PI42C_BOVIN
ID PI42C_BOVIN Reviewed; 421 AA.
AC Q0P5F7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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}.
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; BC120101; AAI20102.1; -; mRNA.
DR RefSeq; NP_001069664.1; NM_001076196.1.
DR AlphaFoldDB; Q0P5F7; -.
DR SMR; Q0P5F7; -.
DR STRING; 9913.ENSBTAP00000005146; -.
DR PaxDb; Q0P5F7; -.
DR PRIDE; Q0P5F7; -.
DR Ensembl; ENSBTAT00000005146; ENSBTAP00000005146; ENSBTAG00000003942.
DR GeneID; 540005; -.
DR KEGG; bta:540005; -.
DR CTD; 79837; -.
DR VEuPathDB; HostDB:ENSBTAG00000003942; -.
DR VGNC; VGNC:32908; PIP4K2C.
DR eggNOG; KOG0229; Eukaryota.
DR GeneTree; ENSGT00940000156890; -.
DR HOGENOM; CLU_004312_7_0_1; -.
DR InParanoid; Q0P5F7; -.
DR OMA; SEWDGDC; -.
DR OrthoDB; 1562683at2759; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000003942; Expressed in thyroid gland and 104 other tissues.
DR GO; GO:0005776; C:autophagosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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; 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:0042802; F:identical protein binding; IEA:Ensembl.
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: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; IEA:Ensembl.
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_0000285749"
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 REGION 294..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 47142 MW; 2C567240657C2242 CRC64;
MASSSVPPTA VPAATAAPGA GFGFASKTKK KHFVQQKVKV FRAADPLVGV FLWGVAHSIN
ELSQVPPPVM LLPDDFKASS KIKVNNHLFH RENLPSHFKF KEYCPQVFRN LRDRFGIDDQ
DYLVSLTRSP PTESEGSDGR FLISYDRTLV IKEVSSEDIA DMHSNLSNYH QYIVKCHGNT
LLPQFLGMYR VSVDSEDSYM LVMRNMFSHR LPVHRKYDLK GSLVSREASD KEKVKELPTL
KDMDFLNKNQ KVYIGEEEKK VFLEKLKRDV EFLVQLKIMD YSLLLGIHDI IRGSEPEEDG
PVREEESEGD GDCGLTGPPA PVGSYGTSPE GIGGYIHSHR PLGPGEFESF IDVYAIRSAE
GAPQKEVYFM GLIDILTQYD AKKKAAHAAK TVKHGAGAEI STVHPEQYAK RFLDFITNIF
A
