1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2

Preferred order of sections

Names and origin

Protein names

Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
EC=3.1.4.11

Alternative name(s):
Phosphoinositide phospholipase C-gamma-2
Phospholipase C-gamma-2
Short name=PLC-gamma-2

Gene names

Name:

Plcg2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1265 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling By similarity.
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H₂O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.
Cofactor	Calcium By similarity.
Subunit structure	Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated). Ref.3
Post-translational modification	Phosphorylated on tyrosine residues by BTK and SYK; upon ligand-induced activation of a variety of growth factor receptors and immune system receptors. Phosphorylation leads to increased phospholipase activity By similarity. Phosphorylated on tyrosine residues by CSF1R. Ref.3
Sequence similarities	Contains 1 C2 domain. Contains 1 PH domain. 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
Domain	Repeat SH2 domain SH3 domain
Ligand	Calcium
Molecular function	Hydrolase Transducer
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell receptor signaling pathway Inferred from mutant phenotype PubMed 10925250. Source: UniProtKB T cell receptor signaling pathway Inferred from direct assay PubMed 15728238. Source: MGI activation of store-operated calcium channel activity Inferred from mutant phenotype PubMed 15611229. Source: MGI follicular B cell differentiation Inferred from mutant phenotype PubMed 12928432. Source: MGI inositol trisphosphate biosynthetic process Inferred from direct assay PubMed 9013981. Source: MGI intracellular signal transduction Inferred from electronic annotation. Source: InterPro negative regulation of programmed cell death Inferred from mutant phenotype PubMed 12928432. Source: MGI phosphatidylinositol biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB phospholipid catabolic process Inferred from electronic annotation. Source: InterPro regulation of gene expression Inferred from mutant phenotype PubMed 12928432. Source: MGI release of sequestered calcium ion into cytosol Inferred from mutant phenotype PubMed 10925250. Source: UniProtKB response to lipopolysaccharide Inferred from direct assay PubMed 9013981. Source: MGI
Cellular_component	cytosol Inferred from mutant phenotype PubMed 10925250. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	phosphatidylinositol phospholipase C activity Inferred from sequence or structural similarity. Source: UniProtKB 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
Epor	P14753	2	EBI-617954,EBI-617901
Fhl2	O70433	3	EBI-617954,EBI-299379
Flna	Q8BTM8	3	EBI-617954,EBI-641991
Fn1	P11276	6	EBI-617954,EBI-641955
Inpp5d	Q9ES52	3	EBI-617954,EBI-300210
Pdcd6ip	Q9WU78	7	EBI-617954,EBI-641897
Trim27	Q62158	4	EBI-617954,EBI-642025
Zbtb7b	Q64321	3	EBI-617954,EBI-642868

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1265

1265

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2

PRO_0000342364

Regions

Domain

1 – 131

131

PH

Domain

312 – 456

145

PI-PLC X-box

Domain

532 – 635

104

SH2 1

Domain

646 – 735

90

SH2 2

Domain

769 – 829

61

SH3

Domain

930 – 1044

115

PI-PLC Y-box

Domain

1048 – 1152

105

C2

Sites

Active site

327

1

By similarity

Active site

372

1

By similarity

Amino acid modifications

Modified residue

753

1

Phosphotyrosine; by BTK Probable

Modified residue

759

1

Phosphotyrosine; by BTK By similarity

Modified residue

1197

1

Phosphotyrosine; by BTK By similarity

Modified residue

1217

1

Phosphotyrosine Ref.4

Modified residue

1245

1

Phosphotyrosine Ref.4

Experimental info

Sequence conflict

787

1

E → G in BAE24959. Ref.1

Secondary structure

1

.

1265

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q8CIH5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E4A2A6AD6F05160E
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FASTA

1,265

147,592

        10         20         30         40         50         60 
MTTMVNVDTL PEYEKSQIKR ALELGTVMTV FNARKSTPER RTVQMIMETR QVAWSKTADK 

        70         80         90        100        110        120 
IEGFLDIMEI KEIRPGKNSK DFERAKAVRH KAECCFTILY GTQFVLSTLS LATDSKEDAV 

       130        140        150        160        170        180 
KWLSGLKILH QEAMSASTPT MIESWLRKQI YSVDQTRRNS ISLRELKTIL PLVNFKVSGI 

       190        200        210        220        230        240 
KFLKDKLVEI GAQKDELSFE QFHLFYKKLM FDQQKSILDE FKKDSSVFIL GNTDRPDASA 

       250        260        270        280        290        300 
VYLQDFQRFL LHEQQELWAQ DLNKVRERMT KFIDDTMRET AEPFLFVDEF LTYLFSRENS 

       310        320        330        340        350        360 
IWDEKYDAVD MQDMNNPLSH YWISSSHNTY LTGDQLRSES STEAYIRCLR AGCRCIELDC 

       370        380        390        400        410        420 
WDGPDGKPII YHGWTRTTKI KFDDVVQAIR DHAFVTSSFP VILSIEEHCS VEQQRHMAKV 

       430        440        450        460        470        480 
FKEVLGDMLL TKPTEASADQ LPSPSQLREK IIIKHKKLGP KGDVDVNVED KKDEHKPQGE 

       490        500        510        520        530        540 
LYMWDSIDQK WTRHYCAIAD AKLSFGDDIE QAVEEEPVQD TPPTELHFGE KWFHKKVESR 

       550        560        570        580        590        600 
TSAEKLLQEY CAETGAKDGT FLVRESETFP NDYTLSFWRS GRVQHCRIRS TMENGVMKYY 

       610        620        630        640        650        660 
LTDNLTFNSI YALIQHYREA HLRCAEFELR LTDPVPNPNP HESKPWYYDS LSRGEAEDML 

       670        680        690        700        710        720 
MRIPRDGAFL IRKREGTNSY AITFRARGKV KHCRINRDGR HFVLGTSAYF ESLVELVSYY 

       730        740        750        760        770        780 
EKHALYRKMR LRYPVTPELL ERYNMERDIN SLYDVSRMYV DPSEINPSMP QRTVKALYDY 

       790        800        810        820        830        840 
KAKRSDELTF CRGALIHNVS KEPGGWWKGD YGTRIQQYFP SNYVEDISAG DAEEMEKQII 

       850        860        870        880        890        900 
EDNPLGSLCK GILDLNTYNV VKAPQGKNQK AFVFILEPKK QGDPPVEFAT DRVEELFEWF 

       910        920        930        940        950        960 
QSIREITWKM DTKENNMKYW ERNQSIAIEL SDLVVYCKPT SKTKDHLENP DFREIRSFVE 

       970        980        990       1000       1010       1020 
TKADSIVRQK PVDLLRYNQK GLTRVYPKGQ RVDSSNYDPF RLWLCGSQMV ALNFQTPDKY 

      1030       1040       1050       1060       1070       1080 
MQMNHALFSL NGRTGYVLQP ESMRSEKYDP MPLESQRKIL MTLTVKVLGA RHLPKLGRSI 

      1090       1100       1110       1120       1130       1140 
ACPFVEVEIC GAEYDSNKFK TTVVNDNGLS PVWAPTQEKV TFEIYDPNLA FLRFVVYEED 

      1150       1160       1170       1180       1190       1200 
MFSDPNFLAH ATYPIKGIKS GFRSVPLKNG YSEDIELASL LVFCEMRPVL ESEEELYSSC 

      1210       1220       1230       1240       1250       1260 
RQLRRRQEEL NNQLFLYDTH QNLRGANRDA LVKEFNVNEN QLQLYQEKCN RRLREKRVSN 


SRFYS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow macrophage and Embryonic heart.
[2]	"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: Czech II and FVB/N. Tissue: Mammary tumor.
[3]	"Sequential activation of phoshatidylinositol 3-kinase and phospholipase C-gamma2 by the M-CSF receptor is necessary for differentiation signaling." Bourette R.P., Myles G.M., Choi J.L., Rohrschneider L.R. EMBO J. 16:5880-5893(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH CSF1R.
[4]	"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-753; TYR-1217 AND TYR-1245, MASS SPECTROMETRY. Tissue: Mast cell.
[5]	"Crystal structure of the N-terminal SH2 domain of mouse phospholipase c-gamma 2." RIKEN structural genomics initiative (RSGI) Submitted (SEP-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 516-640.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK142173 mRNA. Translation: BAE24959.1.
AK151039 mRNA. Translation: BAE30056.1.
BC019654 mRNA. Translation: AAH19654.1.
BC023877 mRNA. Translation: AAH23877.1.

IPI

IPI00229848.

RefSeq

NP_758489.1. NM_172285.1.

UniGene

Mm.192699.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DX0	X-ray	2.50	A/B	516-640	[»]
2EQI	NMR	-	A	772-828	[»]

ProteinModelPortal

Q8CIH5.

SMR

Q8CIH5. Positions 159-446, 476-511, 520-829, 844-909, 930-1181.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8CIH5. 28 interactions.

MINT

MINT-1348529.

STRING

10090.ENSMUSP00000079991.

PTM databases

PhosphoSite

Q8CIH5.

Proteomic databases

PaxDb

Q8CIH5.

PRIDE

Q8CIH5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000081232; ENSMUSP00000079991; ENSMUSG00000034330.

GeneID

234779.

KEGG

mmu:234779.

UCSC

uc009npc.1. mouse.

Organism-specific databases

CTD

5336.

MGI

MGI:97616. Plcg2.

Phylogenomic databases

eggNOG

NOG268751.

GeneTree

ENSGT00700000104020.

HOGENOM

HOG000230864.

HOVERGEN

HBG053611.

InParanoid

Q8CIH5.

KO

K05859.

OMA

MLMRIPR.

OrthoDB

EOG4VDPXP.

Gene expression databases

Bgee

Q8CIH5.

Genevestigator

Q8CIH5.

Family and domain databases

Gene3D

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.
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.
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.

SMART

SM00239. C2. 1 hit.
SM00233. PH. 2 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.
PS50003. PH_DOMAIN. 1 hit.
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

EvolutionaryTrace

Q8CIH5.

NextBio

382355.

SOURCE

Search...

Entry information

Entry name

PLCG2_MOUSE

Accession

Primary (citable) accession number: Q8CIH5
Secondary accession number(s): Q3UBA8, Q3UQT0, Q8VE69

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents