Plcg1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
UniProt Data
| Accession | Q62077 [ UniProt ] |
| Name | PLCG1_MOUSE |
| Description | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 |
| Species | Mus musculus |
| Sequence Length | 1302 |
Enzyme Annotations (1)
- EC:3.1.4.11 Phosphoinositide phospholipase C.
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.
GO Annotations
Cellular component (11)
- GO:0001726 Ruffle
Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork. - GO:0001726 Ruffle
Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork. - GO:0005737 Cytoplasm
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. - GO:0005829 Cytosol
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. - GO:0005829 Cytosol
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. - GO:0005886 Plasma membrane
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. - GO:0005911 Cell-cell junction
A cell junction that forms a connection between two or more cells in a multicellular organism; excludes direct cytoplasmic junctions such as ring canals. - GO:0008180 COP9 signalosome
A protein complex that catalyzes the deneddylation of proteins, including the cullin component of SCF ubiquitin E3 ligase; deneddylation increases the activity of cullin family ubiquitin ligases. The signalosome is involved in many regulatory process, including some which control development, in many species; also regulates photomorphogenesis in plants; in many species its subunits are highly similar to those of the proteasome. - GO:0030027 Lamellipodium
A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments. - GO:0030027 Lamellipodium
A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments. - GO:0042995 Cell projection
A prolongation or process extending from a cell, e.g. a flagellum or axon.
Molecular function (6)
- GO:0004435 Phosphatidylinositol phospholipase C activity
Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H(2)O = 1,2-diacylglycerol + 1D-myo-inositol 1,4,5-trisphosphate + H(+). - GO:0005168 Neurotrophin TRKA receptor binding
Interacting selectively and non-covalently with the neurotrophin TRKA receptor. - GO:0005515 Protein binding
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). - GO:0019901 Protein kinase binding
Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. - GO:0030971 Receptor tyrosine kinase binding
Interacting selectively and non-covalently with a receptor that possesses protein tyrosine kinase activity. - GO:0035254 Glutamate receptor binding
Interacting selectively and non-covalently with a glutamate receptor.
Biological process (13)
- GO:0001701 In utero embryonic development
The process whose specific outcome is the progression of the embryo in the uterus over time, from formation of the zygote in the oviduct, to birth. An example of this process is found in Mus musculus. - GO:0002223 Stimulatory C-type lectin receptor signaling pathway
Any series of molecular signals generated as a consequence of binding to a C-type lectin receptor capable of cellular activation. - GO:0007173 Epidermal growth factor receptor signaling pathway
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor EGFR (ERBB1) on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription. - GO:0010634 Positive regulation of epithelial cell migration
Any process that activates or increases the frequency, rate or extent of epithelial cell migration. - GO:0010634 Positive regulation of epithelial cell migration
Any process that activates or increases the frequency, rate or extent of epithelial cell migration. - GO:0016477 Cell migration
The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms. - GO:0019722 Calcium-mediated signaling
Any intracellular signal transduction in which the signal is passed on within the cell via calcium ions. - GO:0043536 Positive regulation of blood vessel endothelial cell migration
Any process that activates or increases the frequency, rate or extent of the migration of the endothelial cells of blood vessels. - GO:0045766 Positive regulation of angiogenesis
Any process that activates or increases angiogenesis. - GO:0050852 T cell receptor signaling pathway
A series of molecular signals initiated by the cross-linking of an antigen receptor on a T cell. - GO:0051281 Positive regulation of release of sequestered calcium ion into cytosol
Any process that activates or increases the frequency, rate or extent of the release into the cytosolic compartment of calcium ions sequestered in the endoplasmic reticulum or mitochondria. - GO:0071364 Cellular response to epidermal growth factor stimulus
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an epidermal growth factor stimulus. - GO:0071364 Cellular response to epidermal growth factor stimulus
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an epidermal growth factor stimulus.
Protein Sequence
>Q62077 MAGVATPCANGCGPGAPSEAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGSIDIREIKE IRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIKGLTWLMEDTLQAATPLQIERWLRKQ FYSVDRNREDRISAKDLKNMLSQVNYRVPNMRFLRERLTDLEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLETNALRT GERPEHCQVSLSEFQQFLLEYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDELVTFLFSKENSVWNSQLDAVCPD TMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEH AFVASEYPVILSIEDHCSIAQQRNMAQHFRKVLGDTLLTKPVDIAADGLPSPNQLRRKILIKHKKLAEGSAYEEVPTSVM YSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEASSSTELHSSEKWFHGKLGAGRD GRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFWRNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQ QVPLRCNEFEMRLSEPVPQTNAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQE GQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNPGFYVEANPMPTFKCAVKALF DYKAQREDELTFTKSAIIQNVEKQDGGWWRGDYGGKKQLWFPSNYVEEMINPAVLEPEREHLDENSPLGDLLRGVLDVPA CQIAIRPEGKNNRLFVFSISMPSVAQWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKMMERRKKIALELSELVVYC RPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNF QTPDKPMQMNQALFMAGGHCGYVLQPSTMRDEAFDPFDKSSLRGLEPCVICIEVLGARHLPKNGRGIVCPFVEIEVAGAE YDSTKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDL ELASLLIKIDIFPAKENGDLSPFSGISLRERASDASSQLFHVRAREGSFEARYQQPFEDFRISQEHLADHFDSRERSTSD GPSSATNLIEDPLHDKLWKCSL
