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 |