PI51B_RAT
ID PI51B_RAT Reviewed; 539 AA.
AC Q5CZZ9;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase type-1 beta {ECO:0000250|UniProtKB:P70181};
DE Short=PIP5K1-beta {ECO:0000250|UniProtKB:P70181};
DE Short=PtdIns(4)P-5-kinase 1 beta {ECO:0000250|UniProtKB:P70181};
DE EC=2.7.1.68 {ECO:0000250|UniProtKB:P70181};
DE AltName: Full=Phosphatidylinositol 4-phosphate 5-kinase type I alpha {ECO:0000312|EMBL:AAH90349.1};
DE Short=PIP5KIalpha {ECO:0000312|EMBL:AAH90349.1};
DE AltName: Full=Phosphatidylinositol 4-phosphate 5-kinase type I beta {ECO:0000250|UniProtKB:P70181};
DE Short=PIP5KIbeta {ECO:0000250|UniProtKB:P70181};
GN Name=Pip5k1b {ECO:0000312|RGD:1310914};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445 AND SER-448, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-
CC phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-
CC bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that
CC regulates several cellular processes such as signal transduction,
CC vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and
CC cell motility (By similarity). PtdIns(4,5)P2 can directly act as a
CC second messenger or can be utilized as a precursor to generate other
CC second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol
CC (DAG) or phosphatidylinositol-3,4,5-trisphosphate
CC (PtdIns(3,4,5)P3/PIP3) (By similarity). Mediates RAC1-dependent
CC reorganization of actin filaments. Contributes to the activation of
CC phospholipase PLD2. Together with PIP5K1A, is required, after
CC stimulation by G-protein coupled receptors, for the synthesis of IP3
CC that will induce stable platelet adhesion (By similarity).
CC {ECO:0000250|UniProtKB:P70181, ECO:0000250|UniProtKB:Q99755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14426;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-
CC 3-phospho-1D-myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol
CC 4,5-bisphosphate + ADP + H(+); Xref=Rhea:RHEA:40363,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77136,
CC ChEBI:CHEBI:77137, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40364;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-
CC myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-
CC sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40367, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:77139, ChEBI:CHEBI:77140, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40368;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-
CC myo-inositol + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phospho-1D-myo-inositol 5-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40379, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:77163, ChEBI:CHEBI:77164, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40380;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phospho-1D-myo-inositol + ATP = 1-octadecanoyl-2-(9Z,12Z)-
CC octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate +
CC ADP + H(+); Xref=Rhea:RHEA:40383, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77158, ChEBI:CHEBI:77159,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P70181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40384;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phospho-(1D-myo-inositol) + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate +
CC ADP + H(+); Xref=Rhea:RHEA:40375, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77160, ChEBI:CHEBI:133606,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P70181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40376;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-
CC inositol + ATP = 1,2-di(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-
CC 1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40387,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77165,
CC ChEBI:CHEBI:77167, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40388;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC -!- SUBUNIT: Interacts with RAC1, AJUBA, PLD1, PLD2 and ARF1.
CC {ECO:0000250|UniProtKB:P70181}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P70181}. Cell membrane
CC {ECO:0000250|UniProtKB:P70181}. Endomembrane system. Note=Associated
CC with membranes. {ECO:0000250}.
CC -!- CAUTION: There is confusion in the literature with phosphatidylinositol
CC 4-phosphate 5-kinase type I nomenclature due to the fact that
CC frequently mouse PIP5K1B is named Phosphatidylinositol 4-phosphate 5-
CC kinase type I alpha. {ECO:0000305}.
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DR EMBL; BC090349; AAH90349.1; -; mRNA.
DR RefSeq; NP_001012761.1; NM_001012743.1.
DR RefSeq; XP_017444762.1; XM_017589273.1.
DR AlphaFoldDB; Q5CZZ9; -.
DR SMR; Q5CZZ9; -.
DR STRING; 10116.ENSRNOP00000063506; -.
DR iPTMnet; Q5CZZ9; -.
DR PhosphoSitePlus; Q5CZZ9; -.
DR PaxDb; Q5CZZ9; -.
DR PRIDE; Q5CZZ9; -.
DR GeneID; 309419; -.
DR KEGG; rno:309419; -.
DR CTD; 8395; -.
DR RGD; 1310914; Pip5k1b.
DR VEuPathDB; HostDB:ENSRNOG00000015232; -.
DR eggNOG; KOG0229; Eukaryota.
DR InParanoid; Q5CZZ9; -.
DR OMA; NSNMKER; -.
DR OrthoDB; 1562683at2759; -.
DR PhylomeDB; Q5CZZ9; -.
DR TreeFam; TF319618; -.
DR Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-RNO-201688; WNT mediated activation of DVL.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR PRO; PR:Q5CZZ9; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000015232; Expressed in jejunum and 17 other tissues.
DR ExpressionAtlas; Q5CZZ9; baseline and differential.
DR Genevisible; Q5CZZ9; RN.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001931; C:uropod; ISO:RGD.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISO:RGD.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISO:RGD.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cytoplasm; Kinase; Lipid metabolism; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..539
FT /note="Phosphatidylinositol 4-phosphate 5-kinase type-1
FT beta"
FT /id="PRO_0000185460"
FT DOMAIN 25..395
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70181"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 539 AA; 60733 MW; EB3F487BAD88A350 CRC64;
MSSTAENGDA VPGKQNEEKT YKKTASSAIK GAIQLGIGYT VGNLTSKPER DVLMQDFYVV
ESVFLPSEGS NLTPAHHYPD FRFKTYAPLA FRYFRELFGI KPDDYLYSIC SEPLIELSNP
GASGSLFFLT SDDEFIIKTV QHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCMQSGG
INIRIVVMNN VLPRAMRMHL TYDLKGSTYK RRASRKEREK PNPTFKDLDF LQDMHEGLYF
DTETYNALMK TLQRDCRVLE SFKIMDYSLL LGIHILDHSL KDKEEEPLQN APDAKRPGMQ
KVLYSTAMES IQGPGKSADG IIAENPDTMG GIPAKSHKGE KLLLFMGIID ILQSYRLMKK
LEHSWKALVY DGDTVSVHRP SFYADRFLKF MNSRVFKKIQ ALKASPSKKR CNSIAALKAT
SQEILSSISQ EWKDEKQDLL TEGQSFSSLD EEALGSRHRP DLVPSTPSLF EAASLATTIS
SSSLYVGEHY PHDRTTLYSN SKGLPSSSTF TLEEGTIYLT AEPNALETQD DASVLDVYL
