P4K2B_CHICK
ID P4K2B_CHICK Reviewed; 479 AA.
AC Q5ZIK0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=RCJMB04_25j21;
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: 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ720784; CAG32443.1; -; mRNA.
DR RefSeq; NP_001026328.1; NM_001031157.1.
DR AlphaFoldDB; Q5ZIK0; -.
DR SMR; Q5ZIK0; -.
DR STRING; 9031.ENSGALP00000023196; -.
DR PaxDb; Q5ZIK0; -.
DR GeneID; 422807; -.
DR KEGG; gga:422807; -.
DR CTD; 55300; -.
DR VEuPathDB; HostDB:geneid_422807; -.
DR eggNOG; KOG2381; Eukaryota.
DR InParanoid; Q5ZIK0; -.
DR OrthoDB; 1273723at2759; -.
DR PhylomeDB; Q5ZIK0; -.
DR PRO; PR:Q5ZIK0; -.
DR Proteomes; UP000000539; 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..479
FT /note="Phosphatidylinositol 4-kinase type 2-beta"
FT /id="PRO_0000285167"
FT DOMAIN 118..449
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..130
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 151..153
FT /note="Important for substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 159..172
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 262..270
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 299..307
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 340..360
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 355..364
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT COMPBIAS 44..58
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 255..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 269..270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
SQ SEQUENCE 479 AA; 53922 MW; 2CB1742BB38BCF70 CRC64;
MESGSEEPDE QLLLLSEPAL HAGPPAGRAA PGGAVRLRGE PGLEEEEEGE EDSGPEGDGE
EEPLLRASGR GRRAGAARDK EPRVGAGHTG HAIDMNTFLD DPEFAEIITR AEQVIECGVL
PERISQGSSG SYFVKDCKGK TIGVFKPKSE EPYGHLNPKW TKYFHKICCP CCFGRGCLVP
NQGYLSEAGA YLVDDKLGLG VVPKTKVVWL VSETFNYSAI DRAKSRGKKY ALEKVPKVAK
KFNRIGLPPK VGSFQLFVEG YKEADYWLRK FETDPLPENT RKEFQSQFER LVILDYVIRN
TDRGNDNWLV RYEKQDDGLN LSDKDIQWTV TEESTIKIAA IDNGLAFPFK HPDEWRAYPF
HWAWLSQAQV PFSQETRDLV LPRISDMNFV QDLCEDLHEL FKTDKGFDKA TFENQMSVMR
GQILNLTQAL KDGKSPIQLV QMPRVIVERS STGSQGRIVH LSNAFTQTFH SRKPFFSSW
