Detail Information for IndEnz0005000063
IED ID IndEnz0005000063
Enzyme Type ID lipase000063
Protein Name Phosphatidylinositol 3-kinase catalytic subunit type 3
PI3-kinase type 3
PI3K type 3
EC 2.7.1.137
Phosphoinositide-3-kinase class 3
Gene Name vps-34 let-512 B0025.1
Organism Caenorhabditis elegans
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans
Enzyme Sequence MIPGMRATPTESFSFVYSCDLQTNVQVKVAEFEGIFRDVLNPVRRLNQLFAEITVYCNNQQIGYPVCTSFHTPPDSSQLARQKLIQKWNEWLTLPIRYSDLSRDAFLHITIWEHEDDEIVNNSTFSRRLVAQSKLSMFSKRGILKSGVIDVQMNVSTTPDPFVKQPETWKYSDAWGDEIDLLFKQVTRQSRGLVEDVPWLDPFASRRIEMIRAKYKYSSPDRHVFLVLEMAAIRLGPTFYKVVYYEDETKNMRVSTSVNGGVGIVSACTRYCVADPELLLESLAEVKHSAMTRRIRDVEDERHRQVKPNKQAKDRLETIVNLPSSQVLTREQRDLVWKFRHYLRQFPKALNKYLRSVNWVHPQEVKTALALMNDWELIEAEDALELLSSAFTHPAVRAYSVSRLLEAASPEQVLLYLPQLVQALKYEQGQQLPEEGNPVPVVSEEEGKIPSVATTPTEELEGRDMTVVTKKEARKAASGDLATFLIDYALASPKVSNYLYWHLKTEIESTKESKEEHSKMYQNIQDRLMEALVKRPDTRAQVDSLHQQQIFVEDLIILMNEAKARGGRLNESKSAEFRTMLSRAKHMLDLKGVHLPLDPSFRLSSVIPDTASFFKSEMMPAKISFKVLQPNGKADRNIPEEYTVIFKTGDDLRQDQLIQQMVRLIDIILKKGQLDLKLTPYLVLSTGVGQGFVQCIKSKPLRAIQEQYKAHKMDCIREAMKELRPGDGPFGIEPNVIDNYVRSLAGYSVIMYILGLGDRHLDNLLLCENGKLFHVDFGFILGRDPKPMPPPMKLTSEMVQVMGGVKSKQFLEFVQHVDSAYRILRRHSNVLLNLFSLMLDAGIPDIAAEPDKAIFKIEQRLRLDLSDEAATKHIFTQIESSLNAKMAMISDIIHAYKQNLM
Enzyme Length 901
Uniprot Accession Number Q9TXI7
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by wortmannin. {ECO:0000269|PubMed:11927551}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000255|PIRNR:PIRNR000587, ECO:0000269|PubMed:11927551};
DNA Binding
EC Number 2.7.1.137
Enzyme Function FUNCTION: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate (PubMed:11927551). Together with bec-1, mediates the production of phosphatidylinositol 3-phosphate on intracellular vesicles and thereby regulates membrane trafficking (PubMed:11927551, PubMed:16111945). Plays a role in endosome-to-Golgi retrograde transport of mig-14 (PubMed:21183797). Involved in clearance of apoptotic cell corpses by phagosomes (PubMed:22272187). Phagosome maturation requires two sequential and non-overlapping pulses of phosphatidylinositol-3-phosphate (PI3P) on the vesicle surface which mediates recruitment of sortins snx-1 and lst-4 and small GTPases rab-5, rab-2 and rab-7, downstream of dynamin dyn-1 (PubMed:22272187, PubMed:18425118). The first pulse is initiated by piki-1, then maintained by vps-34 which also produces the second pulse (PubMed:22272187). Required for embryonic development (PubMed:22272187). Together with bec-1, involved in L3/L4 larval molting stage probably by regulating cuticle shedding (PubMed:11927551). Regulates the expansion of the nucleus outer membrane (PubMed:11927551). Involved in the secretion and localization of lrp-1 at the apical surface of hyp7 syncytium (PubMed:16111945). May regulate endocytosis in hypodermal cells (PubMed:11927551). May play a role in the formation of gut granules (a lysosome-related organelle) (PubMed:15843430). Plays a role in germ stem cell proliferation during larval development (PubMed:28285998). {ECO:0000269|PubMed:11927551, ECO:0000269|PubMed:15843430, ECO:0000269|PubMed:16111945, ECO:0000269|PubMed:18425118, ECO:0000269|PubMed:21183797, ECO:0000269|PubMed:22272187, ECO:0000269|PubMed:28285998}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (2); Chain (1); Domain (3); Region (3); Sequence conflict (8)
Keywords ATP-binding;Alternative splicing;Cell projection;Cytoplasm;Endocytosis;Kinase;Lipid biosynthesis;Lipid metabolism;Membrane;Nucleotide-binding;Nucleus;Phagocytosis;Reference proteome;Transferase
Interact With Q22592
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000269|PubMed:11927551}; Peripheral membrane protein {ECO:0000269|PubMed:11927551}. Cytoplasm {ECO:0000269|PubMed:11927551}. Cytoplasmic granule {ECO:0000269|PubMed:11927551}. Cell projection, phagocytic cup {ECO:0000269|PubMed:18425118}. Note=Colocalizes with rab-5 and dyn-1 at the phagocytic cup. {ECO:0000269|PubMed:18425118}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10778742; 11560892; 14551910; 17164286; 18182484; 18282106; 19343510; 19360094; 19816564; 20305638; 20519582; 20921409; 21076391; 21085631; 21177967; 21367940; 21494661; 21906946; 22267497; 22286215; 22347378; 22446320; 22560298; 22634595; 22862955; 22901814; 23172915; 23800452; 24154628; 24165672; 24884423; 25487147; 26009280; 26109047; 26240185; 27400265; 27562069; 28455411; 29092895; 6593563; 9230900;
Motif
Gene Encoded By
Mass 103,059
Kinetics
Metal Binding
Rhea ID RHEA:12709
Cross Reference Brenda