P4K2B_XENTR
ID P4K2B_XENTR Reviewed; 492 AA.
AC Q28G26;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=TGas067g11.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-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; CR761607; CAJ83481.1; -; mRNA.
DR RefSeq; NP_001016953.1; NM_001016953.2.
DR AlphaFoldDB; Q28G26; -.
DR SMR; Q28G26; -.
DR STRING; 8364.ENSXETP00000002097; -.
DR PaxDb; Q28G26; -.
DR PRIDE; Q28G26; -.
DR GeneID; 549707; -.
DR KEGG; xtr:549707; -.
DR CTD; 55300; -.
DR Xenbase; XB-GENE-974293; pi4k2b.
DR eggNOG; KOG2381; Eukaryota.
DR InParanoid; Q28G26; -.
DR OrthoDB; 1273723at2759; -.
DR Reactome; R-XTR-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-XTR-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-XTR-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-XTR-1660516; Synthesis of PIPs at the early endosome membrane.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; 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: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..492
FT /note="Phosphatidylinositol 4-kinase type 2-beta"
FT /id="PRO_0000285170"
FT DOMAIN 127..462
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..139
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 160..162
FT /note="Important for substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 168..181
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 271..279
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 308..316
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 353..373
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 368..377
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT COMPBIAS 52..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 264..267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 278..279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
SQ SEQUENCE 492 AA; 55770 MW; A6DD5C61D7734092 CRC64;
MEPKQTADAR DSPPLLVFLE PAAEEVTAHT APLSPNPQSA RAAPGSAVRF FSDSAREEEA
GEDEPLLKKS GPVSPRAARK GRTRLSSSSD RENMSGGHVG NGEFNVILDD LEFADIIHRA
EQAIESGVFP ERISQGSSGS YFVKDPKGKI IGVFKPKSEE PYGHLNPKWT KYFHKICCPC
CFGRGCLVPN QGYLSEAGAY LVDEKLGLGV VPKTKVVWLV SETFNYSAID RAKSRGKKYA
LEKVPKVGRK FHRIGLPPKV GSFQLFVDGY KEADYWLRKF ETDPLPENTR KQLQCQFEKL
VILDYVIRNT DRGNDNWLIR YDSQDDDELM EKGDDFPLKD WKEIKEPVIK IAAIDNGLAF
PFKHPDEWRA YPFHWAWLPQ AKVPFSQETR DLILPRISDM NFVQDLCEDL YELFKTDKGF
DKATFEKQMS VMRGQILNLT QALKDGKTPI QLVQMPRVVV ERSCSGSQGR IVQMSNAFTQ
TFHCRKPFFS SW
