P4K2A_XENTR
ID P4K2A_XENTR Reviewed; 471 AA.
AC Q505I0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 94.
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 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].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2005) 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; BC094534; AAH94534.1; -; mRNA.
DR RefSeq; NP_001263612.1; NM_001276683.1.
DR AlphaFoldDB; Q505I0; -.
DR SMR; Q505I0; -.
DR PaxDb; Q505I0; -.
DR GeneID; 594904; -.
DR KEGG; xtr:594904; -.
DR CTD; 55361; -.
DR Xenbase; XB-GENE-491468; pi4k2a.
DR eggNOG; KOG2381; Eukaryota.
DR InParanoid; Q505I0; -.
DR OMA; LDKDRGH; -.
DR OrthoDB; 1273723at2759; -.
DR PhylomeDB; Q505I0; -.
DR TreeFam; TF314740; -.
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 7.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000013516; Expressed in testis and 13 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: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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic 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:0035651; F:AP-3 adaptor complex binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
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..471
FT /note="Phosphatidylinositol 4-kinase type 2-alpha"
FT /id="PRO_0000285163"
FT DOMAIN 117..445
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..129
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 150..152
FT /note="Important for substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 158..171
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 261..269
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 298..306
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 336..356
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 351..360
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT COMPBIAS 10..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 254..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT LIPID 167
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 168
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 170
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 171
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 471 AA; 53484 MW; 1209E79DDA3CB8E7 CRC64;
MDETSPLVSP DRDQTDYSYQ SQCSPGVPVC LSPNGRFSAV PGVVVRIPGS ATSPIRGSAA
SGPSPPGSPC DRERQPLLER SQTRGAAAQA ERERNKFPDD PEFAEVVKKA EKAIVRDILP
ERISQGSSGS YFVKNEQGEI IAVFKPKNEE PYGQLNPKWT KWLQKLCCPC CFGRDCLVLN
QGYLSEAGAS LVDQKLELNI VPRTKVVFLA SETFNYSAID RVKSRGKRLA LEKVPKVGQR
FNRIGLPPKV GSFQLFVKGY KDADYWLRRF EADPLPENTN RQLQLQFERL VVLDYIIRNT
DRGNDNWLIK YDCPMDSASA RDDWVMVKEP VIKIAAIDNG LAFPLKHPDS WRAYPFYWAW
LPQAKIQFSQ EIKDLILPKI SDPNFVKDLE EDLYELFKRD PGFDRGQFRK QIAVMRGQIL
NLTQALKDGK SPLQLVQTPP VIVETARSHQ KSTSESYTQS FQSRKPFFSW W
