Plcg1
entrez
25738
canonical
uniprot
P10686
canonical
ensembl
ENSRNOG00000051490
resolver
ensp
ENSRNOP00000069822
resolver
enst
ENSRNOT00000078909
resolver
genesymbol
Plcg1
resolver
uniprot
G3V845
resolver
uniprot_entry
G3V845_RAT
resolver
uniprot_entry
PLCG1_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Activated by phosphorylation on tyrosine residues. {ECO:0000250|UniProtKB:P19174}.
uniprot
proteins
amino_acid_sequence
MAGVGTPCANGCGPSAPSEAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGSIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIKGLTWLMEDTLQAATPLQIERWLRKQFYSVDRNREDRISAKDLKNMLSQVNYRVPNMRFLRERLTDFEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLETNTLRTGERPELCQVSLSEFQQFLLEYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDELVTFLFSKENSVWNSQLDAVCPETMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIAQQRNMAQHFRKVLGDTLLTKPVDIAADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSVMYSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEASGSTELHSSEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFWRNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQTNAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQEGQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNPGFYVEANPMPTFKCAVKALFDYKAQREDELTFTKSAIIQNVEKQDGGWWRGDYGGKKQLWFPSNYVEEMINPAILEPEREHLDENSPLGDLLRGVLDVPACQIAIRPEGKNNRLFVFSISMPSVAQWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKMMERRKKIALELSELVVYCRPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMAGGHCGYVLQPSTMRDEAFDPFDKSSLRGLEPCVICIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDLELASLLIKIDIFPAKENGDLSPFSGTSLRERASDASSQLFHVRAREGSFEARYQQPFEDFRISQEHLADHFDSRERRAPRRTRVNGDNRL
uniprot
proteins
ec_number
3.1.4.11
uniprot
proteins
function
FUNCTION: Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (PubMed:7531435). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, EGFR, FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:7531435). Plays a role in actin reorganization and cell migration (By similarity). Guanine nucleotide exchange factor that binds the GTPase DNM1 and catalyzes the dissociation of GDP, allowing a GTP molecule to bind in its place, therefore enhancing DNM1-dependent endocytosis (PubMed:15252117). {ECO:0000250|UniProtKB:P19174, ECO:0000250|UniProtKB:Q62077, ECO:0000269|PubMed:15252117, ECO:0000269|PubMed:7531435}.
uniprot
proteins
mass_dalton
148548
uniprot
proteins
mutagenesis
MUTAGEN 842; /note="P->L: Inhibits interaction with AGAP2."; /evidence="ECO:0000269|PubMed:11823862
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by CBLB in activated T-cells. {ECO:0000250|UniProtKB:Q62077}.; PTM: Tyrosine phosphorylated in response to signaling via activated FLT3, KIT and PDGFRA (By similarity). Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. Tyrosine phosphorylated by activated FLT1 and KDR. Tyrosine phosphorylated by activated PDGFRB. The receptor-mediated activation of PLCG1 involves its phosphorylation by tyrosine kinases, in response to ligation of a variety of growth factor receptors and immune system receptors. For instance, SYK phosphorylates and activates PLCG1 in response to ligation of the B-cell receptor. May be dephosphorylated by PTPRJ. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells (By similarity). {ECO:0000250|UniProtKB:P19174, ECO:0000250|UniProtKB:Q62077}.
uniprot
proteins
pubmed
11823862
uniprot
proteins
pubmed
15252117
uniprot
proteins
pubmed
16500902
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
2840660
uniprot
proteins
pubmed
7518429
uniprot
proteins
pubmed
7531435
uniprot
proteins
pubmed
8392838
uniprot
proteins
sequence_length
1290
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell projection, lamellipodium {ECO:0000250|UniProtKB:P19174}. Cell projection, ruffle {ECO:0000250|UniProtKB:P19174}. Note=Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment. {ECO:0000250|UniProtKB:P19174}.
uniprot
proteins