P4K2B_DANRE
ID P4K2B_DANRE Reviewed; 501 AA.
AC Q49GP5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Phosphatidylinositol 4-kinase type 2-beta;
DE EC=2.7.1.67 {ECO:0000250|UniProtKB:Q8TCG2};
DE AltName: Full=Phosphatidylinositol 4-kinase type II-beta;
GN Name=pi4k2b; ORFNames=zgc:158305;
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 [MRNA].
RA Ma H., Balla T.;
RT "Phosphatidylinositol 4-kinases of Danio rerio.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Contributes to the overall PI4-kinase activity of the cell.
CC This contribution may be especially significant in plasma membrane,
CC endosomal and Golgi compartments. The phosphorylation of
CC phosphatidylinositol (PI) to PI4P is the first committed step in the
CC generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor
CC of the second messenger inositol 1,4,5-trisphosphate (InsP3).
CC {ECO:0000250|UniProtKB:Q8TCG2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67; Evidence={ECO:0000250|UniProtKB:Q8TCG2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC Evidence={ECO:0000250|UniProtKB:Q8TCG2};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8TCG2}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8TCG2}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8TCG2}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8TCG2}. Cell membrane
CC {ECO:0000250|UniProtKB:Q8TCG2}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q8TCG2}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; AY929291; AAY16566.1; -; mRNA.
DR EMBL; BC129195; AAI29196.1; -; mRNA.
DR RefSeq; NP_001038950.1; NM_001045485.2.
DR AlphaFoldDB; Q49GP5; -.
DR SMR; Q49GP5; -.
DR STRING; 7955.ENSDARP00000038731; -.
DR PaxDb; Q49GP5; -.
DR GeneID; 564750; -.
DR KEGG; dre:564750; -.
DR CTD; 55300; -.
DR ZFIN; ZDB-GENE-070112-990; pi4k2b.
DR eggNOG; KOG2381; Eukaryota.
DR InParanoid; Q49GP5; -.
DR OrthoDB; 1273723at2759; -.
DR PhylomeDB; Q49GP5; -.
DR Reactome; R-DRE-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-DRE-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-DRE-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-DRE-1660516; Synthesis of PIPs at the early endosome membrane.
DR PRO; PR:Q49GP5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0033339; P:pectoral fin development; IMP:ZFIN.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR039756; Lsb6/PI4K2.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR PANTHER; PTHR12865; PTHR12865; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Cytoplasm; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; Kinase; Lipid metabolism; Membrane; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..501
FT /note="Phosphatidylinositol 4-kinase type 2-beta"
FT /id="PRO_0000285168"
FT DOMAIN 141..471
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..153
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 174..176
FT /note="Important for substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 182..195
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 285..293
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 322..330
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 362..382
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 377..386
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 278..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 292..293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
SQ SEQUENCE 501 AA; 56199 MW; 1E615C79533140B4 CRC64;
MMAECDPTDG EPGNGSGDST PETNFLSSEV PAVLFEKTRS APSLGLSLNP GAAVRISDST
ESVLTELEAD GSGEEALLLP GPAGSLSPRA GKEKRTRRNM LSSSSDNLAS PGNSSGEFNH
FPEDPEFGEI IQRAEQAIEN GVFPERISQG SSGSYFVKDP KGKIIGVFKP KSEEPYGHLN
PKWTKYFHKV CCPCCFGRGC LIPNQGYLSE AAASLVDQKL GLWIVPKTKV VHLASETFHY
NAIDRAKSRG KKYALEKVPK VGRRFHRVGL PPKVGSFQLF VEGYHEADFW LRKFEAEPLP
ENMRKQLQSQ FERLVVLDYV IRNTDRGNDN WLIKYEKPGD GELTEKESEW TDPKDSAIKI
AAIDNGLAFP FKHPDEWRAY PFHWAWLPQA KVAFSQETRD LVLSRISDMN FVQDLCEDLY
EMFRTDKGFD KTMFEKQMSV MRGQILNLTQ ALKDGKSPIQ LVQMPRVVVE RSRSGGQGRV
VQLGNAFTQT FHCKRPFFTS W
