P4K2A_XENLA
ID P4K2A_XENLA Reviewed; 469 AA.
AC Q08B31;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Phosphatidylinositol 4-kinase type 2-alpha;
DE EC=2.7.1.67 {ECO:0000250|UniProtKB:Q9BTU6};
DE AltName: Full=Phosphatidylinositol 4-kinase type II-alpha;
GN Name=pi4k2a;
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 (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Membrane-bound phosphatidylinositol-4 kinase (PI4-kinase)
CC that catalyzes the phosphorylation of phosphatidylinositol (PI) to
CC phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important
CC roles in endocytosis, Golgi function, protein sorting and membrane
CC trafficking. Besides, phosphorylation of phosphatidylinositol (PI) to
CC phosphatidylinositol 4-phosphate (PI4P) is the first committed step in
CC the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a
CC precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3).
CC {ECO:0000250|UniProtKB:Q9BTU6}.
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:Q9BTU6};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q9BTU6}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9BTU6}. Membrane raft
CC {ECO:0000250|UniProtKB:Q9BTU6}. Endosome
CC {ECO:0000250|UniProtKB:Q99M64}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q99M64}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q2TBE6}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q2TBE6}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:Q2TBE6}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q2TBE6}. Membrane
CC {ECO:0000250|UniProtKB:Q2TBE6}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9BTU6}. Perikaryon
CC {ECO:0000250|UniProtKB:Q2TBE6}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q2TBE6}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; BC124897; AAI24898.1; -; mRNA.
DR RefSeq; NP_001121279.1; NM_001127807.1.
DR AlphaFoldDB; Q08B31; -.
DR SMR; Q08B31; -.
DR MaxQB; Q08B31; -.
DR DNASU; 100158362; -.
DR GeneID; 100158362; -.
DR KEGG; xla:100158362; -.
DR CTD; 100158362; -.
DR Xenbase; XB-GENE-866066; pi4k2a.L.
DR OMA; YIIRNTX; -.
DR OrthoDB; 1273723at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 100158362; Expressed in spleen and 19 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0035838; C:growing cell tip; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0031224; C:intrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; ISS:UniProtKB.
DR GO; GO:0035651; F:AP-3 adaptor complex binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISS:UniProtKB.
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; Cell projection; Cytoplasmic vesicle; Endosome;
KW Golgi apparatus; Kinase; Lipid metabolism; Lipoprotein; Membrane;
KW Mitochondrion; Nucleotide-binding; Palmitate; Phosphoprotein;
KW Reference proteome; Synapse; Synaptosome; Transferase.
FT CHAIN 1..469
FT /note="Phosphatidylinositol 4-kinase type 2-alpha"
FT /id="PRO_0000285162"
FT DOMAIN 115..443
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 50..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..127
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 148..150
FT /note="Important for substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 156..169
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 259..267
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 296..304
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 334..354
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 349..358
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT COMPBIAS 10..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 252..255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT LIPID 165
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 166
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 168
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 169
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 469 AA; 53206 MW; DD9B4F285E4DCDB3 CRC64;
MDETSPLVSP DRDQTEYSYQ SQCSPGATVP LSPNGRFSAL PGVVVRIPGT ATSCGSAASG
PSPPGSPCDQ ERQPLLERSQ TRAAAAQAER EMNKFPDDPA FAEVVKKAEK AIMRDILPER
ISQGSSGSYF VKDEQGEIIA VFKPKNEEPY GQLNPKWTKW LQKLCCPCCF GRDCLVLNQG
YLSEAGASLV DQKLDLNIVP RTKVVFLASE TFNYSAIDRV KSRGKRLALE KVPKVGQRFN
RIGLPPKVGS FQIFVKSYKD ADYWLRRFEA DPLPENTNRQ LQLQFERLVV LDYIIRNTDR
GNDNWLIKYD CPMDSASARD DWVMVKEPVI KIAAIDNGLA FPLKHPDSWR AYPFYWAWLP
QAKIQFSQEI KDLILPKISD PNFVKDLEED LYELFKKDQG FDRGQFRKQI AVMRGQILNL
TQAMKDGKSP LQLVQTPPVI VETARSHQKS TSESYTQSFQ SRKPFFSWW
