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Protein

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

Gene

Plcg1

Organism
Rattus norvegicus (Rat)
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

  • calcium ion binding Source: InterPro
  • insulin receptor binding Source: RGD
  • phosphatidylinositol phospholipase C activity Source: Reactome
  • phosphoprotein binding Source: RGD
  • signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  • activation of phospholipase C activity Source: Reactome
  • calcium ion transport Source: RGD
  • cellular response to epidermal growth factor stimulus Source: UniProtKB
  • Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  • inositol trisphosphate biosynthetic process Source: RGD
  • intracellular signal transduction Source: InterPro
  • phospholipid catabolic process Source: InterPro
  • positive regulation of epithelial cell migration Source: RGD
  • protein secretion Source: RGD
  • regulation of store-operated calcium channel activity Source: RGD
  • response to gravity Source: RGD
  • response to hydrogen peroxide Source: RGD
  • response to morphine Source: RGD
  • response to organonitrogen compound Source: RGD
  • signal transduction Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.4.11. 5301.
ReactomeiR-RNO-1489509. DAG and IP3 signaling.
R-RNO-167021. PLC-gamma1 signalling.
R-RNO-2029485. Role of phospholipids in phagocytosis.
R-RNO-418890. Role of second messengers in netrin-1 signaling.
R-RNO-5218921. VEGFR2 mediated cell proliferation.

Chemistry databases

SwissLipidsiSLP:000000960.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC:3.1.4.11)
Alternative name(s):
Phosphoinositide phospholipase C-gamma-1
Phospholipase C-gamma-1
Short name:
PLC-gamma-1
Gene namesi
Name:Plcg1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3347. Plcg1.

Subcellular locationi

GO - Cellular componenti

  • COP9 signalosome Source: UniProtKB
  • cytoplasm Source: RGD
  • lamellipodium Source: UniProtKB
  • plasma membrane Source: Reactome
  • ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi842P → L: Inhibits interaction with AGAP2. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5188.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000885002 – 12901-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1Add BLAST1289

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei506PhosphotyrosineBy similarity1
Modified residuei771Phosphotyrosine; by SYKBy similarity1
Modified residuei775PhosphotyrosineBy similarity1
Modified residuei783Phosphotyrosine; by ITK, SYK and TXKBy similarity1
Modified residuei977PhosphotyrosineBy similarity1
Modified residuei1221PhosphoserineCombined sources1
Modified residuei1227PhosphoserineBy similarity1
Modified residuei1233PhosphoserineBy similarity1
Modified residuei1248PhosphoserineCombined sources1
Modified residuei1253PhosphotyrosineBy similarity1
Modified residuei1263PhosphoserineBy 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, KIT and PDGFRB. 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

PaxDbiP10686.
PRIDEiP10686.

PTM databases

iPTMnetiP10686.
PhosphoSitePlusiP10686.

Miscellaneous databases

PMAP-CutDBP10686.

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 the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain) with RET (By similarity). Interacts with FLT1 (tyrosine-phosphorylated). Interacts with AXL, FLT4 and KIT. Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated) (By similarity). 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
FGFR1P113624EBI-520788,EBI-1028277From a different organism.
Fgfr1Q045892EBI-520788,EBI-2480918
Jak2Q621203EBI-520788,EBI-646604From a different organism.
Khdrbs1Q607492EBI-520788,EBI-519077From a different organism.
Khdrbs2Q9WU012EBI-520788,EBI-8339046From a different organism.
PTPN1P180314EBI-520788,EBI-968788From a different organism.
TRPC3Q135072EBI-520788,EBI-520807From a different organism.

GO - Molecular functioni

  • insulin receptor binding Source: RGD
  • phosphoprotein binding Source: RGD

Protein-protein interaction databases

BioGridi247766. 1 interactor.
DIPiDIP-2863N.
IntActiP10686. 12 interactors.
MINTiMINT-231720.
STRINGi10116.ENSRNOP00000022276.

Chemistry databases

BindingDBiP10686.

Structurei

Secondary structure

11290
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi491 – 499Combined sources9
Turni500 – 503Combined sources4
Beta strandi504 – 513Combined sources10
Beta strandi516 – 519Combined sources4
Beta strandi551 – 553Combined sources3
Helixi556 – 558Combined sources3
Helixi561 – 576Combined sources16
Beta strandi583 – 587Combined sources5
Beta strandi589 – 591Combined sources3
Beta strandi594 – 600Combined sources7
Beta strandi605 – 613Combined sources9
Beta strandi616 – 618Combined sources3
Beta strandi620 – 624Combined sources5
Beta strandi627 – 631Combined sources5
Helixi632 – 641Combined sources10
Helixi665 – 668Combined sources4
Beta strandi669 – 672Combined sources4
Helixi675 – 682Combined sources8
Beta strandi690 – 695Combined sources6
Beta strandi701 – 708Combined sources8
Beta strandi711 – 720Combined sources10
Beta strandi723 – 726Combined sources4
Beta strandi729 – 733Combined sources5
Helixi734 – 743Combined sources10
Helixi758 – 762Combined sources5
Beta strandi796 – 800Combined sources5
Beta strandi817 – 822Combined sources6
Beta strandi825 – 833Combined sources9
Beta strandi836 – 842Combined sources7
Helixi843 – 845Combined sources3
Beta strandi846 – 848Combined sources3
Beta strandi860 – 862Combined sources3
Turni864 – 870Combined sources7
Beta strandi874 – 876Combined sources3
Beta strandi882 – 886Combined sources5
Beta strandi890 – 892Combined sources3
Beta strandi896 – 900Combined sources5
Beta strandi904 – 906Combined sources3
Beta strandi909 – 912Combined sources4
Helixi916 – 930Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y0MX-ray1.20A791-851[»]
1YWOX-ray1.81A790-851[»]
1YWPX-ray1.60A790-851[»]
2FJLNMR-A489-547[»]
A851-933[»]
3GQIX-ray2.50B545-770[»]
4K44X-ray1.70A/B664-766[»]
4K45X-ray1.50A664-766[»]
B770-787[»]
5EG3X-ray2.61B661-773[»]
ProteinModelPortaliP10686.
SMRiP10686.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10686.

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.
InParanoidiP10686.
KOiK01116.
PhylomeDBiP10686.

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.

P10686-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGVGTPCAN GCGPSAPSEA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT
60 70 80 90 100
FQVKLETRQI TWSRGADKIE GSIDIREIKE IRPGKTSRDF DRYQEDPAFR
110 120 130 140 150
PDQSHCFVIL YGMEFRLKTL SLQATSEDEV NMWIKGLTWL MEDTLQAATP
160 170 180 190 200
LQIERWLRKQ FYSVDRNRED RISAKDLKNM LSQVNYRVPN MRFLRERLTD
210 220 230 240 250
FEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLETNTLRT GERPELCQVS
260 270 280 290 300
LSEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDELVT
310 320 330 340 350
FLFSKENSVW NSQLDAVCPE TMNNPLSHYW ISSSHNTYLT GDQFSSESSL
360 370 380 390 400
EAYARCLRMG CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH
410 420 430 440 450
AFVASEYPVI LSIEDHCSIA QQRNMAQHFR KVLGDTLLTK PVDIAADGLP
460 470 480 490 500
SPNQLKRKIL IKHKKLAEGS AYEEVPTSVM YSENDISNSI KNGILYLEDP
510 520 530 540 550
VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASG STELHSSEKW
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 VEKQDGGWWR GDYGGKKQLW FPSNYVEEMI
860 870 880 890 900
NPAILEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS
910 920 930 940 950
MPSVAQWSLD 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
QALFMAGGHC GYVLQPSTMR DEAFDPFDKS SLRGLEPCVI CIEVLGARHL
1110 1120 1130 1140 1150
PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW PAKPFHFQIS
1160 1170 1180 1190 1200
NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL
1210 1220 1230 1240 1250
ELASLLIKID IFPAKENGDL SPFSGTSLRE RASDASSQLF HVRAREGSFE
1260 1270 1280 1290
ARYQQPFEDF RISQEHLADH FDSRERRAPR RTRVNGDNRL
Length:1,290
Mass (Da):148,548
Last modified:July 1, 1989 - v1
Checksum:iBB3240C27972CE3B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03806 mRNA. Translation: AAA41921.1.
L14476 Genomic DNA. No translation available.
PIRiA31317.
RefSeqiNP_037319.1. NM_013187.1.
UniGeneiRn.11243.

Genome annotation databases

GeneIDi25738.
KEGGirno:25738.
UCSCiRGD:3347. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03806 mRNA. Translation: AAA41921.1.
L14476 Genomic DNA. No translation available.
PIRiA31317.
RefSeqiNP_037319.1. NM_013187.1.
UniGeneiRn.11243.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y0MX-ray1.20A791-851[»]
1YWOX-ray1.81A790-851[»]
1YWPX-ray1.60A790-851[»]
2FJLNMR-A489-547[»]
A851-933[»]
3GQIX-ray2.50B545-770[»]
4K44X-ray1.70A/B664-766[»]
4K45X-ray1.50A664-766[»]
B770-787[»]
5EG3X-ray2.61B661-773[»]
ProteinModelPortaliP10686.
SMRiP10686.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247766. 1 interactor.
DIPiDIP-2863N.
IntActiP10686. 12 interactors.
MINTiMINT-231720.
STRINGi10116.ENSRNOP00000022276.

Chemistry databases

BindingDBiP10686.
ChEMBLiCHEMBL5188.
SwissLipidsiSLP:000000960.

PTM databases

iPTMnetiP10686.
PhosphoSitePlusiP10686.

Proteomic databases

PaxDbiP10686.
PRIDEiP10686.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25738.
KEGGirno:25738.
UCSCiRGD:3347. rat.

Organism-specific databases

CTDi5335.
RGDi3347. Plcg1.

Phylogenomic databases

eggNOGiKOG1264. Eukaryota.
ENOG410XPXE. LUCA.
HOGENOMiHOG000230864.
HOVERGENiHBG053611.
InParanoidiP10686.
KOiK01116.
PhylomeDBiP10686.

Enzyme and pathway databases

BRENDAi3.1.4.11. 5301.
ReactomeiR-RNO-1489509. DAG and IP3 signaling.
R-RNO-167021. PLC-gamma1 signalling.
R-RNO-2029485. Role of phospholipids in phagocytosis.
R-RNO-418890. Role of second messengers in netrin-1 signaling.
R-RNO-5218921. VEGFR2 mediated cell proliferation.

Miscellaneous databases

EvolutionaryTraceiP10686.
PMAP-CutDBP10686.
PROiP10686.

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_RAT
AccessioniPrimary (citable) accession number: P10686
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 30, 2016
This is version 187 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, 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.