{"metadata":{"accession":"IPR001711","entry_id":null,"type":"domain","go_terms":[{"identifier":"GO:0004435","name":"phosphatidylinositol phospholipase C activity","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0006629","name":"lipid metabolic process","category":{"code":"P","name":"biological_process"}},{"identifier":"GO:0007165","name":"signal transduction","category":{"code":"P","name":"biological_process"}},{"identifier":"GO:0035556","name":"intracellular signal transduction","category":{"code":"P","name":"biological_process"}}],"source_database":"interpro","member_databases":{"profile":{"PS50008":"Phosphatidylinositol-specific phospholipase Y-box domain profile"},"pfam":{"PF00387":"Phosphatidylinositol-specific phospholipase C, Y domain"},"smart":{"SM00149":"Phospholipase C, catalytic domain (part); domain Y"}},"integrated":null,"hierarchy":{"accession":"IPR001711","name":"Phospholipase C, phosphatidylinositol-specific, Y domain","type":"Domain","children":[]},"name":{"name":"Phospholipase C, phosphatidylinositol-specific, Y domain","short":"PLipase_C_Pinositol-sp_Y"},"description":[{"text":"

Phosphatidylinositol-specific phospholipase C ([ec:3.1.4.11]), an eukaryotic intracellular enzyme, plays an important role in signal transduction processes [[cite:PUB00000624]] (see [interpro:IPR001192]). It catalyzes the hydrolysis of 1-phosphatidyl-D-myo-inositol-3,4,5-triphosphate into the second messenger molecules diacylglycerol and inositol-1,4,5-triphosphate. This catalytic process is tightly regulated by reversible phosphorylation and binding of regulatory proteins [[cite:PUB00000014], [cite:PUB00002715], [cite:PUB00005394]].

\r\n

In mammals, there are at least 6 different isoforms of PI-PLC, they differ in their domain structure, their regulation, and their tissue distribution. Lower eukaryotes also possess multiple isoforms of PI-PLC.

\r\n

All eukaryotic PI-PLCs contain two regions of homology, sometimes referred to as 'X-box' (see [interpro:IPR000909]) and 'Y-box'. The order of these two regions is always the same (NH2-X-Y-COOH), but the spacing is variable. In most isoforms, the distance between these two regions is only 50-100 residues but in the gamma isoforms one PH domain, two SH2 domains, and one SH3 domain are inserted between the two PLC-specific domains. The two conserved regions have been shown to be important for the catalytic activity. At the C-terminal of the Y-box, there is a C2 domain (see [interpro:IPR000008]) possibly involved in Ca-dependent membrane attachment.

","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00000624":{"PMID":1849017,"ISBN":null,"volume":"1092","issue":"1","year":1991,"title":"The PtdIns-PLC superfamily and signal transduction.","URL":null,"raw_pages":"49-71","medline_journal":"Biochim Biophys Acta","ISO_journal":"Biochim. Biophys. Acta","authors":["Meldrum E","Parker PJ","Carozzi A."],"DOI_URL":"http://dx.doi.org/10.1016/0167-4889(91)90177-Y"},"PUB00000014":{"PMID":1419362,"ISBN":null,"volume":"26","issue":null,"year":1992,"title":"Multiple forms of phospholipase C isozymes and their activation mechanisms.","URL":null,"raw_pages":"35-61","medline_journal":"Adv Second Messenger Phosphoprotein Res","ISO_journal":"Adv. Second Messenger Phosphoprotein Res.","authors":["Rhee SG","Choi KD."],"DOI_URL":null},"PUB00002715":{"PMID":1319994,"ISBN":null,"volume":"267","issue":"18","year":1992,"title":"Regulation of inositol phospholipid-specific phospholipase C isozymes.","URL":null,"raw_pages":"12393-6","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Rhee SG","Choi KD."],"DOI_URL":"http://intl.jbc.org/cgi/content/abstract/267/18/12393"},"PUB00005394":{"PMID":1335185,"ISBN":null,"volume":"17","issue":"12","year":1992,"title":"Regulation of phospholipase C by G proteins.","URL":null,"raw_pages":"502-6","medline_journal":"Trends Biochem Sci","ISO_journal":"Trends Biochem. Sci.","authors":["Sternweis PC","Smrcka AV."],"DOI_URL":"http://dx.doi.org/10.1016/0968-0004(92)90340-F"}},"set_info":null,"overlaps_with":[{"accession":"IPR017946","name":"PLC-like phosphodiesterase, TIM beta/alpha-barrel domain superfamily","type":"homologous_superfamily"}],"counters":{"subfamilies":0,"domain_architectures":694,"interactions":0,"matches":38510,"pathways":381,"proteins":38404,"proteomes":3047,"sets":0,"structural_models":{"alphafold":20284},"structures":30,"taxa":11850},"entry_annotations":{"alignment:seed":275,"alignment:full":22617},"cross_references":{"prositedoc":{"displayName":"PROSITE Doc","description":"PROSITE is a database of protein families and domains.","rank":18,"accessions":[{"accession":"PDOC50007","url":"http://prosite.expasy.org/PDOC50007"}]},"gp":{"displayName":"Genome Properties","description":"Genome properties is an annotation system whereby functional attributes can be assigned to a genome, based on the presence of a defined set of protein signatures within that genome.","rank":45,"accessions":[{"accession":"GenProp1511","url":"https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1511"},{"accession":"GenProp1548","url":"https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1548"}]},"ec":{"displayName":"ENZYME","description":"ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.","rank":19,"accessions":[{"accession":"2.3.1.-","url":"https://enzyme.expasy.org/EC/2.3.1.-"},{"accession":"2.4.99.28","url":"https://enzyme.expasy.org/EC/2.4.99.28"},{"accession":"3.1.4.11","url":"https://enzyme.expasy.org/EC/3.1.4.11"}]}},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}