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1Q5VWL5_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
NameN/A
DescriptionPhospholipase c, epsilon 1.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005509 calcium ion binding (IEA)
0005085 guanyl-nucleotide exchange factor activity (IEA)
0004435 phosphoinositide phospholipase C activity (IEA)
0007242 intracellular signaling cascade (IEA)
0006629 lipid metabolism (IEA)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains assigned to SynO:
Phosphoinositide-specific phospholipase C (PLC) mediates the cellular actions of avariety of hormones.eurotransmitters and growth factors . Agonist-dependent activation of PLC causes hydrolysis of membrane phosphatidylinositol4.-bisphosphate (PIP2).enerating the second messengers inositol 1..-trisphosphate(IP3) and diacylglycerol (DAG). IP3 binds specific intracellular receptors to triggerCa2+ mobilisation.hile DAG mediates activation of a family of protein kinase C isozymes.Based on molecular size.mmunoreactivity and amino acid sequence.everalsubtypes have been classified. Overall.equence identity between sub-types is low.et all isoforms share two conserved domains.esignated X and Y.In PLC-beta subtypes. and Y domains are separated by a stretch of 70-120 amino acidsrich in Ser.hr and acidic residues. Their C terminus is rich in basic residues. In PLC-gammas.here is an insert of more than 400 residues containing an SH3 and two SH2 domains. PLCs show little similarity in the 300-residue N-terminal region preceding the X-domain.This entry represents a PLC region found towards the C-terminus which contains the X and Y boxes and the Ca2+-dependent membrane-targeting module of these proteins.
  IPR001192:Phosphoinositide-specific phospholipase C, C-terminal (PLC)
InterPro domains unassigned to SynO:
Phosphatidylinositol-specific phospholipase C (). eukaryotic intracellular enzyme.lays an important role in signal transduction processes . It catalyzes the hydrolysis of 1-phosphatidyl-D-myo-inositol-3..-triphosphate into the second messenger molecules diacylglycerol and inositol-1..-triphosphate. This catalytic process is tightly regulated by reversible phosphorylation and binding of regulatory proteins . In mammals.here are at least 6 different isoforms of PI-PLC.hey differ in their domain structure.heir regulation.nd their tissue distribution. Lower eukaryotes also possess multiple isoforms of PI-PLC. All eukaryotic PI-PLCs contain two regions of homology.ometimes referred to as the X-box and Y-box. The order of these two regions is always the same (NH2-X-Y-COOH).ut the spacing is variable. In most isoforms.he distancebetween these two regions is only 50-100 residues but in the gamma isoforms one PH domain.wo SH2 domains.nd 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. By profile analysis.e could show that sequences with significant similarity to the X-box domain occur also in prokaryotic and trypanosome PI-specific phospholipases C. Apart from this region.he prokaryotic enzymes show no similarity to their eukaryotic counterparts.
  IPR000909:Phosphatidylinositol-specific phospholipase C, X region
Phosphatidylinositol-specific phospholipase C ().n eukaryotic intracellular enzyme.lays an important role in signal transduction processes (see ). It catalyzes the hydrolysis of 1-phosphatidyl-D-myo-inositol-3..-triphosphate into the second messenger molecules diacylglycerol and inositol-1..-triphosphate. This catalytic process is tightly regulated by reversible phosphorylation and binding of regulatory proteins .In mammals.here are at least 6 different isoforms of PI-PLC.hey differ in their domain structure.heir regulation.nd their tissue distribution. Lower eukaryotes also possess multiple isoforms of PI-PLC.All eukaryotic PI-PLCs contain two regions of homology.ometimes referred to as X-box (see ) and Y-box. The order of these two regions is always the same (NH2-X-Y-COOH).ut the spacing is variable. In most isoforms.he distance between these two regions is only 50-100 residues but in the gamma isoforms one PH domain.wo SH2 domains.nd 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.here is a C2 domain (see ) possibly involved in Ca-dependent membrane attachment.
  IPR001711:Phosphatidylinositol-specific phospholipase C, Y domain
Proteins with this domain are mostly RasGTP effectors and include guanine-nucleotide releasing factor in mammals . This factor stimulates the dissociation of GDP from the Ras-related RALA and RALB GTPases which allows GTP binding and activation of the GTPases. It interacts and acts as an effector molecule for R-ras.-Ras and Rap .The domain is also present in a number of other proteins among them the sexual differentiation protein in yeast that is essential for mating and meiosis and yeast adenylate cyclase. These proteins contain repeated leucine-rich (LRR) segments.
  IPR000159:RA
The C2 domain is a Ca2+-dependent membrane-targeting module found in many cellular proteins involved in signal transduction or membrane trafficking. C2 domains are unique among membrane targeting domains in that they show wide range of lipid selectivity for the major components of cell membranes.ncluding phosphatidylserine and phosphatidylcholine. This C2 domain is about 116 amino-acid residues and is located between the two copies ofthe C1 domain in Protein Kinase C (that bind phorbol esters and diacylglycerol) (see )and the protein kinase catalytic domain (see ). Regions withsignificant homology to the C2-domain have been found in many proteins.The C2 domain is thought to be involved in calcium-dependent phospholipidbinding and in membrane targetting processes such as subcellular localisation. The 3D structure of theC2 domain of synaptotagmin has been reported.he domain forms an eight-stranded beta sandwich constructed around a conserved 4-stranded motif.esignated a C2 key . Calcium binds ina cup-shaped depression formed by the N- and C-terminal loops of theC2-key motif. Structural analyses of several C2 domains have shown them to consist of similar ternary structures in which three Ca2+-binding loops are located at the end of an 8 stranded antiparallel beta sandwich.
  IPR000008:C2 calcium-dependent membrane targeting
Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyze GTP to GDP . The balance between the GTP bound (active) and GDP bound (inactive) states is regulated by the opposite action of proteins activating the GTPase activity and that of proteins which promote the loss of bound GDP and the uptake of fresh GTP . The latter proteins are known as guanine-nucleotide dissociation stimulators (GDSs) (or also as guanine-nucleotide releasing (or exchange) factors (GRFs)). Proteins that act as GDS can be classified into at least two families.n the basis of sequence similarities.he CDC24 family (see ) and the CDC25 family.The size of the proteins of the CDC25 family range from 309 residues (LTE1) to 1596 residues (sos). The sequence similarity shared by all these proteins is limited to a region of about 250 amino acids generally located in their C-terminal section (currently the only exceptions are sos and ralGDS where this domain makes up the central part of the protein). This domain has been shown.n CDC25 an SCD25.o be essential for the activity of these proteins.
  IPR001895:Guanine-nucleotide dissociation stimulator CDC25
Small GTPases of the Ras family alternate between 2 conformations induced by the binding of either GTP or GDP. Guanine nucleotide exchange factors (GEFs) induce the dissociation of GDP to allow association of the more abundant GTP. The Ras-like family of small GTPases includes.mong others.as.ap1.-ras.nd Ral. The family is characterized by similarities in the effector domain. The Ras GTPase Rap1 is activated rapidly in response to activation of a variety of receptors. Rap1 activation is mediated by several second messengers.ncluding calcium.iacylglycerol.nd cAMP. GEFs have been identified that mediate these effects. One such GEF is Epac.n exchange protein directly activated by cAMP.hich represents a novel cAMP-induced.rotein kinase A-independent pathway .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008937:Ras guanine nucleotide exchange factor
The Ca2+-dependent.ipid-binding domain (CaLB) has been identified in a number of proteins.or example the amino-terminal.38 amino acid C2 domain of cytosolic phospholipase A2 (cPLA2-C2) which mediates an initial step in the production of lipid mediators of inflammation: the Ca2+-dependent translocation of the enzyme to intracellular membranes with subsequent liberation of arachidonic acid. The domain is composed of eight antiparallel beta-strands with six interconnecting loops that fits the "type II" topology for C2 domains. The structure has been identified as a beta-sandwich in the "Greek key" motif .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008973:C2 calcium/lipid-binding region, CaLB
This domain consists of a duplication of two EF-hand units.here each unit is composed of two helices connected by a twelve-residue calcium-binding loop. The calcium ion in the EF-hand loop is coordinated in a pentagonal bipyramidal configuration. Many calcium-binding proteins contain an EF-hand type calcium-binding domain . These include: calbindin D9K.100 proteins such as calcyclin.olcalcin phl p 7 (a calcium-binding pollen allergen).steonectin.arvalbumin.almodulin family of proteins (troponin C.altractin.dc4p.yosin essential chain.alcineurin.ecoverin.eurocalcin).lasmodial-specific CaII-binding protein Cbp40.enta-EF-Hand proteins (sorcin.rancalcin.alpain).s well as multidomain proteins such as phosphoinositide-specific phospholipase C.ystrophin.b1 and alpha-actinin. The fold consists of four helices and an open array of two hairpins.
  IPR011992:EF-Hand type
Phosphatidylinositol-specific phospholipase C ().n eukaryotic intracellular enzyme.lays an important role in signal transduction processes (see ). It catalyzes the hydrolysis of 1-phosphatidyl-D-myo-inositol-3..-triphosphate into the second messenger molecules diacylglycerol and inositol-1..-triphosphate. This catalytic process is tightly regulated by reversible phosphorylation and binding of regulatory proteins .In mammals.here are at least 6 different isoforms of PI-PLC.hey differ in their domain structure.heir regulation.nd their tissue distribution. Lower eukaryotes also possess multiple isoforms of PI-PLC.All eukaryotic PI-PLCs contain two regions of homology.ometimes referred to as X-box (see ) and Y-box. The order of these two regions is always the same (NH2-X-Y-COOH).ut the spacing is variable. In most isoforms.he distance between these two regions is only 50-100 residues but in the gamma isoforms one PH domain.wo SH2 domains.nd 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.here is a C2 domain (see ) possibly involved in Ca-dependent membrane attachment.This entry represents the X and Y box regions of phosphatidylinositol-specific phospholipase C.
  IPR013841:Phosphatidylinositol-specific phospholipase C, X and Y boxes
IPR000909:PLCXc 
Evalue:-81.7958800173441 
Location:1392-1540IPR001711:PLCYc 
Evalue:-45.2146701649892 
Location:1729-1846IPR000159:RA 
Evalue:-18.3872165679932 
Location:2135-2238IPR000008:C2 
Evalue:-15.2757244110107 
Location:1871-1945IPR001895:RasGEF 
Evalue:-7.10237290870956 
Location:528-831IPR011992:EF-Hand_type 
Evalue:0 
Location:1324-1387IPR001192:PHPHLIPASEC 
Evalue:0 
Location:1954-1964
SequencesProtein: Q5VWL5_HUMAN (2312 aa)
mRNA: AF190642
Local Annotation
Synapse Ontology
Any process that activates or increases the rate, frequency or extent of synaptic growth at neuromuscular junction.
sdb:0047 positive regulation of synaptic growth at neuromuscular junction  (Evidence:domains)
those channels, like InsP3-gated calcium channels which activated by InsP3 and release calcium into plasma.
sdb:0117 ionotropic receptor on the ER  (Evidence:domains)
protein kinase-catalyzed phosphorylation of specific ion channel subunits lead to cell surface expression of ion channel subunit
sdb:0201 cell surface expression of ion channel subunit  (Evidence:domains)
activation of calmodulin-dependent protein kinases
sdb:0204 activation of calmodulin-dependent protein kinase  (Evidence:domains)
calcium-regulated transcription factor
sdb:0215 calcium-regulated transcription factor  (Evidence:domains)
intracellular calcium store release to change the concentration of cytosolic calcium.
sdb:0321 intracellular calcium store release  (Evidence:domains)
KO assignmentK05860
  Level 3 annotation:
    phospholipase C, epsilon
  Level 2 annotation:
    Inositol phosphate metabolism
    Calcium signaling pathway
    Phosphatidylinositol signaling system
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 481 residues, 95780558-95781999Exon2: 97 residues, 95881920-95882206Exon3: 107 residues, 95920926-95921243Exon4: 50 residues, 95977052-95977198Exon5: 88 residues, 95983800-95984059Exon6: 70 residues, 95985661-95985867Exon7: 227 residues, 95995692-95996368Exon8: 63 residues, 96002062-96002245Exon9: 41 residues, 96003936-96004054Exon10: 54 residues, 96004639-96004796Exon11: 43 residues, 96008546-96008669Exon12: 47 residues, 96008760-96008897Exon13: 81 residues, 96012240-96012479Exon14: 22 residues, 96015393-96015455Exon15: 57 residues, 96015539-96015705Exon16: 38 residues, 96018675-96018783Exon17: 41 residues, 96020232-96020349Exon18: 55 residues, 96023308-96023467Exon19: 45 residues, 96029528-96029658Exon20: 42 residues, 96033536-96033658Exon21: 41 residues, 96034594-96034712Exon22: 46 residues, 96043254-96043386Exon23: 99 residues, 96048125-96048416Exon24: 56 residues, 96054228-96054392Exon25: 89 residues, 96056173-96056435Exon26: 41 residues, 96058327-96058446Exon27: 45 residues, 96063000-96063129Exon28: 72 residues, 96066293-96066503Exon29: 55 residues, 96071647-96071806Exon30: 75 residues, 96074095-96074314Exon31: 73 residues, 96074638-96074851Exon32: 142 residues, 96077714-96078136Exon33: 2 residues, -Jump to Q5VWL5_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2627 95780558-96078136 ~-298K 5364(+)Loci: 3909 95707938-95711287 ~-3K 5361(-)Link out to UCSC