E9Q3L2 · PI4KA_MOUSE
- ProteinPhosphatidylinositol 4-kinase alpha
- GenePi4ka
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2105 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate.
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H+
Activity regulation
Activated by Triton X-100, insensitive to inhibition by adenosine and inhibited by wortmannin (By similarity).
The PI4K complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns4P) synthesis. Interaction with TMEM150A regulates PtdIns4P synthesis (By similarity).
The PI4K complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns4P) synthesis. Interaction with TMEM150A regulates PtdIns4P synthesis (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | Golgi-associated vesicle membrane | |
Cellular Component | plasma membrane | |
Molecular Function | 1-phosphatidylinositol 4-kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | kinase activity | |
Biological Process | modulation by host of viral process | |
Biological Process | phosphatidylinositol phosphate biosynthetic process | |
Biological Process | phosphatidylinositol-mediated signaling | |
Biological Process | phosphorylation | |
Biological Process | reorganization of cellular membranes to establish viral sites of replication |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylinositol 4-kinase alpha
- EC number
- Short namesPI4-kinase alpha; PI4K-alpha; PtdIns-4-kinase alpha
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionE9Q3L2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localization to the plasma membrane is mediated by the PI4K complex and association with EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and HYCC (HYCC1 or HYCC2). Localization to the plasma membrane is regulated by TMEM150A.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Early embryonic lethality. Conditional knockout mice show a dramatic depletion of cellular phosphatidylinositol 4-phosphate (PtdIns4P).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 103 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000435632 | 1-2105 | Phosphatidylinositol 4-kinase alpha | |||
Sequence: MAAAGARGGGGGGGGGGGGGSGSSSGSSTSRGFYFNTVLSLARSLAVQRPASLEKVQKLLCMCPVDFHGIFQLDERRRDAVIALGIFLIESDLQHKDCVVPYLLRLLRGLPKVYWVEESTARKGRGNLPVAESFSFCLVTLLSDVACRDPSLRDEILEAILQVLHVLLGMCQALEIQEKEYLCKYAIPCLIGISRSFGRYSNSEESLLSKLFPKVSPHSLRIPEELEGVRRRSFNDFRSILPSNLLTVCQEGTLKRKTSSVSSISQVSPERGIPPPSSPGGSAFHYFEASCLPDGTALEPEYYFSTISSSFSISPLFNGITYKEFCIPLEMLRELLNLVKKIVEEPVLKSLDAIVAGVMEANPSADLYYTTFSDPLYLTMFKMLRDTLYYMKDLPTSFVKEIHDFVLEQFNMSQGELQKILHDADRIHSEMSPLKLRCQANAACVDLMVWAVKDEQGAENLCIKLSEKLQSKTSSKVIIAHLPLLICCLQGLGRLCERFPVVVHSVTPSLRDFLVIPSPVLVKLYKYHSQYHTVAGSDIKISVTNEHSESTLNVLPGKKNQPSMYEQLRDIAIDNICRCLKAGLTVDPVIVEAFLASLSNRLYISQESDKDAHLIPDHTIRALGHIAVALRDTPKVMEPILQILQQKFCQPPSPLDVLIIDQLGCLVITGNQYIYQEVWNLFQQISVKASSVVYSATKDYKDHGYRHCSLAVINALANIAANIQEEHLVDELLMNLLELFVQLGLEGKRASERASEKGPALKASSSAGNLGVLIPVIAVLTRRLPPIKEAKPRLQKLFRDFWLYSVLMGFAVEGSGLWPEEWYEGVCEIATKSPLLTFPSKEPLRSVLQYNSAMKNDTVTPAELSELRSTIINLLDPPPEVSALINKLDFAMSTYLLSVYRLEYMRVLRSTDPDRFQVMFCYFEDKAIQKDKSGMMQCVIAVADKVFDAFLNMMAEKAKTKENEEELERHAQFLLVNFNHIHKRIRRVADKYLSGLVDKFPHLLWSGTVLKTMLDILQTLSLSLSADIHKDQPYYDIPDAPYRITVPDTYEARESIVKDFAARCGMILQEAMKWAPTVTKSHLQEYLNKHQNWVSGLSQHTGLAMATESILHFAGYNKQNTTLGATQLTERPACVKKDYSNFMASLNLRNRYAGEVHGMIRFSGATGQMSDLNKMMVQDLITALDHSHPQHYTQAMFKLTAMLISSKDCDPQLLHHLCWGPLRMFNEHGMETALACWEWLLAGKNGVEVPFMREMAGAWHMTVEQKFGLFSVETKEADPLAASEASQPRPCPPEVTPHYIWIDFLVQRFEIAKYCSSDQVEIFSSLLQRSMSLNIGGARGSMNRHVAAIGPRFKLLTLGLSLLHADVVPNATIRNVLREKIYSTAFDYFSCPPKFPTQGEKRLREDISIMIKFWTAMFSDKKYLTASQLVPPDNQDTRSNLDITVGSRQQATQGWINTYPLSSGMSTISKKSGMSKKTNRGSQLHKYYMKRRTLLLSLLATEIERLITWYNPLSAPELELDQAGENSVANWRSKYISLSEKQWKDNVNLAWSISPYLAVQLPARFKNTEAIGNEVTRLVRLDPGAVSDVPEAIKFLVTWHTIDADAPELSHVLCWAPTDPPTGLSYFSSMYPPHPLTAQYGVKVLRSFPPDAILFYIPQIVQALRYDKMGYVREYILWAAAKSQLLAHQFIWNMKTNIYLDEEGHQKDPDIGDLLEQLVEEITGSLSGPAKDFYQREFDFFNKITNVSAIIKPYPKGDERKKACLSALSEVKVQPGCYLPSNPEAIVLDIDYKSGTPMQSAAKAPYLAKFKVKRCGVSELEKEGLQCRSDAEDECFSQEADGKKICWQAAIFKVGDDCRQDMLALQIIDLFKNIFQLVGLDLFVFPYRVVATAPGCGVIECIPDCTSRDQLGRQTDFGMYDYFTRQYGDESTLAFQQARYNFIRSMAAYSLLLFLLQIKDRHNGNIMLDKKGHIIHIDFGFMFESSPGGNLGWEPDIKLTDEMVMIMGGKMEATPFKWFMEMCVRGYLAVRPYMDAVVSLVTLMLDTGLPCFRGQTIKLLKHRFSPNMTEREAANFIMKVIQNCFLSNRSRTYDMIQYYQNDIPY | ||||||
Modified residue | 233 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 259 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 260 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 262 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 263 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 265 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 268 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 432 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1439 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of a phosphatidylinositol 4-kinase (PI4K) complex, composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and HYCC (HYCC1 or HYCC2). Interacts with TMEM150A; regulating recruitment to the plasma membrane. Interacts with TTC7A.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-24 | Disordered | ||||
Sequence: MAAAGARGGGGGGGGGGGGGSGSS | ||||||
Domain | 1533-1721 | PIK helical | ||||
Sequence: SKYISLSEKQWKDNVNLAWSISPYLAVQLPARFKNTEAIGNEVTRLVRLDPGAVSDVPEAIKFLVTWHTIDADAPELSHVLCWAPTDPPTGLSYFSSMYPPHPLTAQYGVKVLRSFPPDAILFYIPQIVQALRYDKMGYVREYILWAAAKSQLLAHQFIWNMKTNIYLDEEGHQKDPDIGDLLEQLVEE | ||||||
Domain | 1811-2089 | PI3K/PI4K catalytic | ||||
Sequence: KVKRCGVSELEKEGLQCRSDAEDECFSQEADGKKICWQAAIFKVGDDCRQDMLALQIIDLFKNIFQLVGLDLFVFPYRVVATAPGCGVIECIPDCTSRDQLGRQTDFGMYDYFTRQYGDESTLAFQQARYNFIRSMAAYSLLLFLLQIKDRHNGNIMLDKKGHIIHIDFGFMFESSPGGNLGWEPDIKLTDEMVMIMGGKMEATPFKWFMEMCVRGYLAVRPYMDAVVSLVTLMLDTGLPCFRGQTIKLLKHRFSPNMTEREAANFIMKVIQNCFLSNR | ||||||
Region | 1817-1823 | G-loop | ||||
Sequence: VSELEKE | ||||||
Region | 1957-1965 | Catalytic loop | ||||
Sequence: QIKDRHNGN | ||||||
Region | 1976-2000 | Activation loop | ||||
Sequence: HIDFGFMFESSPGGNLGWEPDIKLT |
Sequence similarities
Belongs to the PI3/PI4-kinase family. Type III PI4K subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,105
- Mass (Da)237,042
- Last updated2016-02-17 v2
- Checksum25EB66874330ED51
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A140T8I9 | A0A140T8I9_MOUSE | Pi4ka | 2044 | ||
A0A338P7D3 | A0A338P7D3_MOUSE | Pi4ka | 319 | ||
A0A338P6S0 | A0A338P6S0_MOUSE | Pi4ka | 153 | ||
A0A338P6F9 | A0A338P6F9_MOUSE | Pi4ka | 74 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 861 | in Ref. 2; AAH75629 | ||||
Sequence: P → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC110573 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC049252 EMBL· GenBank· DDBJ | AAH49252.1 EMBL· GenBank· DDBJ | mRNA | ||
BC055479 EMBL· GenBank· DDBJ | AAH55479.1 EMBL· GenBank· DDBJ | mRNA | ||
BC075629 EMBL· GenBank· DDBJ | AAH75629.1 EMBL· GenBank· DDBJ | mRNA | ||
AK136942 EMBL· GenBank· DDBJ | BAE23184.1 EMBL· GenBank· DDBJ | mRNA |