PI42C_DANRE
ID PI42C_DANRE Reviewed; 416 AA.
AC Q6IQE1; Q7ZVF5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=pip5k2, pip5k2c;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC045883; AAH45883.1; -; mRNA.
DR EMBL; BC071466; AAH71466.1; -; mRNA.
DR RefSeq; NP_956395.2; NM_200101.2.
DR AlphaFoldDB; Q6IQE1; -.
DR SMR; Q6IQE1; -.
DR STRING; 7955.ENSDARP00000042700; -.
DR PaxDb; Q6IQE1; -.
DR PRIDE; Q6IQE1; -.
DR GeneID; 373124; -.
DR KEGG; dre:373124; -.
DR CTD; 373124; -.
DR ZFIN; ZDB-GENE-030828-9; pip4k2ca.
DR eggNOG; KOG0229; Eukaryota.
DR InParanoid; Q6IQE1; -.
DR OrthoDB; 1562683at2759; -.
DR PhylomeDB; Q6IQE1; -.
DR Reactome; R-DRE-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-DRE-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-DRE-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-DRE-8847453; Synthesis of PIPs in the nucleus.
DR PRO; PR:Q6IQE1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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..416
FT /note="Phosphatidylinositol 5-phosphate 4-kinase type-2
FT gamma"
FT /id="PRO_0000285754"
FT DOMAIN 38..415
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT CONFLICT 94
FT /note="E -> K (in Ref. 1; AAH45883)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="V -> I (in Ref. 1; AAH45883)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 47379 MW; 3AD56CEC182438A5 CRC64;
MASLGNSGSA SSPMVMLAPK TKTKKRHFMQ QKVKVFRASD PMLSVFMWGV NHSINDLNQV
PVPVMLLPDD FKANTKIKVN NHLFNKENLP SHFEFKEYCP QVFRNLRERF GIEDLDYQAS
LARSAPMKGD GQGEGLLFTS YDRTLIVKQI SSEEVADMHN ILSEYHQHIV KCHGSTLLPQ
FLGMYRITVE SEDTYLIVMR NMFSHRLLVH RKYDLKGSLV DREASDKEKV KELPTFKDMD
FRNNMQKVYV TEEQKEKMME KLNRDVEFLV KLKIMDYSLL LGIHDVARGE REEEEAEEPC
YEDDADPENG LAPALQVGSY GTSPEGIAGY MNSIKPLGPG EFDPYIDVYA VKSAPGAPQR
EVYFMGLIDV LTQYDTKKKA AHAAKTVKHG AGAEISTVHP EQYAKRFREF ISNIFA
