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Protein

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

Gene

PLCG1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.

Cofactori

Enzyme regulationi

Activated by phosphorylation on tyrosine residues.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei335PROSITE-ProRule annotation1
Active sitei380PROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi165 – 176PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC:3.1.4.11)
Alternative name(s):
PLC-148
Phosphoinositide phospholipase C-gamma-1
Phospholipase C-II
Short name:
PLC-II
Phospholipase C-gamma-1
Short name:
PLC-gamma-1
Gene namesi
Name:PLCG1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5566.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000884972 – 12911-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1Add BLAST1290

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei506PhosphotyrosineBy similarity1
Modified residuei771Phosphotyrosine; by SYK2 Publications1
Modified residuei775PhosphotyrosineBy similarity1
Modified residuei783Phosphotyrosine3 Publications1
Modified residuei783Phosphotyrosine; by ITK, SYK and TXKBy similarity1
Modified residuei977PhosphotyrosineBy similarity1
Modified residuei1222PhosphoserineBy similarity1
Modified residuei1228PhosphoserineBy similarity1
Modified residuei1249PhosphoserineBy similarity1
Modified residuei1254Phosphotyrosine3 Publications1
Modified residuei1264PhosphoserineBy similarity1

Post-translational modificationi

May be dephosphorylated by PTPRJ (By similarity). Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. 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. Tyrosine phosphorylated in response to signaling via activated FLT1, FLT3, PDGFRA, PDGFRB and KIT. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells (By similarity).By similarity
Ubiquitinated by CBLB in activated T-cells.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP08487.
PRIDEiP08487.

PTM databases

iPTMnetiP08487.

Interactioni

Subunit structurei

Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts (via SH3 domain) with AGAP2. 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 (By similarity). Interacts with RALGPS1. Interacts (via SH2 domain) with PDGFRB (tyrosine phosphorylated) (By similarity). Interacts (via SH3 domain) with HEV ORF3 protein. Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts with FLT1 (tyrosine-phosphorylated). Interacts with AXL, FLT4 and KIT (By similarity). Interacts (via SH2 domain) with RET. Interacts (via SH2 domain) with PDGFRA (tyrosine phosphorylated). Interacts with PIP5K1C (By similarity). Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding) (By similarity). Interacts with SYK; activates PLCG1 (By similarity). Interacts with TESPA1 (By similarity). Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CBLP226813EBI-8013886,EBI-518228From a different organism.
LATO43561-24EBI-8013886,EBI-8070286From a different organism.
LCP2Q130945EBI-8013886,EBI-346946From a different organism.
PDGFRBP096193EBI-8013886,EBI-641237From a different organism.
SykP480254EBI-8013886,EBI-300116From a different organism.
VAV1P154984EBI-8013886,EBI-625518From a different organism.

Protein-protein interaction databases

DIPiDIP-42760N.
IntActiP08487. 8 interactors.
MINTiMINT-2837008.
STRINGi9913.ENSBTAP00000023383.

Chemistry databases

BindingDBiP08487.

Structurei

Secondary structure

11291
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi664 – 666Combined sources3
Beta strandi667 – 670Combined sources4
Beta strandi671 – 673Combined sources3
Helixi676 – 684Combined sources9
Beta strandi685 – 688Combined sources4
Beta strandi691 – 695Combined sources5
Beta strandi697 – 700Combined sources4
Beta strandi702 – 708Combined sources7
Beta strandi711 – 713Combined sources3
Beta strandi716 – 718Combined sources3
Beta strandi721 – 725Combined sources5
Beta strandi727 – 732Combined sources6
Helixi735 – 743Combined sources9
Beta strandi746 – 749Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FCINMR-A663-759[»]
2PLDNMR-A663-759[»]
2PLENMR-A663-759[»]
ProteinModelPortaliP08487.
SMRiP08487.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08487.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 142PH 1PROSITE-ProRule annotationAdd BLAST116
Domaini152 – 187EF-handPROSITE-ProRule annotationAdd BLAST36
Domaini320 – 464PI-PLC X-boxPROSITE-ProRule annotationAdd BLAST145
Domaini489 – 523PH 2; first partPROSITE-ProRule annotationAdd BLAST35
Domaini550 – 657SH2 1PROSITE-ProRule annotationAdd BLAST108
Domaini668 – 756SH2 2PROSITE-ProRule annotationAdd BLAST89
Domaini791 – 851SH3PROSITE-ProRule annotationAdd BLAST61
Domaini895 – 931PH 2; second partPROSITE-ProRule annotationAdd BLAST37
Domaini953 – 1070PI-PLC Y-boxPROSITE-ProRule annotationAdd BLAST118
Domaini1075 – 1177C2PROSITE-ProRule annotationAdd BLAST103

Domaini

The SH3 domain mediates interaction with CLNK and RALGPS1.By similarity

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 EF-hand domain.PROSITE-ProRule annotation
Contains 2 PH domains.PROSITE-ProRule annotation
Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation
Contains 2 SH2 domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiKOG1264. Eukaryota.
ENOG410XPXE. LUCA.
HOGENOMiHOG000230864.
HOVERGENiHBG053611.
InParanoidiP08487.
KOiK01116.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
2.30.29.30. 3 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028380. PLC-gamma1.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 2 hits.
PTHR10336:SF52. PTHR10336:SF52. 2 hits.
PfamiPF00168. C2. 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]
PIRSFiPIRSF000952. PLC-gamma. 1 hit.
PRINTSiPR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTiSM00239. 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]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50004. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08487-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGAASPCAN GCGPSAPSDA EVVHLCRSLE VGTVMTLFYS KKSQRPERKT
60 70 80 90 100
FQVKLETRQI TWSRGADKIE GAIDIREIKE IRPGKTSRDF DRYQEDPAFR
110 120 130 140 150
PDQSHCFVIL YGMEFRLKTL SLQATSEDEV NMWIRGLTWL MEDTLQAATP
160 170 180 190 200
LQIERWLRKQ FYSVDRNRED RISAKDLKNM LSQVNYRVPN MRFLRERLTD
210 220 230 240 250
LEQRTSDITY GQFAQLYRSL MYSAQKTMDL PFLEASALRA GERPELCRVS
260 270 280 290 300
LPEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDEFVT
310 320 330 340 350
FLFSKENSIW NSQLDEVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL
360 370 380 390 400
EAYARCLRMG CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH
410 420 430 440 450
AFVASEYPVI LSIEDHCSIA QQRNMAQYFK KVLGDTLLTK PVDIAADGLP
460 470 480 490 500
SPNQLKRKIL IKHKKLAEGS AYEEVPTSVM YSENDISNSI KNGILYLEDP
510 520 530 540 550
VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASG STELHSNEKW
560 570 580 590 600
FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW
610 620 630 640 650
RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE
660 670 680 690 700
MRLSEPVPQT NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN
710 720 730 740 750
SYAISFRAEG KIKHCRVQQE GQTVMLGNSE FDSLVDLISY YEKHPLYRKM
760 770 780 790 800
KLRYPINEEA LEKIGTAEPD YGALYEGRNP GFYVEANPMP TFKCAVKALF
810 820 830 840 850
DYKAQREDEL TFTKSAIIQN VEKQEGGWWR GDYGGKKQLW FPSNYVEEMV
860 870 880 890 900
SPAALEPERE HLDENSPLGD LLRGVLDVPA CQIAVRPEGK NNRLFVFSIS
910 920 930 940 950
MASVAHWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA
960 970 980 990 1000
LELSELVVYC RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF
1010 1020 1030 1040 1050
LQYNRLQLSR IYPKGQRLDS SNYDPLPMWI CGSQLVALNF QTPDKPMQMN
1060 1070 1080 1090 1100
QALFLAGGHC GYVLQPSVMR DEAFDPFDKS SLRGLEPCAI CIEVLGARHL
1110 1120 1130 1140 1150
PKNGRGIVCP FVEIEVAGAE YDSIKQKTEF VVDNGLNPVW PAKPFHFQIS
1160 1170 1180 1190 1200
NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEGL
1210 1220 1230 1240 1250
ELASLLVKID VFPAKQENGD LSPFGGASLR ERSCDASGPL FHGRAREGSF
1260 1270 1280 1290
EARYQQPFED FRISQEHLAD HFDGRDRRTP RRTRVNGDNR L
Length:1,291
Mass (Da):148,313
Last modified:August 1, 1988 - v1
Checksum:i9F31C7DAA3F8EA77
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00301 mRNA. Translation: CAA68406.1.
PIRiS00666.
RefSeqiNP_776850.1. NM_174425.3.
UniGeneiBt.307.

Genome annotation databases

GeneIDi281987.
KEGGibta:281987.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00301 mRNA. Translation: CAA68406.1.
PIRiS00666.
RefSeqiNP_776850.1. NM_174425.3.
UniGeneiBt.307.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FCINMR-A663-759[»]
2PLDNMR-A663-759[»]
2PLENMR-A663-759[»]
ProteinModelPortaliP08487.
SMRiP08487.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-42760N.
IntActiP08487. 8 interactors.
MINTiMINT-2837008.
STRINGi9913.ENSBTAP00000023383.

Chemistry databases

BindingDBiP08487.
ChEMBLiCHEMBL5566.

PTM databases

iPTMnetiP08487.

Proteomic databases

PaxDbiP08487.
PRIDEiP08487.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281987.
KEGGibta:281987.

Organism-specific databases

CTDi5335.

Phylogenomic databases

eggNOGiKOG1264. Eukaryota.
ENOG410XPXE. LUCA.
HOGENOMiHOG000230864.
HOVERGENiHBG053611.
InParanoidiP08487.
KOiK01116.

Miscellaneous databases

EvolutionaryTraceiP08487.
PROiP08487.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
2.30.29.30. 3 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028380. PLC-gamma1.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 2 hits.
PTHR10336:SF52. PTHR10336:SF52. 2 hits.
PfamiPF00168. C2. 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]
PIRSFiPIRSF000952. PLC-gamma. 1 hit.
PRINTSiPR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTiSM00239. 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]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50004. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiPLCG1_BOVIN
AccessioniPrimary (citable) accession number: P08487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: November 30, 2016
This is version 176 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.