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P24135 (PLCG2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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-IV
Short name=PLC-IV
Phospholipase C-gamma-2
Short name=PLC-gamma-2
Gene names
Name:Plcg2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 126512651-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
PRO_0000088502

Regions

Domain20 – 131112PH
Domain312 – 456145PI-PLC X-box
Domain532 – 635104SH2 1
Domain646 – 73590SH2 2
Domain769 – 82961SH3
Domain930 – 1044115PI-PLC Y-box
Domain1059 – 115294C2

Sites

Active site3271 By similarity
Active site3721 By similarity

Amino acid modifications

Modified residue7531Phosphotyrosine; by BTK By similarity
Modified residue7591Phosphotyrosine; by BTK By similarity
Modified residue11971Phosphotyrosine; by BTK Ref.2
Modified residue12171Phosphotyrosine By similarity
Modified residue12451Phosphotyrosine By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P24135 [UniParc].

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

FASTA1,265147,735
        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 

« Hide

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.
PIRA34163.
RefSeqNP_058864.1. NM_017168.1.
UniGeneRn.9751.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EOBNMR-A633-743[»]
ProteinModelPortalP24135.
SMRP24135. Positions 520-744, 772-829.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000018678.

Chemistry

ChEMBLCHEMBL5230.

PTM databases

PhosphoSiteP24135.

Proteomic databases

PaxDbP24135.
PRIDEP24135.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29337.
KEGGrno:29337.
UCSCRGD:3348. rat.

Organism-specific databases

CTD5336.
RGD3348. Plcg2.

Phylogenomic databases

eggNOGNOG268751.
HOGENOMHOG000230864.
HOVERGENHBG053611.
InParanoidP24135.
KOK05859.
PhylomeDBP24135.

Gene expression databases

GenevestigatorP24135.

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

EvolutionaryTraceP24135.
NextBio608820.
PROP24135.

Entry information

Entry namePLCG2_RAT
AccessionPrimary (citable) accession number: P24135
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: April 16, 2014
This is version 133 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