Descriptions

PLCD1 functions the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3), which is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Autoinhibitory region is a portion of the linker that separates the conserved X and Y boxes comprising the catalytic TIM barrel. The disordered X/Y linker is capable of autoinhibition by hindering productive binding of PLC-δ1 to membranes and thereby restricting access of PtdIns(4,5)P2 to the active site. 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)

Target domain

316-656 (TIM barrel)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q8R3B1

Entry ID Method Resolution Chain Position Source
AF-Q8R3B1-F1 Predicted AlphaFoldDB

52 variants for Q8R3B1

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3400407573 6 D>G No EVA
rs254615756 17 P>L No EVA
rs3389087294 37 R>H No EVA
rs3389090838 92 P>L No EVA
rs3389049607 92 P>S No EVA
rs3389049588 98 S>F No EVA
rs3389076916 101 F>V No EVA
rs3389049585 130 D>N No EVA
rs3389074722 145 I>F No EVA
rs3547795131 146 H>Y No EVA
rs3399645048 149 L>W No EVA
rs3389083481 177 D>N No EVA
rs1132316980 212 A>V No EVA
rs3400743108 223 G>D No EVA
rs3400740464 224 S>P No EVA
rs3389068813 253 S>T No EVA
rs3389049604 263 T>N No EVA
rs3389083418 263 T>P No EVA
rs3389056022 285 N>S No EVA
rs3547643746 306 L>F No EVA
rs3389091676 316 L>P No EVA
rs3547630856 320 L>F No EVA
rs3389083444 323 P>S No EVA
rs3389090794 339 C>* No EVA
rs3389068820 340 L>V No EVA
rs3389056009 344 C>W No EVA
rs3389074743 353 I>F No EVA
rs247141402 357 G>C No EVA
rs247141402 357 G>S No EVA
rs3389068892 358 Y>C No EVA
rs3389060911 365 L>P No EVA
rs3547587355 381 S>T No EVA
rs3389083649 396 E>G No EVA
rs3547622090 408 I>N No EVA
rs3389074705 421 V>A No EVA
rs3389076858 424 S>R No EVA
rs3389074797 433 E>G No EVA
rs250719358 435 I>V No EVA
rs3410685010 438 K>T No EVA
rs3389087372 452 N>D No EVA
rs3547733636 494 D>N No EVA
rs3547631004 501 S>G No EVA
rs3389090870 565 V>L No EVA
rs3389082636 593 F>S No EVA
rs3389081108 596 N>I No EVA
rs3400834985 622 Q>* No EVA
rs3389074755 622 Q>L No EVA
rs3389087333 691 V>L No EVA
rs3389056018 696 D>N No EVA
rs3389083701 710 S>Y No EVA
rs3400821529 727 K>N No EVA
rs3547686442 749 F>I No EVA

No associated diseases with Q8R3B1

10 regional properties for Q8R3B1

Type Name Position InterPro Accession
domain C2 domain 609 - 737 IPR000008
domain Phosphatidylinositol-specific phospholipase C, X domain 296 - 441 IPR000909
domain Phospholipase C, phosphatidylinositol-specific, Y domain 492 - 609 IPR001711
domain Pleckstrin homology domain 19 - 132 IPR001849
domain EF-hand domain 140 - 175 IPR002048
domain Phosphoinositide-specific phospholipase C, EF-hand-like domain 204 - 288 IPR015359
binding_site EF-Hand 1, calcium-binding site 153 - 165 IPR018247-1
binding_site EF-Hand 1, calcium-binding site 189 - 201 IPR018247-2
domain 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1, catalytic domain 295 - 596 IPR028391
domain 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1, EF-hand domain 144 - 283 IPR046975

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

3 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.
mitochondrial membrane Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.

7 GO annotations of molecular function

Name Definition
calcium ion binding Binding to a calcium ion (Ca2+).
calcium-dependent phospholipid binding Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester, in the presence of calcium.
enzyme binding Binding to an enzyme, a protein with catalytic activity.
inositol 1,4,5 trisphosphate binding Binding to inositol 1,4,5 trisphosphate.
phosphatidylinositol phospholipase C activity Catalysis of the reaction
phosphatidylinositol-4,5-bisphosphate binding Binding to phosphatidylinositol-4,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' and 5' positions.
phospholipid binding Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester.

14 GO annotations of biological process

Name Definition
angiogenesis Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels.
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.
labyrinthine layer blood vessel development The process whose specific outcome is the progression of a blood vessel of the labyrinthine layer of the placenta over time, from its formation to the mature structure. The embryonic vessels grow through the layer to come in close contact with the maternal blood supply.
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).
positive regulation of inositol trisphosphate biosynthetic process Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
positive regulation of norepinephrine secretion Any process that increases the frequency, rate or extent of the regulated release of norepinephrine.
regulation of cell population proliferation Any process that modulates the frequency, rate or extent of cell proliferation.
regulation of cytosolic calcium ion concentration Any process involved in the maintenance of an internal steady state of calcium ions within the cytosol of a cell or between the cytosol and its surroundings.
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.
response to calcium ion Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a calcium ion stimulus.
response to peptide hormone Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a peptide hormone stimulus. A peptide hormone is any of a class of peptides that are secreted into the blood stream and have endocrine functions in living animals.

29 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
Q1RML2 PLCZ1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1 Bos taurus (Bovine) PR
P10895 PLCD1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 Bos taurus (Bovine) SS
Q2VRL0 PLCZ1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1 Gallus gallus (Chicken) PR
Q86YW0 PLCZ1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1 Homo sapiens (Human) PR
Q9P212 PLCE1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1 Homo sapiens (Human) SS
Q9BRC7 PLCD4 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 Homo sapiens (Human) SS
Q15111 PLCL1 Inactive phospholipase C-like protein 1 Homo sapiens (Human) PR
Q9UPR0 PLCL2 Inactive phospholipase C-like protein 2 Homo sapiens (Human) PR
Q8N3E9 PLCD3 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 Homo sapiens (Human) SS
P51178 PLCD1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 Homo sapiens (Human) EV
Q8K2J0 Plcd3 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 Mus musculus (Mouse) PR
Q8K394 Plcl2 Inactive phospholipase C-like protein 2 Mus musculus (Mouse) PR
Q8K4S1 Plce1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1 Mus musculus (Mouse) SS
P51432 Plcb3 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 Mus musculus (Mouse) SS
Q62077 Plcg1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-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
Q7YRU3 PLCZ 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1 Sus scrofa (Pig) PR
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
Q39032 PLC1 Phosphoinositide phospholipase C 1 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
Q8GV43 PLC6 Phosphoinositide phospholipase C 6 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
Q944C1 PLC4 Phosphoinositide phospholipase C 4 Arabidopsis thaliana (Mouse-ear cress) PR
A5D6R3 plcd3a 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3-A Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MDSGRDFLTL HGLQDDPDLQ ALLKGSQLLK VKSSSWRRER FYKLQEDCKT IWQESRKVMR
70 80 90 100 110 120
SPESQLFSIE DIQEVRMGHR TEGLEKFARD IPEDRCFSIV FKDQRNTLDL IAPSPADVQH
130 140 150 160 170 180
WVQGLRKIID RSGSMDQRQK LQHWIHSCLR KADKNKDNKM NFKEVKDFLK ELNVQVDDSY
190 200 210 220 230 240
ARKIFRECDH SQTDSLEDEE IETFYRMLTQ RAEIDRAFAE AAGSAETLSV EKLVTFLQHQ
250 260 270 280 290 300
QREEEAGPAL ALSLIERYEP SETAKAQRQM TKDGFLMYLL SADGNAFSLA HRRVYQDMNQ
310 320 330 340 350 360
PLSHYLVSSS HNTYLLEDQL TGPSSTEAYI RALCKGCRCL ELDCWDGPNQ EPIIYHGYTF
370 380 390 400 410 420
TSKILFCDVL RAIRDYAFKA SPYPVILSLE NHCSLEQQRV MAHHLRAILG PMLLDQPLDG
430 440 450 460 470 480
VTTSLPSPEQ LKEKILLKGK KLGGLLPAGG ENGPEATDVS DEDEAAEMED EAVRSQVQHK
490 500 510 520 530 540
PKEDKLKLVP ELSDMVIYCK SVHFGGFSSP STSGQAFYEM ASFSESRALR LLQESGNSFV
550 560 570 580 590 600
RHNVGHLSRI YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ TPGPEMDVYL GCFQDNGGCG
610 620 630 640 650 660
YVLKPAFLRD PDTTFNSRAL TQGPWWAPKK LRVWIISGQQ LPKVNKNKNS IVDPKVIVEI
670 680 690 700 710 720
HGVGQDVASR QTAVITNNGF NPRWDTEFEF VVAVPDLALV RFMVEDYDSS SKNDFIGQST
730 740 750
IPWNSLKQGY RHVHLLSKNG DLHPSATLFV KISIQD