Descriptions

(Annotation based on sequence homology with Q00722)
PLCB2 encodes for 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2, hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P2) into the second messengers diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Autoinhibitory region is a portion of the linker that separates the conserved X and Y boxes comprising the catalytic TIM barrel, at residues 466-537, and occludes the active site of PLCB2. Specifically, the ordered region of X/Y linker at residues 516-535 seems to fine-tune access to the active site, in which deletion of this region only gave partial activation of PLCB2. However, the disordered region of X/Y linker at residues 470-515 is the major autoinhibitory region, in which deletion of this region enhanced activity by 10-fold higher basal activity relative to the ordered region.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for O89040

Entry ID Method Resolution Chain Position Source
AF-O89040-F1 Predicted AlphaFoldDB

7 variants for O89040

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3319985897 1015 M>I No EVA
rs105561320 1020 R>I No EVA
rs105647278 1030 F>L No EVA
rs106050987 1033 T>P No EVA
rs105854020 1036 T>P No EVA
rs3320002478 1140 M>I No EVA
rs3319889292 1146 A>V No EVA

No associated diseases with O89040

8 regional properties for O89040

Type Name Position InterPro Accession
domain C2 domain 666 - 794 IPR000008
domain Phosphatidylinositol-specific phospholipase C, X domain 312 - 464 IPR000909
domain Phospholipase C, phosphatidylinositol-specific, Y domain 550 - 666 IPR001711
domain Phospholipase C-beta, C-terminal domain 977 - 1151 IPR014815
domain Phosphoinositide-specific phospholipase C, EF-hand-like domain 214 - 303 IPR015359
domain 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2, catalytic domain 311 - 653 IPR028403
domain PLC-beta, PH domain 12 - 144 IPR037862
domain 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2, EF-hand domain 149 - 299 IPR046969

Functions

Description
EC Number 3.1.4.11 Phosphoric diester hydrolases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 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.
G-protein beta/gamma-subunit complex The heterodimer formed by the beta and gamma subunits of a heterotrimeric G protein, which dissociates from the alpha subunit upon guanine nuclotide exchange.
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

5 GO annotations of molecular function

Name Definition
calcium ion binding Binding to a calcium ion (Ca2+).
G-protein beta/gamma-subunit complex binding Binding to a complex of G-protein beta/gamma subunits.
phosphatidylinositol phospholipase C activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H(2)O = 1,2-diacylglycerol + 1D-myo-inositol 1,4,5-trisphosphate + H(+).
phospholipase C activity Catalysis of the reaction: a phospholipid + H2O = 1,2-diacylglycerol + a phosphatidate.
phospholipid binding Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester.

6 GO annotations of biological process

Name Definition
detection of chemical stimulus involved in sensory perception of bitter taste The series of events required for a bitter taste stimulus to be received and converted to a molecular signal.
lipid catabolic process The chemical reactions and pathways resulting in the breakdown of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.
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.
phospholipase C-activating G protein-coupled receptor signaling pathway A G protein-coupled receptor signaling pathway in which the signal is transmitted via the activation of phospholipase C (PLC) and a subsequent increase in the intracellular concentration of inositol trisphosphate (IP3) and diacylglycerol (DAG).
sensory perception of bitter taste The series of events required to receive a bitter taste stimulus, convert it to a molecular signal, and recognize and characterize the signal. This is a neurological process.

16 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
Q00722 PLCB2 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 Homo sapiens (Human) EV
A3KGF7 Plcb2 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 Mus musculus (Mouse) PR
P24135 Plcg2 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2 Rattus norvegicus (Rat) SS
P10686 Plcg1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 Rattus norvegicus (Rat) EV
P10687 Plcb1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 Rattus norvegicus (Rat) SS
Q99P84 Plce1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1 Rattus norvegicus (Rat) EV
P10688 Plcd1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 Rattus norvegicus (Rat) SS
Q99JE6 Plcb3 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 Rattus norvegicus (Rat) SS
Q39032 PLC1 Phosphoinositide phospholipase C 1 Arabidopsis thaliana (Mouse-ear cress) PR
Q944C2 PLC5 Phosphoinositide phospholipase C 5 Arabidopsis thaliana (Mouse-ear cress) PR
Q9STZ3 PLC8 Phosphoinositide phospholipase C 8 Arabidopsis thaliana (Mouse-ear cress) PR
Q8GV43 PLC6 Phosphoinositide phospholipase C 6 Arabidopsis thaliana (Mouse-ear cress) PR
Q56W08 PLC3 Phosphoinositide phospholipase C 3 Arabidopsis thaliana (Mouse-ear cress) PR
Q6NMA7 PLC9 Phosphoinositide phospholipase C 9 Arabidopsis thaliana (Mouse-ear cress) PR
Q944C1 PLC4 Phosphoinositide phospholipase C 4 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MSLLNPVLLP PKVKAYLSQG ERFIKWDDET SIASPVILRV DPKGYYLYWT HQSKEMEFLD
70 80 90 100 110 120
VTSIRDTRFG KFAKIPKSQK LREVFNMDFP DNHFLLKTFT VVSGPDMVGL TFHNFVSYKE
130 140 150 160 170 180
NVGKDWAEDV LALAKHPMTA NASRSTFLDK ILVKLKMQLS PEGKIPVKNF FQMFPADRKR
190 200 210 220 230 240
VEAALSACHL AKGKNDAINP EDFPESVYKS FLMSLCPRPE IDEIFTSYHA KAKPYMTKEH
250 260 270 280 290 300
LTKFINQKQR DPRLNSLLFP PARPEQVQAL IDKYEPSGIN VQRGQLSPEG MVWFLCGPEN
310 320 330 340 350 360
SVLAHDTLRI HQDMTQPLNH YFINSSHNTY LTAGQFSGPS SAEMYRQVLL SGCRCVELDC
370 380 390 400 410 420
WKGKPPDEEP IITHGFTMTT DILFKEAVEA IAESAFKTSP YPVILSFENH VDSPRQQAKM
430 440 450 460 470 480
AEYCRTMFGE TLLTEPLENF PLKPGMPLPS PEDLRGKILI KNKKNQFSGP ASPNKKPDGV
490 500 510 520 530 540
SEGGFPSSVP VEEDTGWTAE DRTEVEEGEE EEEVEEEEEE ESGNLDEEEI KKMQSDEGTA
550 560 570 580 590 600
GLEVTAYEEM SSLVNYIQPT KFISFEFSAQ KNRSYLVSSF TELKAYELLS KASMQFVDYN
610 620 630 640 650 660
KRQMSRVYPK GTRMDSSNYM PQMFWNAGCQ MVALNFQTMD LPMQQNMALF EFNGQSGYLL
670 680 690 700 710 720
KHEFMRRQDK QFNPFSVDRI DVVVATTLSI TVISGQFLSE RSVRTYVEVE LFGLPGDPKR
730 740 750 760 770 780
RYRTKLSPTA NSINPVWKEE PFIFEKILVP ELASLRIAVM EEGGKFIGHR IIPINALHSG
790 800 810 820 830 840
YHHLCLRSES NMPLTMPALF VFLEMKDYVP DTWADLTVAL ANPIKYFSAH DKKSVKLKEV
850 860 870 880 890 900
TGSLPEKLFS GIPVASQSNG APVSAGNGST APGTKAKEEA TKEVAEPQTT SLEELRELKG
910 920 930 940 950 960
VVKLQRRHEK ELRELERRGA RRWEELLQRG AAQLAELQDP AASCKLRPGK GSRKKRIVPC
970 980 990 1000 1010 1020
EETIVVPREV LEGPDPRVQD LKDRLEQELQ QQGEEQYRSV LKRKEQHVTE QIAKMMELAR
1030 1040 1050 1060 1070 1080
EKQAAELKSF KETSETDTKE MKKKLEAKRL ERIQAMTKVT TDKVAQERLK REINNSHIQE
1090 1100 1110 1120 1130 1140
VVQAVKQMTE TLERHQEKLE EKQTACLEQI QAMEKQFQEK ALAEYEAKMK GLEAEVKESM
1150 1160 1170 1180
RACFKACFPT EAEEKPERPC EASEESCPQE PLVNKTDTQE SRL