Q62077 (PLCG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
EC=3.1.4.11

Alternative name(s):
Phosphoinositide phospholipase C-gamma-1
Phospholipase C-gamma-1
Short name=PLC-gamma-1

Gene names

Name:	Plcg1
Synonyms:	Plcg-1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1302 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). 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, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration. Ref.11
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.
Cofactor	Calcium.
Enzyme regulation	Activated by phosphorylation on tyrosine residues.
Subunit structure	Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts with RALGPS1. Interacts (via SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain) with RET By similarity. Interacts with AGAP2 via its SH3 domain. Interacts with LAT (phosphorylated) upon TCR activation. Interacts (via SH3 domain) with the Pro-rich domain of TNK1. Associates with BLNK, VAV1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB in activated T-cells; which inhibits phosphorylation. Interacts with SHB. Interacts (via SH3 domain) with the Arg/Gly-rich-flanked Pro-rich domains of KHDRBS1/SAM68. This interaction is selectively regulated by arginine methylation of KHDRBS1/SAM68. Interacts with INPP5D/SHIP1, THEMIS and CLNK. Interacts with FLT4 and KIT. Interacts with AXL By similarity. Interacts with SYK; activates PLCG1 By similarity. Interacts with FLT1 (tyrosine-phosphorylated). Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated). Interacts with PIP5K1C. Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding). Interacts with TESPA1 By similarity. Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes; the association is weaker in the absence of TESPA1. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.19 Ref.20
Subcellular location	Cell projection › lamellipodium By similarity. Cell projection › ruffle By similarity. Note: Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment By similarity.
Domain	The SH3 domain mediates interaction with RALGPS1 By similarity. The SH3 domain also mediates interaction with CLNK. Ref.9
Post-translational modification	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. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells. May be dephosphorylated by PTPRJ By similarity. Ref.3 Ref.6 Ref.11 Ref.12 Ref.21 Ubiquitinated by CBLB in activated T-cells. Ref.11
Sequence similarities	Contains 1 C2 domain. Contains 1 EF-hand domain. Contains 2 PH domains. Contains 1 PI-PLC X-box domain. Contains 1 PI-PLC Y-box domain. Contains 2 SH2 domains. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Cell projection
Domain	Repeat SH2 domain SH3 domain
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Transducer
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell receptor signaling pathway Inferred from direct assay PubMed 15728238. Source: MGI cellular response to epidermal growth factor stimulus Inferred from sequence or structural similarity. Source: UniProtKB in utero embryonic development Inferred from mutant phenotype PubMed 11744703. Source: MGI intracellular signal transduction Inferred from electronic annotation. Source: InterPro phospholipid catabolic process Inferred from electronic annotation. Source: InterPro positive regulation of angiogenesis Inferred from electronic annotation. Source: Compara positive regulation of blood vessel endothelial cell migration Inferred from electronic annotation. Source: Compara positive regulation of epithelial cell migration Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome lamellipodium Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: Compara ruffle Inferred from sequence or structural similarity. Source: UniProtKB signalosome Inferred from electronic annotation. Source: Compara
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro phosphatidylinositol phospholipase C activity Inferred from electronic annotation. Source: EC phospholipid binding Inferred from electronic annotation. Source: InterPro signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Epor	P14753	4	EBI-300133,EBI-617901
Grb2	Q60631	2	EBI-300133,EBI-1688

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1302	1302	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1		PRO_0000088499
Regions
	Domain	27 – 142	116	PH 1
	Domain	152 – 187	36	EF-hand
	Domain	320 – 464	145	PI-PLC X-box
	Domain	489 – 523	35	PH 2; first part
	Domain	550 – 657	108	SH2 1
	Domain	668 – 756	89	SH2 2
	Domain	791 – 851	61	SH3
	Domain	895 – 931	37	PH 2; second part
	Domain	953 – 1070	118	PI-PLC Y-box
	Domain	1075 – 1177	103	C2
	Calcium binding	165 – 176	12	Potential
Sites
	Active site	335	1	By similarity
	Active site	380	1	By similarity
Amino acid modifications
	Modified residue	379	1	Phosphotyrosine Ref.17
	Modified residue	481	1	Phosphotyrosine Ref.17
	Modified residue	506	1	Phosphotyrosine Ref.17
	Modified residue	771	1	Phosphotyrosine; by SYK Ref.16
	Modified residue	775	1	Phosphotyrosine Ref.16
	Modified residue	783	1	Phosphotyrosine; by ITK, SYK and TXK By similarity
	Modified residue	977	1	Phosphotyrosine Ref.17
	Modified residue	1221	1	Phosphoserine By similarity
	Modified residue	1248	1	Phosphoserine Ref.18
	Modified residue	1253	1	Phosphotyrosine By similarity
	Modified residue	1263	1	Phosphoserine Ref.18
Experimental info
	Sequence conflict	966	1	D → A in CAA64639. Ref.2
	Sequence conflict	984	1	P → R in CAA64639. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q62077 [UniParc]. Last modified January 24, 2006. Version 2. Checksum: 5D123C508D425EB2	FASTA	1,302	149,668
	10 20 30 40 50 60 MAGVATPCAN GCGPGAPSEA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT FQVKLETRQI 70 80 90 100 110 120 TWSRGADKIE GSIDIREIKE IRPGKTSRDF DRYQEDPAFR PDQSHCFVIL YGMEFRLKTL 130 140 150 160 170 180 SLQATSEDEV NMWIKGLTWL MEDTLQAATP LQIERWLRKQ FYSVDRNRED RISAKDLKNM 190 200 210 220 230 240 LSQVNYRVPN MRFLRERLTD LEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLETNALRT 250 260 270 280 290 300 GERPEHCQVS LSEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDELVT 310 320 330 340 350 360 FLFSKENSVW NSQLDAVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL EAYARCLRMG 370 380 390 400 410 420 CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH AFVASEYPVI LSIEDHCSIA 430 440 450 460 470 480 QQRNMAQHFR KVLGDTLLTK PVDIAADGLP SPNQLRRKIL IKHKKLAEGS AYEEVPTSVM 490 500 510 520 530 540 YSENDISNSI KNGILYLEDP VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASS 550 560 570 580 590 600 STELHSSEKW FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW 610 620 630 640 650 660 RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE MRLSEPVPQT 670 680 690 700 710 720 NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN SYAISFRAEG KIKHCRVQQE 730 740 750 760 770 780 GQTVMLGNSE FDSLVDLISY YEKHPLYRKM KLRYPINEEA LEKIGTAEPD YGALYEGRNP 790 800 810 820 830 840 GFYVEANPMP TFKCAVKALF DYKAQREDEL TFTKSAIIQN VEKQDGGWWR GDYGGKKQLW 850 860 870 880 890 900 FPSNYVEEMI NPAVLEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS 910 920 930 940 950 960 MPSVAQWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA LELSELVVYC 970 980 990 1000 1010 1020 RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF LQYNRLQLSR IYPKGQRLDS 1030 1040 1050 1060 1070 1080 SNYDPLPMWI CGSQLVALNF QTPDKPMQMN QALFMAGGHC GYVLQPSTMR DEAFDPFDKS 1090 1100 1110 1120 1130 1140 SLRGLEPCVI CIEVLGARHL PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW 1150 1160 1170 1180 1190 1200 PAKPFHFQIS NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL 1210 1220 1230 1240 1250 1260 ELASLLIKID IFPAKENGDL SPFSGISLRE RASDASSQLF HVRAREGSFE ARYQQPFEDF 1270 1280 1290 1300 RISQEHLADH FDSRERSTSD GPSSATNLIE DPLHDKLWKC SL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[2]	"Phospholipase C in mouse oocytes: characterization of beta and gamma isoforms and their possible involvement in sperm-induced Ca2+ spiking." Dupont G., McGuinness O.M., Johnson M.H., Berridge M.J., Borgese F. Biochem. J. 316:583-591(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 846-1052. Tissue: Oocyte.
[3]	"Signal transduction by normal isoforms and W mutant variants of the Kit receptor tyrosine kinase." Reith A.D., Ellis C., Lyman S.D., Anderson D.M., Williams D.E., Bernstein A., Pawson T. EMBO J. 10:2451-2459(1991) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KIT, PHOSPHORYLATION.
[4]	"Tyrosine mutations within the alpha platelet-derived growth factor receptor kinase insert domain abrogate receptor-associated phosphatidylinositol-3 kinase activity without affecting mitogenic or chemotactic signal transduction." Yu J.C., Heidaran M.A., Pierce J.H., Gutkind J.S., Lombardi D., Ruggiero M., Aaronson S.A. Mol. Cell. Biol. 11:3780-3785(1991) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PDGFRA, ACTIVATION BY PDGFRA.
[5]	"Phosphorylation of tyrosine 720 in the platelet-derived growth factor alpha receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation." Bazenet C.E., Gelderloos J.A., Kazlauskas A. Mol. Cell. Biol. 16:6926-6936(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PDGFRA.
[6]	"The phosphorylated 1169-tyrosine containing region of flt-1 kinase (VEGFR-1) is a major binding site for PLCgamma." Sawano A., Takahashi T., Yamaguchi S., Shibuya M. Biochem. Biophys. Res. Commun. 238:487-491(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH FLT1.
[7]	"Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains." Bedford M.T., Frankel A., Yaffe M.B., Clarke S., Leder P., Richard S. J. Biol. Chem. 275:16030-16036(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KHDRBS1.
[8]	"Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b." Bachmaier K., Krawczyk C., Kozieradzki I., Kong Y.-Y., Sasaki T., Oliveira-dos-Santos A., Mariathasan S., Bouchard D., Wakeham A., Itie A., Le J., Ohashi P.S., Sarosi I., Nishina H., Lipkowitz S., Penninger J.M. Nature 403:211-216(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CBLB.
[9]	"MIST functions through distinct domains in immunoreceptor signaling in the presence and absence of LAT." Goitsuka R., Tatsuno A., Ishiai M., Kurosaki T., Kitamura D. J. Biol. Chem. 276:36043-36050(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CLNK, DOMAIN.
[10]	"Mechanism of TrkB-mediated hippocampal long-term potentiation." Minichiello L., Calella A.M., Medina D.L., Bonhoeffer T., Klein R., Korte M. Neuron 36:121-137(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NTRK2.
[11]	"Essential role of the E3 ubiquitin ligase Cbl-b in T cell anergy induction." Jeon M.-S., Atfield A., Venuprasad K., Krawczyk C., Sarao R., Elly C., Yang C., Arya S., Bachmaier K., Su L., Bouchard D., Jones R., Gronski M., Ohashi P., Wada T., Bloom D., Fathman C.G., Liu Y.-C., Penninger J.M. Immunity 21:167-177(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, UBIQUITINATION, FUNCTION.
[12]	"Tyrosine 769 of the keratinocyte growth factor receptor is required for receptor signaling but not endocytosis." Ceridono M., Belleudi F., Ceccarelli S., Torrisi M.R. Biochem. Biophys. Res. Commun. 327:523-532(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGFR2, PHOSPHORYLATION.
[13]	"Inositol 5'-phosphatase, SHIP1 interacts with phospholipase C-gamma1 and modulates EGF-induced PLC activity." Song M., Kim M.J., Ha S., Park J.B., Ryu S.H., Suh P.-G. Exp. Mol. Med. 37:161-168(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INPP5D.
[14]	"Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-derived growth factor receptor beta provides a dual mechanism of negative regulation." Reddi A.L., Ying G., Duan L., Chen G., Dimri M., Douillard P., Druker B.J., Naramura M., Band V., Band H. J. Biol. Chem. 282:29336-29347(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PDGFRB.
[15]	"Type I gamma phosphatidylinositol phosphate kinase is required for EGF-stimulated directional cell migration." Sun Y., Ling K., Wagoner M.P., Anderson R.A. J. Cell Biol. 178:297-308(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PIP5K1C.
[16]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771 AND TYR-775, MASS SPECTROMETRY. Tissue: Mast cell.
[17]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-379; TYR-481; TYR-506 AND TYR-977, MASS SPECTROMETRY. Tissue: Brain.
[18]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1248 AND SER-1263, MASS SPECTROMETRY. Tissue: Melanoma.
[19]	"Themis controls thymocyte selection through regulation of T cell antigen receptor-mediated signaling." Fu G., Vallee S., Rybakin V., McGuire M.V., Ampudia J., Brockmeyer C., Salek M., Fallen P.R., Hoerter J.A.H., Munshi A., Huang Y.H., Hu J., Fox H.S., Sauer K., Acuto O., Gascoigne N.R.J. Nat. Immunol. 10:848-856(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH THEMIS.
[20]	"Tespa1 is involved in late thymocyte development through the regulation of TCR-mediated signaling." Wang D., Zheng M., Lei L., Ji J., Yao Y., Qiu Y., Ma L., Lou J., Ouyang C., Zhang X., He Y., Chi J., Wang L., Kuang Y., Wang J., Cao X., Lu L. Nat. Immunol. 13:560-568(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB2; LAT AND THEMIS. Tissue: Thymocyte.
[21]	"Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling." Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K., Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D., Muller J.P. J. Biol. Chem. 286:10918-10929(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC065091 mRNA. Translation: AAH65091.1. X95346 mRNA. Translation: CAA64639.1.
IPI	IPI00121089.
RefSeq	NP_067255.2. NM_021280.3.
UniGene	Mm.44463.
3D structure databases
ProteinModelPortal	Q62077.
SMR	Q62077. Positions 73-483, 489-848, 851-933, 952-1207.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q62077. 11 interactions.
MINT	MINT-124146.
PTM databases
PhosphoSite	Q62077.
Proteomic databases
PaxDb	Q62077.
PRIDE	Q62077.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000103115; ENSMUSP00000099404; ENSMUSG00000016933.
GeneID	18803.
KEGG	mmu:18803.
Organism-specific databases
CTD	5335.
MGI	MGI:97615. Plcg1.
Phylogenomic databases
eggNOG	NOG268751.
GeneTree	ENSGT00700000104020.
HOGENOM	HOG000230864.
HOVERGEN	HBG053611.
InParanoid	Q62077.
KO	K01116.
OMA	YRSLMYS.
OrthoDB	EOG4320X7.
Enzyme and pathway databases
BRENDA	3.1.4.11. 3474.
Gene expression databases
ArrayExpress	Q62077.
Bgee	Q62077.
CleanEx	MM_PLCG1.
Genevestigator	Q62077.
Family and domain databases
Gene3D	1.10.238.10. 1 hit. 2.30.29.30. 3 hits. 3.20.20.190. 2 hits. 3.30.505.10. 2 hits.
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR011993. PH_like_dom. IPR001192. Pinositol_PLipase_C. IPR016279. PLC-gamma. IPR017946. PLC-like_Pdiesterase_TIM-brl. IPR001849. Pleckstrin_homology. IPR015359. PLipase_C_EF-hand-like. IPR000909. PLipase_C_PInositol-sp_X_dom. IPR001711. PLipase_C_Pinositol-sp_Y. IPR000980. SH2. IPR001452. SH3_domain. [Graphical view]
PANTHER	PTHR10336. PTHR10336. 1 hit.
Pfam	PF00168. C2. 1 hit. PF09279. efhand_like. 1 hit. PF00169. PH. 1 hit. PF00388. PI-PLC-X. 1 hit. PF00387. PI-PLC-Y. 1 hit. PF00017. SH2. 2 hits. PF00018. SH3_1. 1 hit. [Graphical view]
PIRSF	PIRSF000952. PLC-gamma. 1 hit.
PRINTS	PR00390. PHPHLIPASEC. PR00401. SH2DOMAIN. PR00452. SH3DOMAIN.
SMART	SM00239. C2. 1 hit. SM00233. PH. 3 hits. SM00148. PLCXc. 1 hit. SM00149. PLCYc. 1 hit. SM00252. SH2. 2 hits. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit. SSF50044. SH3. 1 hit.
PROSITE	PS50004. C2. 1 hit. PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 1 hit. PS50003. PH_DOMAIN. 2 hits. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. PS50001. SH2. 2 hits. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	295106.
SOURCE	Search...

Entry information

Entry name

PLCG1_MOUSE

Accession

Primary (citable) accession number: Q62077
Secondary accession number(s): Q6P1G1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
This is version 132 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program