHFVQQK VKVFRASDPL ISVLMWGVNH
SVNELIQVPV PVMLLPDDFK ANSKIKVTNH LFNRENLPSH FKFKDYCPQV FRNLRERFGI
DDQDFQVSLT RSSPYCESEG HDGRFLLSYD KTLVIKEISS EDVADMHIIL SHYHQHIVKC
HESTLLPQFL GMYRLSVDNE DSYIIVMRNM FSHRLTVHRK YDLKGSLVSR EASDKEKVKE
LPTLKDMDFL NKSQKVYVDE EQKRNFMEKL KRDVDFLVQL KLMDYSLLLG IHEVFRAEQE
EEEELEEDNA ENECSPHVNV GSYGTSPEGI AGYLNSHKPL GPGEFEPIID VYAIKSSDNA
PQKEVYFMGL IDILTHYDAK KKAAHAAKTV KHGAGAEIST VHPDQYGKRF LEFVTNIFA
