PI51B_CHICK
ID PI51B_CHICK Reviewed; 540 AA.
AC Q5ZJ58;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 beta {ECO:0000250|UniProtKB:P70181};
DE Short=PIP5KIbeta {ECO:0000250|UniProtKB:P70181};
DE AltName: Full=Type I phosphatidylinositol 4-phosphate 5-kinase beta {ECO:0000250|UniProtKB:P70181};
GN Name=PIP5K1B; ORFNames=RCJMB04_20j15;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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). {ECO:0000250|UniProtKB:P70181,
CC 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 -!- 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}.
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DR EMBL; AJ720576; CAG32235.1; -; mRNA.
DR RefSeq; NP_001026593.1; NM_001031422.1.
DR AlphaFoldDB; Q5ZJ58; -.
DR SMR; Q5ZJ58; -.
DR STRING; 9031.ENSGALP00000037435; -.
DR PaxDb; Q5ZJ58; -.
DR GeneID; 427243; -.
DR KEGG; gga:427243; -.
DR CTD; 8395; -.
DR VEuPathDB; HostDB:geneid_427243; -.
DR eggNOG; KOG0229; Eukaryota.
DR InParanoid; Q5ZJ58; -.
DR OrthoDB; 1562683at2759; -.
DR PhylomeDB; Q5ZJ58; -.
DR PRO; PR:Q5ZJ58; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; Cell membrane; Cytoplasm; Kinase; Lipid metabolism; Membrane;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..540
FT /note="Phosphatidylinositol 4-phosphate 5-kinase type-1
FT beta"
FT /id="PRO_0000185461"
FT DOMAIN 25..395
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 60719 MW; 5F9720849533D784 CRC64;
MSSVTENGDV TAGKPNEEKT YKKTTSSAIK GAIQLGIGYT VGNLTSKPDR DVLMQDFYVV
ESVFLPSEGS NLTPAHHYPD FRFKTYAPLA FRYFRELFGI KPDDYLYSIC SEPLIELSNP
GASGSLFFVT SDDEFIIKTV QHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCVQSGG
INIRIVVMNN VLPRALKMNF TYDLKGSTYK RRASRKEREK SNPTFKDLDF LQDMHEGLYF
DSETHSALMK TLQRDCRVLE SFKIMDYSLL LGIHVLNSNV REKEGESSQN ASDGKRPGGQ
KVLYSTAMES IQGPGKSGDS VVTETTNTMG GIPAKSHKGE KLLLFMGIID ILQSYRLMKK
LEHSWKALVY DGDTVSVHRP SFYADRFLKF MNTRVFKKVQ ALRSSPSKKR CNSITALKAT
SQEIVSAVSQ EWKDEKHSII TEGQSYSSLD EEVLGSRRRP DLVPSTPSLF EAASLATTVS
SSSLNVDERY QRDQTMLYSS SKELPSSSTF TLEDSAIYLT SEQSTLETEN DNASVLDVYL
