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

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P24135 (PLCG2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 124. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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-IV
Short name=PLC-IV
Phospholipase C-gamma-2
Short name=PLC-gamma-2

Gene names

Name:

Plcg2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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.
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H₂O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.
Cofactor	Calcium.
Subunit structure	Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated) By similarity.
Post-translational modification	Phosphorylated on tyrosine residues by CSF1R By similarity. 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. Ref.2
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	intracellular signal transduction Inferred from electronic annotation. Source: InterPro phosphatidylinositol biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB phospholipid catabolic process Inferred from electronic annotation. Source: InterPro release of sequestered calcium ion into cytosol Inferred from sequence or structural similarity. Source: UniProtKB response to ATP Inferred from direct assay PubMed 8958450. Source: RGD response to magnesium ion Inferred from direct assay PubMed 8958450. Source: RGD
Cellular_component	plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	phosphatidylinositol phospholipase C activity Inferred from direct assay Ref.1. Source: RGD phospholipid binding Inferred from electronic annotation. Source: InterPro signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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_0000088502

Regions

Domain

20 – 131

112

Domain

312 – 456

145

PI-PLC X-box

Domain

532 – 635

104

SH2 1

Domain

646 – 735

SH2 2

Domain

769 – 829

SH3

Domain

930 – 1044

115

PI-PLC Y-box

Domain

1059 – 1152

Sites

Active site

327

By similarity

Active site

372

By similarity

Amino acid modifications

Modified residue

753

Phosphotyrosine; by BTK By similarity

Modified residue

759

Phosphotyrosine; by BTK By similarity

Modified residue

1197

Phosphotyrosine; by BTK Ref.2

Modified residue

1217

Phosphotyrosine By similarity

Modified residue

1245

Phosphotyrosine By similarity

Secondary structure

1265

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P24135 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 2C34910D43572723
Show »

FASTA

1,265

147,735

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

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

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

       190        200        210        220        230        240 
KFLKDKLVEI GAQKDELSFE QFHLFYKKLM FEQQKSILDE 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 
FKEVLGDLLL TKPTEASADQ LPSPSQLREK IIIKHKKLGP RGDVDVNVED KKDEHKTQGE 

       490        500        510        520        530        540 
LYMWDSIDQK WTRHYCAIAD AKLSFSDDIE QTVEEDPVQD TPPTELHFGE KWFHKKVESR 

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

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

       670        680        690        700        710        720 
MRIPRDGAFL IRKREGTDSY 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 
EDNPLGSLCR GILDLNTYNV VKAPQGKNQK AFVFILEPKK QGDPPVEFAT DRVEELFEWF 

       910        920        930        940        950        960 
QSIREITWKI 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 MPPESQRKIL MTLTVKVLGA RHLPKLGRSI 

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

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

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


SRFYS

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References

[1]	"A second type of rat phosphoinositide-specific phospholipase C containing a src-related sequence not essential for phosphoinositide-hydrolyzing activity." Emori Y., Homma Y., Sorimachi H., Kawasaki H., Nakanishi O., Suzuki K., Takenawa T. J. Biol. Chem. 264:21885-21890(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Muscle.
[2]	"Identification of the SH2 domain binding protein of Bruton's tyrosine kinase as BLNK--functional significance of Btk-SH2 domain in B-cell antigen receptor-coupled calcium signaling." Hashimoto S., Iwamatsu A., Ishiai M., Okawa K., Yamadori T., Matsushita M., Baba Y., Kishimoto T., Kurosaki T., Tsukada S. Blood 94:2357-2364(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-1197.
[3]	"Solution structure of the second SH2 domain from rat PLC gamma-2." RIKEN structural genomics initiative (RSGI) Submitted (APR-2008) to the PDB data bank Cited for: STRUCTURE BY NMR OF 633-744.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05155 mRNA. Translation: AAA41896.1.

IPI

IPI00211731.

PIR

A34163.

RefSeq

NP_058864.1. NM_017168.1.

UniGene

Rn.9751.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EOB	NMR	-	A	633-743	[»]

ProteinModelPortal

P24135.

SMR

P24135. Positions 520-744, 772-829.

ModBase

Search...

Protein-protein interaction databases

STRING

10116.ENSRNOP00000018678.

PTM databases

PhosphoSite

P24135.

Proteomic databases

PaxDb

P24135.

PRIDE

P24135.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

29337.

KEGG

rno:29337.

UCSC

RGD:3348. rat.

Organism-specific databases

CTD

5336.

RGD

3348. Plcg2.

Phylogenomic databases

eggNOG

NOG268751.

HOGENOM

HOG000230864.

HOVERGEN

HBG053611.

InParanoid

P24135.

K05859.

OrthoDB

EOG4VDPXP.

Gene expression databases

ArrayExpress

P24135.

Genevestigator

P24135.

GermOnline

ENSRNOG00000013676. Rattus norvegicus.

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

ChEMBL

CHEMBL5230.

EvolutionaryTrace

P24135.

NextBio

608820.

Entry information

Entry name

PLCG2_RAT

Accession

Primary (citable) accession number: P24135

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	April 3, 2013
This is version 124 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

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