P4K2B_RAT
ID P4K2B_RAT Reviewed; 477 AA.
AC Q5XIL2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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;
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=Testis;
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).
CC -!- FUNCTION: Together with PI4K2A and the type III PI4Ks (PIK4CA and
CC PIK4CB) it 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 Contributes to the production of InsP3 in stimulated cells and is
CC likely to be involved in the regulation of vesicular trafficking.
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}. Note=Mainly cytosolic, association with
CC membranes of the Golgi, endoplasmic and plasma membrane is stimulated
CC by active RAC1. Association with early endosomes has not been
CC confirmed. {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; BC083668; AAH83668.1; -; mRNA.
DR RefSeq; NP_001005883.1; NM_001005883.1.
DR AlphaFoldDB; Q5XIL2; -.
DR SMR; Q5XIL2; -.
DR STRING; 10116.ENSRNOP00000005349; -.
DR SwissPalm; Q5XIL2; -.
DR PaxDb; Q5XIL2; -.
DR Ensembl; ENSRNOT00000005349; ENSRNOP00000005349; ENSRNOG00000003924.
DR GeneID; 305419; -.
DR KEGG; rno:305419; -.
DR CTD; 55300; -.
DR RGD; 1359515; Pi4k2b.
DR eggNOG; KOG2381; Eukaryota.
DR GeneTree; ENSGT00390000010434; -.
DR HOGENOM; CLU_032516_1_0_1; -.
DR InParanoid; Q5XIL2; -.
DR OMA; FHWAWLS; -.
DR OrthoDB; 1273723at2759; -.
DR PhylomeDB; Q5XIL2; -.
DR TreeFam; TF314740; -.
DR Reactome; R-RNO-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-RNO-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-RNO-1660516; Synthesis of PIPs at the early endosome membrane.
DR PRO; PR:Q5XIL2; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000003924; Expressed in duodenum and 19 other tissues.
DR Genevisible; Q5XIL2; RN.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISO:RGD.
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 Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..477
FT /note="Phosphatidylinositol 4-kinase type 2-beta"
FT /id="PRO_0000285166"
FT DOMAIN 116..447
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..128
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 149..151
FT /note="Important for substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 157..170
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 260..268
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 297..305
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 338..358
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 353..362
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 253..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 267..268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
SQ SEQUENCE 477 AA; 54464 MW; BCC6EECB4594F652 CRC64;
MPEPPRDIMA EACEATRPSE DEDEEREPLL PRVAWAQPRR GAPGSAVRLQ ADQGAAVLRE
PATEEPPVVS EDRSISASLS TELDRTRNAV SETNTFLEDP EFADVVLKAE QAIEIGVFPE
RISQGSSGSY FVKDSKRTII GVFKPKSEEP YGQLNPKWTK YVHKVCCPCC FGRGCLLPNQ
GYLSEAGAYL VDTKLQLGIV PKTKVVWLVS ETFNYSAIDR AKSRGKKYAL EKVPKVGRKF
HRIGLPPKIG SFQLFVKDYK EAEYWLRRFE AEPLPENIRK QFQSQFERLV ILDYIIRNTD
RGNDNWLVKY DEMKYAKKIE SEESNWIDDK QLLIRIAAID NGLAFPFKHP DEWRAYPFHW
AWLPQAKVPF SEETRNLILP FISDMNFVQD LCEDLYELFK TDKGFDRAAF ESQMSVMRGQ
ILNLTQALRD GKSPMQLAQM PCVIVECSKS GGQGRVVHLG SSFTQTVHCR KPFFSSW
