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Primary Information | |
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| BoMiProt ID | Bomi3461 |
| Protein Name | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1/PLC-148 Phosphoinositide phospholipase C-gamma-1/Phospholipase C-II/PLC-II/Phospholipase C-gamma-1/PLC-gamma-1 |
| Organism | Bos taurus |
| Uniprot ID | P08487 |
| Milk Fraction | Whey,MFGM |
| Ref Sequence ID | NP_776850.1 |
| Aminoacid Length | 1291 |
| Molecular Weight | 148313 |
| FASTA Sequence | Download |
| Gene Name | PLCG1 |
| Gene ID | 281987 |
| Protein Existence Status | reviewed |
Secondary Information | |
| Protein Function | PLC-gamma1 activation enhances cell survival through the PKC-dependent phosphorylation of Bcl-2 during the cellular response to heat stress.C2 domain of PLC-γ1 also seems likely to interact with Ca2+ and membranes.Tyr783 in PLC-γ1 is presumed to be the primary site of phosphorylation coupled to enzyme activation. |
| Biochemical Properties | catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of receptor-mediated tyrosine kinase activators. |
| PTMs | Acetylation, Phosphorylation, Ubl conjugation |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|P08487|PLCG1_BOVIN 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 OS=Bos taurus OX=9913 GN=PLCG1 PE=1 SV=1 MAGAASPCANGCGPSAPSDAEVVHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQI TWSRGADKIEGAIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTL SLQATSEDEVNMWIRGLTWLMEDTLQAATPLQIERWLRKQFYSVDRNREDRISAKDLKNM LSQVNYRVPNMRFLRERLTDLEQRTSDITYGQFAQLYRSLMYSAQKTMDLPFLEASALRA GERPELCRVSLPEFQQFLLEYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDEFVT FLFSKENSIWNSQLDEVCPDTMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMG CRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIA QQRNMAQYFKKVLGDTLLTKPVDIAADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSVM YSENDISNSIKNGILYLEDPVNHEWY*506PHYFVLTSSKIYYSEETSSDQGNEDEEEPKEASG STELHSNEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFW RNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQT NAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQE GQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDY*771GALY*775EGRNPGFY*783VEANPMPTFKCAVKALFDYKAQREDELTFTKSAIIQNVEKQEGGWWRGDYGGKKQLW FPSNYVEEMVSPAALEPEREHLDENSPLGDLLRGVLDVPACQIAVRPEGKNNRLFVFSIS MASVAHWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKMMERRKKIALELSELVVYCRPVPFDEEKIGTERACY*977MSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDS SNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFLAGGHCGYVLQPSVMRDEAFDPFDKSSLRGLEPCAICIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSIKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEGLELASLLVKIDVFPAKQENGDLS*1222PFGGAS*1228LRERSCDASGPLFHGRAREGS*1249FEARY*1254QQPFEDFRIS*1264QEHLADHFDGRDRRTPRRTRVNGDNRL |
| SCOP | Class : Alpha and beta proteins (a+b) Fold : SH2-like Superfamily : SH2 domain Family : SH2 domain Domain Name : 2PLD A:6-102 |
| CATH | Matched CATH superfamily 3.30.505.10 |
| Predicted Disorder Regions | NA |
| DisProt Annotation | |
| TM Helix Prediction | no TM helices |
| Significance of PTMs | Activated by phosphorylation on tyrosine residues. PLC-γ1 and PLC-γ2 are phosphorylated on equivalent sites, Tyr783 and Tyr759, respectively, and this phosphorylation is typically required to stimulate phospholipase activity. Phosphorylation is mainly mediated by (RTKs) including Trk receptors and many growth factor receptors such as epidermal growth factor receptor (EGFR).The cSH2/SH3 domain loop contains Tyr783, which is required for phosphorylation-dependent activation of PLC-γ1. |
| PDB ID | 2FCI,2PLD,2PLE,5TNW,5TO4,5TQ1,5TQS, |
| Bibliography | 1.Bai XC, Liu AL, Deng F, Zou ZP, Bai J, Ji QS, Luo SQ. Phospholipase C-gamma1 is required for survival in heat stress: involvement of protein kinase C-dependent Bcl-2 phosphorylation. J Biochem. 2002 Feb;131(2):207-12. doi: 10.1093/oxfordjournals.jbchem.a003089. PMID: 11820933. 2.Hajicek N, Keith NC, Siraliev-Perez E, Temple BR, Huang W, Zhang Q, Harden TK, Sondek J. Structural basis for the activation of PLC-γ isozymes by phosphorylation and cancer-associated mutations. Elife. 2019 Dec 31;8:e51700. doi: 10.7554/eLife.51700. PMID: 31889510; PMCID: PMC7004563. |