P4K2B_XENLA
ID P4K2B_XENLA Reviewed; 495 AA.
AC Q6DCQ8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) 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; BC077943; AAH77943.1; -; mRNA.
DR RefSeq; NP_001087050.1; NM_001093581.1.
DR AlphaFoldDB; Q6DCQ8; -.
DR SMR; Q6DCQ8; -.
DR MaxQB; Q6DCQ8; -.
DR DNASU; 446885; -.
DR GeneID; 446885; -.
DR KEGG; xla:446885; -.
DR CTD; 446885; -.
DR Xenbase; XB-GENE-974298; pi4k2b.L.
DR OMA; ENYAMES; -.
DR OrthoDB; 1273723at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 446885; Expressed in oocyte and 19 other tissues.
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:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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: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..495
FT /note="Phosphatidylinositol 4-kinase type 2-beta"
FT /id="PRO_0000285169"
FT DOMAIN 130..465
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..142
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 163..165
FT /note="Important for substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 171..184
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 274..282
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 311..319
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 356..376
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 371..380
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT COMPBIAS 54..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 267..270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 281..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
SQ SEQUENCE 495 AA; 56349 MW; 4BE57BC43D3F34E0 CRC64;
MEQKQTTEPR DSPPLLVLLD PAAEQLEVSA PHTPLSPQPQ SARAAPGSAV RFFCDSAREE
EAGEDEPLLK KPGPMSPRAV RKGRTRLSSS SDDRENMSSG HVENGEYNVI LNDPEFADII
HRAEQAIESG VFPERISQGS SGSYFVKDPK GKIIGVFKPK SEEPYGHLNP KWTKYFHKIC
CPCCFGRGCL VPNQGYLSEA GAYLVDEKLG LGVVPKTKAV WLVSETFNYS AIDRAKSRGK
KYALEKVPKV GKKFHRIGLP PKVGSFQLFV DGYKEADYWL RKFETDPLPE NTRKQLQSPF
EKLVILDYVI RNTDRGNDNW LIRYDSQDDD ELSEKGDSFP LKDWKEIKEP IIKIAAIDNG
LAFPFKHPDE WRAYPFHWAW LPQAKVPFSQ ETRDLILPRI SDMNFIQDLC EDLYELFKTD
KGFDKDTFEK QMSVMRGQIL NLTQALKDGK TPIQLVQMPR VVVERSYSGS QGRIVQMSNA
FTQTFHCRKP FFSSW
