P51432

SS
Gene name
Plcb3
Protein name
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
Names
EC 3.1.4.11 , Phosphoinositide phospholipase C-beta-3 , Phospholipase C-beta-3 , PLC-beta-3
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:18797
EC number
3.1.4.11: Phosphoric diester hydrolases
Protein Class

Descriptions

PLCB1 catalyzes the hydrolysis of 1-phosphatidylinositol 4,5-bisphosphate into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3), and mediates intracellular signaling downstream of G protein-coupled receptors. Autoinhibitory region is a portion of the linker that separates the conserved X and Y boxes comprising the catalytic TIM barrel, at residues 468-539, and occludes the active site of PLCB1. The active site of a PLC isozyme toward phospholipid membranes should force the negatively charged X/Y linker away from the active site, therein relieving autoinhibition of the enzyme.

Autoinhibitory domains (AIDs)

569-584 (the ordered region of X/Y linker) SS

Target domain

317-707 (TIM barrel)

Relief mechanism

Partner binding

Assay

793-806 (Hα2’ helix) SS

Target domain

712-720 (Cleft between the TIM barrel and C2 domains of the catalytic core)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P51432

Entry ID Method Resolution Chain Position Source
AF-P51432-F1 Predicted AlphaFoldDB

49 variants for P51432

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389517451 71 D>G No EVA
rs3389534510 90 L>M No EVA
rs3408826916 92 F>C No EVA
rs3389524104 154 R>L No EVA
rs3389502600 155 K>N No EVA
rs3389488066 155 K>R No EVA
rs3553936743 264 Y>S No EVA
rs212348407 281 T>K No EVA
rs3389479370 302 G>R No EVA
rs3408937578 372 E>D No EVA
rs3409015507 373 E>G No EVA
rs3408231805 381 F>L No EVA
rs3409105659 381 F>V No EVA
rs3408981590 381 F>Y No EVA
rs3389524070 446 P>S No EVA
rs263643797 479 D>E No EVA
rs3389429644 485 R>W No EVA
rs31309183 545 R>W No EVA
rs3389502680 556 R>G No EVA
rs3389532799 564 E>* No EVA
rs3389517530 582 S>N No EVA
rs3389532722 585 V>I No EVA
rs3389429645 654 R>G No EVA
rs3389532800 711 K>T No EVA
rs3389514912 723 G>S No EVA
rs3389532746 820 G>E No EVA
rs3389524042 845 A>S No EVA
rs3389517456 864 I>V No EVA
rs3389469326 879 A>S No EVA
rs3409303849 919 R>S No EVA
rs3408981644 922 P>R No EVA
rs260944852 928 S>P No EVA
rs3389469277 952 P>L No EVA
rs3389517505 1002 A>T No EVA
rs255849946 1025 E>Q No EVA
rs259080940 1037 R>Q No EVA
rs3389522103 1068 L>F No EVA
rs242309918 1069 K>R No EVA
rs3389522531 1075 T>I No EVA
rs219179876 1078 T>A No EVA
rs3389515809 1096 K>T No EVA
rs3389526743 1103 N>I No EVA
rs3389522511 1119 V>A No EVA
rs3389522498 1123 E>D No EVA
rs1133664427 1142 A>T No EVA
rs3389532792 1146 R>L No EVA
rs264741245 1175 E>D No EVA
rs3389534577 1215 G>V No EVA
rs3389524125 1230 E>K No EVA

No associated diseases with P51432

6 regional properties for P51432

Type Name Position InterPro Accession
domain C2 domain 708 - 836 IPR000008
domain Phosphatidylinositol-specific phospholipase C, X domain 317 - 469 IPR000909
domain Phospholipase C, phosphatidylinositol-specific, Y domain 591 - 707 IPR001711
domain Phospholipase C-beta, C-terminal domain 945 - 1200 IPR014815
domain PLC-beta, PH domain 18 - 149 IPR037862
domain Phosphoinositide phospholipase C beta 1-4-like, EF-hand domain 153 - 221 IPR053945

Functions

Description
EC Number 3.1.4.11 Phosphoric diester hydrolases
Subcellular Localization
  • Cytoplasm
  • Membrane
  • Nucleus
  • And particulate fractions
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
postsynaptic cytosol The region of the cytosol consisting of all cytosol that is part of the postsynapse.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
sarcolemma The outer membrane of a muscle cell, consisting of the plasma membrane, a covering basement membrane (about 100 nm thick and sometimes common to more than one fiber), and the associated loose network of collagen fibers.

4 GO annotations of molecular function

Name Definition
calcium ion binding Binding to a calcium ion (Ca2+).
calmodulin binding Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
molecular adaptor activity The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.
phosphatidylinositol phospholipase C activity Catalysis of the reaction

8 GO annotations of biological process

Name Definition
G protein-coupled receptor signaling pathway The series of molecular signals initiated by a ligand binding to its receptor, in which the activated receptor promotes the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, and ends with regulation of a downstream cellular process. The pathway can start from the plasma membrane, Golgi or nuclear membrane.
inositol trisphosphate metabolic process The chemical reactions and pathways involving myo-inositol phosphate, 1,2,3,4,5,6-cyclohexanehexol, with three phosphate groups attached.
phosphatidylinositol catabolic process The chemical reactions and pathways resulting in the breakdown of phosphatidylinositol, any glycophospholipid with its sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
phosphatidylinositol metabolic process The chemical reactions and pathways involving phosphatidylinositol, any glycophospholipid in which a sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
phosphatidylinositol-mediated signaling The series of molecular signals in which a cell uses a phosphatidylinositol-mediated signaling to convert a signal into a response. Phosphatidylinositols include phosphatidylinositol (PtdIns) and its phosphorylated derivatives.
post-Golgi vesicle-mediated transport The directed movement of substances from the Golgi to other parts of the cell, including organelles and the plasma membrane, mediated by small transport vesicles.
regulation of systemic arterial blood pressure The process that modulates the force with which blood travels through the systemic arterial circulatory system. The process is controlled by a balance of processes that increase pressure and decrease pressure.
release of sequestered calcium ion into cytosol The process in which calcium ions sequestered in the endoplasmic reticulum, Golgi apparatus or mitochondria are released into the cytosolic compartment.

23 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P32383 PLC1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P10894 PLCB1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 Bos taurus (Bovine) SS
Q00722 PLCB2 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 Homo sapiens (Human) EV
Q9NQ66 PLCB1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 Homo sapiens (Human) EV
Q15147 PLCB4 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4 Homo sapiens (Human) PR
Q01970 PLCB3 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 Homo sapiens (Human) EV
Q8R3B1 Plcd1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 Mus musculus (Mouse) SS
Q8K394 Plcl2 Inactive phospholipase C-like protein 2 Mus musculus (Mouse) PR
Q8K2J0 Plcd3 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 Mus musculus (Mouse) PR
Q62077 Plcg1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 Mus musculus (Mouse) SS
Q8K4S1 Plce1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1 Mus musculus (Mouse) SS
A3KGF7 Plcb2 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 Mus musculus (Mouse) PR
Q9Z1B3 Plcb1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 Mus musculus (Mouse) SS
P10687 Plcb1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 Rattus norvegicus (Rat) SS
Q99JE6 Plcb3 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 Rattus norvegicus (Rat) SS
G5EBH0 egl-8 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta egl-8 Caenorhabditis elegans SS
Q8GV43 PLC6 Phosphoinositide phospholipase C 6 Arabidopsis thaliana (Mouse-ear cress) PR
Q6NMA7 PLC9 Phosphoinositide phospholipase C 9 Arabidopsis thaliana (Mouse-ear cress) PR
Q9STZ3 PLC8 Phosphoinositide phospholipase C 8 Arabidopsis thaliana (Mouse-ear cress) PR
Q56W08 PLC3 Phosphoinositide phospholipase C 3 Arabidopsis thaliana (Mouse-ear cress) PR
Q39032 PLC1 Phosphoinositide phospholipase C 1 Arabidopsis thaliana (Mouse-ear cress) PR
Q944C2 PLC5 Phosphoinositide phospholipase C 5 Arabidopsis thaliana (Mouse-ear cress) PR
Q944C1 PLC4 Phosphoinositide phospholipase C 4 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAGARPGVHA LQLEPPTVVE TLRRGSKFIK WDEEASSRNL VTLRVDPNGF FLYWTGPNME
70 80 90 100 110 120
VDTLDISSIR DTRTGRYARL PKDPKIREVL GFGGPDTRLE EKLMTVVAGP DPVNTTFLNF
130 140 150 160 170 180
MAVQDDTVKV WSEELFKLAM NILAQNASRN TFLRKAYTKL KLQVNQDGRI PVKNILKMFS
190 200 210 220 230 240
ADKKRVETAL ESCGLNFNRS ESIRPDEFPL EIFERFLNKL CLRPDIDKIL LEIGAKGKPY
250 260 270 280 290 300
LTLEQLMDFI NQKQRDPRLN EVLYPPLRSS QARLLIEKYE TNKQFLERDQ MSMEGFSRYL
310 320 330 340 350 360
GGEENGILPL EALDLSMDMT QPLSAYFINS SHNTYLTAGQ LAGPSSVEMY RQALLWGCRC
370 380 390 400 410 420
VELDVWKGRP PEEEPFITHG FTMTTEVPLR DVLEAIAEAA FKTSPYPVIL SFENHVDSAK
430 440 450 460 470 480
QQAKMAEYCR SIFGDALLID PLDKYPLSAG IPLPSPQDLM GRILVKNKKR HRPSTGVPDS
490 500 510 520 530 540
SVRKRPLEQS NSALSESSAA TEPSSPQLGS PSSDSCPGLS NGEEVGLEKT SLEPQKSLGE
550 560 570 580 590 600
ESLSREPNVP MPDRDREDEE EDEEEEETTD PKKPTTDEGT ASSEVNATEE MSTLVNYVEP
610 620 630 640 650 660
VKFKSFEAAR KRNKCFEMSS FVETKAMEQL TKSPMEFVEY NKQQLSRIYP KGTRVDSSNY
670 680 690 700 710 720
MPQLFWNVGC QLVALNFQTL DLPMQLNAGV FEYNGRSGYL LKPEFMRRPD KSFDPFTEVI
730 740 750 760 770 780
VDGIVANALR VKVISGQFLS DKKVGIYVEV DMFGLPVDTR RKYRTRTSQG NSFNPVWDEE
790 800 810 820 830 840
PFDFPKVVLP TLASLRIAAF EEGGKFVGHR ILPVSAIRSG YHYVCLRNEA NQPLCLPALL
850 860 870 880 890 900
IYTEASDYIP DDHQDYAEAL INPIKHVSLM DQRAKQLAAL IGESEAQAST ETYQETPCQQ
910 920 930 940 950 960
PGSQLPSNPT PNPLDASPRW PPGPTTSSTS SSLSSPGQRD DLIASILSEV TPTPLEELRS
970 980 990 1000 1010 1020
HKAMVKLRSR QDRDLRELHK KHQRKAVALT RRLLDGLAQA RAEGKCRPSP SALGKATNSE
1030 1040 1050 1060 1070 1080
DVKEEEEAKQ YREFQNRQVQ SLLELREAQA DVETKRKLEH LRQAHQRLKE VVLDTHTTQF
1090 1100 1110 1120 1130 1140
KRLKELNERE KKELQKILDR KRNNSISEAK TREKHKKEVE LTEINRRHIT ESVNSIRRLE
1150 1160 1170 1180 1190 1200
EAQKQRHERL VAGQQQVLQQ LEEEEPKLLA QLTQECQEQR ERLPQEIRRC LLGETAEGLG
1210 1220 1230
DGPLVACASN GHAPGSGGHL SSADSESQEE NTQL