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Q8CIH5 (PLCG2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1265 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processLipid degradation
Lipid metabolism
   DomainRepeat
SH2 domain
SH3 domain
   LigandCalcium
   Molecular functionHydrolase
Transducer
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from mutant phenotype PubMed 10925250. Source: UniProtKB

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_componentcytosol

Inferred from mutant phenotype PubMed 10925250. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionphosphatidylinositol phospholipase C activity

Inferred from sequence or structural similarity. Source: UniProtKB

phospholipase C activity

Traceable author statement PubMed 11744703. Source: MGI

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 126512651-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
PRO_0000342364

Regions

Domain1 – 131131PH
Domain312 – 456145PI-PLC X-box
Domain532 – 635104SH2 1
Domain646 – 73590SH2 2
Domain769 – 82961SH3
Domain930 – 1044115PI-PLC Y-box
Domain1048 – 1152105C2

Sites

Active site3271 By similarity
Active site3721 By similarity

Amino acid modifications

Modified residue7531Phosphotyrosine; alternate Ref.4
Modified residue7531Phosphotyrosine; by BTK; alternate Probable
Modified residue7591Phosphotyrosine; by BTK By similarity
Modified residue11971Phosphotyrosine; by BTK By similarity
Modified residue12171Phosphotyrosine Ref.4
Modified residue12451Phosphotyrosine Ref.4

Experimental info

Sequence conflict7871E → G in BAE24959. Ref.1

Secondary structure

..................................... 1265
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8CIH5 [UniParc].

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

FASTA1,265147,592
        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' 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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
RefSeqNP_758489.1. NM_172285.1.
UniGeneMm.192699.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DX0X-ray2.50A/B516-640[»]
2EQINMR-A772-828[»]
ProteinModelPortalQ8CIH5.
SMRQ8CIH5. Positions 159-446, 476-511, 520-909, 930-1181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8CIH5. 32 interactions.
MINTMINT-1348529.
STRING10090.ENSMUSP00000079991.

PTM databases

PhosphoSiteQ8CIH5.

Proteomic databases

PaxDbQ8CIH5.
PRIDEQ8CIH5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000081232; ENSMUSP00000079991; ENSMUSG00000034330.
GeneID234779.
KEGGmmu:234779.
UCSCuc009npc.1. mouse.

Organism-specific databases

CTD5336.
MGIMGI:97616. Plcg2.

Phylogenomic databases

eggNOGNOG268751.
GeneTreeENSGT00730000110782.
HOGENOMHOG000230864.
HOVERGENHBG053611.
InParanoidQ8CIH5.
KOK05859.
OMAFPNDYTL.
OrthoDBEOG7W419X.
PhylomeDBQ8CIH5.
TreeFamTF313216.

Gene expression databases

BgeeQ8CIH5.
GenevestigatorQ8CIH5.

Family and domain databases

Gene3D2.30.29.30. 3 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.
InterProIPR000008. C2_dom.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028381. PLC-gamma2.
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]
PANTHERPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF25. PTHR10336:SF25. 1 hit.
PfamPF00168. C2. 1 hit.
PF09279. EF-hand_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]
PIRSFPIRSF000952. PLC-gamma. 1 hit.
PRINTSPR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
SMARTSM00239. 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]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEPS50004. 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]
ProtoNetSearch...

Other

EvolutionaryTraceQ8CIH5.
NextBio382355.
PROQ8CIH5.
SOURCESearch...

Entry information

Entry namePLCG2_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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