PLCD1

Functionⁱ

The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes (PubMed:9188725).

Essential for trophoblast and placental development (By similarity).

Binds phosphatidylinositol 4,5-bisphosphate (PubMed:7890667, PubMed:9188725).

By similarity2 Publications

Catalytic activityⁱ

a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate)
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
1D-myo-inositol 1,4,5-trisphosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
a 1,2-diacyl-sn-glycerol
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.1
  "Cloning and identification of amino acid residues of human phospholipase C delta 1 essential for catalysis."
  Cheng H.F., Jiang M.J., Chen C.L., Liu S.M., Wong L.P., Lomasney J.W., King K.
  J. Biol. Chem. 270:5495-5505(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-327; ARG-338; GLU-341; HIS-356; SER-381; SER-388; LYS-434; LYS-440; LYS-441 AND ARG-549, TISSUE SPECIFICITY.
- Ref.6
  "Phosphoinositide binding specificity among phospholipase C isozymes as determined by photo-cross-linking to novel substrate and product analogs."
  Tall E., Dorman G., Garcia P., Runnels L., Shah S., Chen J., Profit A., Gu Q.M., Chaudhary A., Prestwich G.D., Rebecchi M.J.
  Biochemistry 36:7239-7248(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY.
EC:
3.1.4.11
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.1
  "Cloning and identification of amino acid residues of human phospholipase C delta 1 essential for catalysis."
  Cheng H.F., Jiang M.J., Chen C.L., Liu S.M., Wong L.P., Lomasney J.W., King K.
  J. Biol. Chem. 270:5495-5505(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-327; ARG-338; GLU-341; HIS-356; SER-381; SER-388; LYS-434; LYS-440; LYS-441 AND ARG-549, TISSUE SPECIFICITY.
- Ref.6
  "Phosphoinositide binding specificity among phospholipase C isozymes as determined by photo-cross-linking to novel substrate and product analogs."
  Tall E., Dorman G., Garcia P., Runnels L., Shah S., Chen J., Profit A., Gu Q.M., Chaudhary A., Prestwich G.D., Rebecchi M.J.
  Biochemistry 36:7239-7248(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the
forward
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Cloning and identification of amino acid residues of human phospholipase C delta 1 essential for catalysis."
  Cheng H.F., Jiang M.J., Chen C.L., Liu S.M., Wong L.P., Lomasney J.W., King K.
  J. Biol. Chem. 270:5495-5505(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-327; ARG-338; GLU-341; HIS-356; SER-381; SER-388; LYS-434; LYS-440; LYS-441 AND ARG-549, TISSUE SPECIFICITY.
direction.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate)
zoom
+
H₂O
=
1D-myo-inositol 1,4,5-trisphosphate
zoom
+
a 1,2-diacyl-sn-glycerol
zoom
+
H⁺
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
1D-myo-inositol 1-phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
a 1,2-diacyl-sn-glycerol
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Cloning and identification of amino acid residues of human phospholipase C delta 1 essential for catalysis."
  Cheng H.F., Jiang M.J., Chen C.L., Liu S.M., Wong L.P., Lomasney J.W., King K.
  J. Biol. Chem. 270:5495-5505(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-327; ARG-338; GLU-341; HIS-356; SER-381; SER-388; LYS-434; LYS-440; LYS-441 AND ARG-549, TISSUE SPECIFICITY.
This reaction proceeds in the
forward
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Cloning and identification of amino acid residues of human phospholipase C delta 1 essential for catalysis."
  Cheng H.F., Jiang M.J., Chen C.L., Liu S.M., Wong L.P., Lomasney J.W., King K.
  J. Biol. Chem. 270:5495-5505(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-327; ARG-338; GLU-341; HIS-356; SER-381; SER-388; LYS-434; LYS-440; LYS-441 AND ARG-549, TISSUE SPECIFICITY.
direction.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)
zoom
+
H₂O
=
1D-myo-inositol 1-phosphate
zoom
+
a 1,2-diacyl-sn-glycerol
zoom
+
H⁺

Cofactorⁱ

Ca²⁺1 PublicationNote: Binds 3 Ca²⁺ ions per subunit. Two of the Ca²⁺ ions are bound to the C2 domain.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	311	PROSITE-ProRule annotation	1
Metal bindingⁱ	312	Calcium 1; catalyticBy similarity	1
Metal bindingⁱ	341	Calcium 1; catalyticBy similarity	1
Metal bindingⁱ	343	Calcium 1; catalyticBy similarity	1
Active siteⁱ	356	PROSITE-ProRule annotation	1
Metal bindingⁱ	390	Calcium 1; catalyticBy similarity	1
Binding siteⁱ	438	SubstrateBy similarity	1
Binding siteⁱ	440	SubstrateBy similarity	1
Binding siteⁱ	522	SubstrateBy similarity	1
Binding siteⁱ	549	SubstrateBy similarity	1
Metal bindingⁱ	651	Calcium 2; via carbonyl oxygenBy similarity	1
Metal bindingⁱ	653	Calcium 2By similarity	1
Metal bindingⁱ	677	Calcium 2By similarity	1
Metal bindingⁱ	706	Calcium 3By similarity	1
Metal bindingⁱ	707	Calcium 3; via carbonyl oxygenBy similarity	1
Metal bindingⁱ	708	Calcium 3By similarity	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Calcium bindingⁱ	153 – 164	1PROSITE-ProRule annotationAdd BLAST		12
Calcium bindingⁱ	189 – 200	2PROSITE-ProRule annotationAdd BLAST		12

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Transducer
Biological process	Lipid degradation, Lipid metabolism
Ligand	Calcium, Metal-binding

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS07195-MONOMER
BRENDAⁱ	3.1.4.11, 2681
PathwayCommonsⁱ	P51178
Reactomeⁱ	R-HSA-1855204, Synthesis of IP3 and IP4 in the cytosol

Chemistry databases

SwissLipidsⁱ	SLP:000001065

SwissLipidsⁱ

SLP:000001065

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1Curated (EC:3.1.4.112 Publications) Alternative name(s): Phosphoinositide phospholipase C-delta-1 Phospholipase C-III Short name: PLC-III Phospholipase C-delta-1 Short name: PLC-delta-1
Gene namesⁱ	Name:PLCD1Imported
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 3

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9060, PLCD1
MIMⁱ	602142, gene
neXtProtⁱ	NX_P51178
VEuPathDBⁱ	HostDB:ENSG00000187091.13

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Nail disorder, non-syndromic congenital, 3 (NDNC3)1 Publication

The disease is caused by variants affecting the gene represented in this entry.

Disease descriptionA nail disorder characterized by a white appearance of the nail plate (true leukonychia), the nail bed (pseudoleukonychia), or neither (apparent leukonychia). Leukonychia may involve all of the nail (leukonychia totalis) or only part of the nail (leukonychia partialis), or can appear as one or more transverse bands (leukonychia striata) or white spots (leukonychia punctata).

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_066399	209	T → R in NDNC3. 1 Publication		1
Natural variantⁱVAR_066400	574	I → T in NDNC3. 1 Publication		1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	327	E → G: No effect on hydrolysis inositol phospholipids. 1 Publication	1
Mutagenesisⁱ	338	R → L: Abolishes hydrolysis inositol phospholipids. No effect on binding to phosphatidylinositol 4,5-bisphosphate. 1 Publication	1
Mutagenesisⁱ	341	E → G: Abolishes hydrolysis inositol phospholipids. No effect on binding to phosphatidylinositol 4,5-bisphosphate. 1 Publication	1
Mutagenesisⁱ	356	H → L: Abolishes hydrolysis inositol phospholipids. No effect on binding to phosphatidylinositol 4,5-bisphosphate. 1 Publication	1
Mutagenesisⁱ	381	S → A: Decreases hydrolysis inositol phospholipids. 1 Publication	1
Mutagenesisⁱ	388	S → A: No effect on hydrolysis inositol phospholipids. 1 Publication	1
Mutagenesisⁱ	434	K → Q: Decreases on hydrolysis inositol phospholipids. 1 Publication	1
Mutagenesisⁱ	440	K → Q: No effect on hydrolysis inositol phospholipids. 1 Publication	1
Mutagenesisⁱ	441	K → Q: Decreases on hydrolysis inositol phospholipids. 1 Publication	1
Mutagenesisⁱ	549	R → G: Decreases on hydrolysis inositol phospholipids. 1 Publication	1

Keywords - Diseaseⁱ

Disease variant

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5333
MalaCards human disease database More...MalaCardsⁱ	PLCD1
MIMⁱ	151600, phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000187091
Orphanetⁱ	2387, Leukonychia totalis
PharmGKBⁱ	PA33388

Miscellaneous databases

Pharosⁱ	P51178, Tchem

Pharosⁱ

P51178, Tchem

Chemistry databases

ChEMBLⁱ	CHEMBL3727
Drug and drug target database More...DrugBankⁱ	DB03401, 1D-myo-inositol 1,4,5-trisphosphate DB03956, Inositol 2,4,5-trisphosphate

Genetic variation databases

BioMutaⁱ	PLCD1
DMDMⁱ	206729887

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000088504	1 – 756	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1Add BLAST		756

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	191	O-linked (GlcNAc) serineBy similarity	1
Glycosylationⁱ	193	O-linked (GlcNAc) threonineBy similarity	1
Modified residueⁱ	457	PhosphothreonineBy similarity	1
Modified residueⁱ	460	PhosphoserineCombined sources	1

Keywords - PTMⁱ

Glycoprotein, Phosphoprotein

Proteomic databases

EPDⁱ	P51178
jPOSTⁱ	P51178
MassIVEⁱ	P51178
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P51178
PaxDbⁱ	P51178
PeptideAtlas More...PeptideAtlasⁱ	P51178
PRIDEⁱ	P51178
ProteomicsDBⁱ	56300 [P51178-1] 56301 [P51178-2]

2D gel databases

REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	IPI00746030

REPRODUCTION-2DPAGEⁱ

IPI00746030

PTM databases

GlyGenⁱ	P51178, 2 sites
iPTMnetⁱ	P51178
PhosphoSitePlusⁱ	P51178
SwissPalmⁱ	P51178

Expressionⁱ

Tissue specificityⁱ

Strongly expressed in lung, liver and heart. Also expressed at least in pancreas, kidney, skeletal muscle, placenta and brain.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000187091, Expressed in male germ cell and 238 other tissues
ExpressionAtlasⁱ	P51178, baseline and differential
Genevisibleⁱ	P51178, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000187091, Low tissue specificity

HPAⁱ

ENSG00000187091, Low tissue specificity

Interactionⁱ

Subunit structureⁱ

Interacts with TGM2.

By similarity

Binary interactionsⁱ

Hide details

P51178

With	#Exp.	IntAct
HGS [O14964]	3	EBI-4405387,EBI-740220
NTAQ1 [Q96HA8]	3	EBI-4405387,EBI-741158

GO - Molecular functionⁱ

GTPase activating protein binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- "Regulation of phospholipase C-delta1 by ARGHAP6, a GTPase-activating protein for RhoA: possible role for enhanced activity of phospholipase C in hypertension."
  Ochocka A.M., Grden M., Sakowicz-Burkiewicz M., Szutowicz A., Pawelczyk T.
  Int J Biochem Cell Biol 40:2264-2273(2008) [PubMed] [Europe PMC] [Abstract]

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	111349, 26 interactors
IntActⁱ	P51178, 14 interactors
Molecular INTeraction database More...MINTⁱ	P51178
STRINGⁱ	9606.ENSP00000430344

Chemistry databases

BindingDBⁱ

P51178

Miscellaneous databases

RNActⁱ	P51178, protein

RNActⁱ

P51178, protein

Structureⁱ

3D structure databases

SMRⁱ	P51178
ModBaseⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	21 – 130	PHPROSITE-ProRule annotationAdd BLAST	110
Domainⁱ	140 – 175	EF-hand 1PROSITE-ProRule annotationAdd BLAST	36
Domainⁱ	176 – 211	EF-hand 2PROSITE-ProRule annotationAdd BLAST	36
Domainⁱ	296 – 440	PI-PLC X-boxPROSITE-ProRule annotationAdd BLAST	145
Domainⁱ	492 – 609	PI-PLC Y-boxPROSITE-ProRule annotationAdd BLAST	118
Domainⁱ	611 – 737	C2PROSITE-ProRule annotationAdd BLAST	127

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	30 – 57	Substrate bindingBy similarityAdd BLAST		28

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	KOG0169, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000158392
HOGENOMⁱ	CLU_002738_0_2_1
InParanoidⁱ	P51178
OMAⁱ	VCQNLHI
Database of Orthologous Groups More...OrthoDBⁱ	368239at2759
PhylomeDBⁱ	P51178
TreeFamⁱ	TF313216

Family and domain databases

Gene3Dⁱ	2.30.29.30, 1 hit 2.60.40.150, 1 hit 3.20.20.190, 2 hits
InterProⁱ	View protein in InterPro IPR000008, C2_dom IPR035892, C2_domain_sf IPR011992, EF-hand-dom_pair IPR018247, EF_Hand_1_Ca_BS IPR002048, EF_hand_dom IPR011993, PH-like_dom_sf IPR001849, PH_domain IPR001192, PI-PLC_fam IPR028391, PLC-delta1 IPR017946, PLC-like_Pdiesterase_TIM-brl IPR015359, PLC_EF-hand-like IPR000909, PLipase_C_PInositol-sp_X_dom IPR001711, PLipase_C_Pinositol-sp_Y
PANTHERⁱ	PTHR10336, PTHR10336, 1 hit PTHR10336:SF80, PTHR10336:SF80, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00168, C2, 1 hit PF09279, EF-hand_like, 1 hit PF00388, PI-PLC-X, 1 hit PF00387, PI-PLC-Y, 1 hit
PRINTSⁱ	PR00390, PHPHLIPASEC
SMARTⁱ	View protein in SMART SM00239, C2, 1 hit SM00054, EFh, 2 hits SM00233, PH, 1 hit SM00148, PLCXc, 1 hit SM00149, PLCYc, 1 hit
SUPFAMⁱ	SSF47473, SSF47473, 1 hit SSF51695, SSF51695, 1 hit
PROSITEⁱ	View protein in PROSITE PS50004, C2, 1 hit PS00018, EF_HAND_1, 2 hits PS50222, EF_HAND_2, 2 hits PS50003, PH_DOMAIN, 1 hit PS50007, PIPLC_X_DOMAIN, 1 hit PS50008, PIPLC_Y_DOMAIN, 1 hit

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

Isoform 1 (identifier: P51178-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDSGRDFLTL HGLQDDEDLQ ALLKGSQLLK VKSSSWRRER FYKLQEDCKT 
        60         70         80         90        100
IWQESRKVMR TPESQLFSIE DIQEVRMGHR TEGLEKFARD VPEDRCFSIV 
       110        120        130        140        150
FKDQRNTLDL IAPSPADAQH WVLGLHKIIH HSGSMDQRQK LQHWIHSCLR 
       160        170        180        190        200
KADKNKDNKM SFKELQNFLK ELNIQVDDSY ARKIFRECDH SQTDSLEDEE 
       210        220        230        240        250
IEAFYKMLTQ RVEIDRTFAE AAGSGETLSV DQLVTFLQHQ QREEAAGPAL 
       260        270        280        290        300
ALSLIERYEP SETAKAQRQM TKDGFLMYLL SADGSAFSLA HRRVYQDMGQ 
       310        320        330        340        350
PLSHYLVSSS HNTYLLEDQL AGPSSTEAYI RALCKGCRCL ELDCWDGPNQ 
       360        370        380        390        400
EPIIYHGYTF TSKILFCDVL RAIRDYAFKA SPYPVILSLE NHCTLEQQRV 
       410        420        430        440        450
MARHLHAILG PMLLNRPLDG VTNSLPSPEQ LKGKILLKGK KLGGLLPPGG 
       460        470        480        490        500
EGGPEATVVS DEDEAAEMED EAVRSRVQHK PKEDKLRLAQ ELSDMVIYCK 
       510        520        530        540        550
SVHFGGFSSP GTPGQAFYEM ASFSENRALR LLQESGNGFV RHNVGHLSRI 
       560        570        580        590        600
YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ TPGPEMDVYQ GRFQDNGACG 
       610        620        630        640        650
YVLKPAFLRD PNGTFNPRAL AQGPWWARKR LNIRVISGQQ LPKVNKNKNS 
       660        670        680        690        700
IVDPKVTVEI HGVSRDVASR QTAVITNNGF NPWWDTEFAF EVVVPDLALI 
       710        720        730        740        750
RFLVEDYDAS SKNDFIGQST IPLNSLKQGY RHVHLMSKNG DQHPSATLFV 

KISLQD

Length:756

Mass (Da):85,665

Last modified:September 23, 2008 - v2

Checksum:ⁱ6C6FD7F89BA08C83

GO

Isoform 2 (identifier: P51178-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-11: MDSGRDFLTLH → MQCLGIRSRSRSRELYLQERSLKVAALNGRRL

« Hide

        10         20         30         40         50
MQCLGIRSRS RSRELYLQER SLKVAALNGR RLGLQDDEDL QALLKGSQLL 
        60         70         80         90        100
KVKSSSWRRE RFYKLQEDCK TIWQESRKVM RTPESQLFSI EDIQEVRMGH 
       110        120        130        140        150
RTEGLEKFAR DVPEDRCFSI VFKDQRNTLD LIAPSPADAQ HWVLGLHKII 
       160        170        180        190        200
HHSGSMDQRQ KLQHWIHSCL RKADKNKDNK MSFKELQNFL KELNIQVDDS 
       210        220        230        240        250
YARKIFRECD HSQTDSLEDE EIEAFYKMLT QRVEIDRTFA EAAGSGETLS 
       260        270        280        290        300
VDQLVTFLQH QQREEAAGPA LALSLIERYE PSETAKAQRQ MTKDGFLMYL 
       310        320        330        340        350
LSADGSAFSL AHRRVYQDMG QPLSHYLVSS SHNTYLLEDQ LAGPSSTEAY 
       360        370        380        390        400
IRALCKGCRC LELDCWDGPN QEPIIYHGYT FTSKILFCDV LRAIRDYAFK 
       410        420        430        440        450
ASPYPVILSL ENHCTLEQQR VMARHLHAIL GPMLLNRPLD GVTNSLPSPE 
       460        470        480        490        500
QLKGKILLKG KKLGGLLPPG GEGGPEATVV SDEDEAAEME DEAVRSRVQH 
       510        520        530        540        550
KPKEDKLRLA QELSDMVIYC KSVHFGGFSS PGTPGQAFYE MASFSENRAL 
       560        570        580        590        600
RLLQESGNGF VRHNVGHLSR IYPAGWRTDS SNYSPVEMWN GGCQIVALNF 
       610        620        630        640        650
QTPGPEMDVY QGRFQDNGAC GYVLKPAFLR DPNGTFNPRA LAQGPWWARK 
       660        670        680        690        700
RLNIRVISGQ QLPKVNKNKN SIVDPKVTVE IHGVSRDVAS RQTAVITNNG 
       710        720        730        740        750
FNPWWDTEFA FEVVVPDLAL IRFLVEDYDA SSKNDFIGQS TIPLNSLKQG 
       760        770 
YRHVHLMSKN GDQHPSATLF VKISLQD

Show »

Length:777

Mass (Da):88,135

Checksum:ⁱ6260C76BE397266B

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	224	S → P in AAA73567 (PubMed:7890667).Curated	1
Sequence conflictⁱ	264	A → T in AAA73567 (PubMed:7890667).Curated	1
Sequence conflictⁱ	591	G → D in AAA73567 (PubMed:7890667).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_066399	209	T → R in NDNC3. 1 Publication	1
Natural variantⁱVAR_046560	257	R → H. Corresponds to variant dbSNP:rs933135Ensembl.	1
Natural variantⁱVAR_066400	574	I → T in NDNC3. 1 Publication	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_042919	1 – 11	MDSGRDFLTLH → MQCLGIRSRSRSRELYLQER SLKVAALNGRRL in isoform 2. 1 PublicationAdd BLAST		11

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U09117 mRNA Translation: AAA73567.1 AK090774 mRNA Translation: BAG52226.1 AC144536 Genomic DNA No translation available. CH471055 Genomic DNA Translation: EAW64507.1 BC050382 mRNA Translation: AAH50382.2
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS2671.1 [P51178-1] CCDS46793.1 [P51178-2]
PIRⁱ	A55943
NCBI Reference Sequences More...RefSeqⁱ	NP_001124436.1, NM_001130964.1 [P51178-2] NP_006216.2, NM_006225.3 [P51178-1]

Genome annotation databases

Ensemblⁱ	ENST00000334661; ENSP00000335600; ENSG00000187091 [P51178-1] ENST00000463876; ENSP00000430344; ENSG00000187091 [P51178-2]
GeneIDⁱ	5333
KEGGⁱ	hsa:5333
UCSC genome browser More...UCSCⁱ	uc003chm.4, human [P51178-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P51178	Phosphoinositide phospholipase C		HUMAN		756	UniRef100_P51178

Protein	Similar proteins		Species	Score	Length	Source
P51178	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1	)	RAT		756	UniRef90_P10688
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1		MOUSE		756
Phosphoinositide phospholipase C		CALJA		900
Phosphoinositide phospholipase C		PANPA		781
Phosphoinositide phospholipase C		NOMLE		779
+215

Protein	Similar proteins		Species	Score	Length	Source
P51178	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1	)	RAT		756	UniRef50_P10688
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1		MOUSE		756
Phosphoinositide phospholipase C		CALJA		900
Phosphoinositide phospholipase C		PANPA		781
Phosphoinositide phospholipase C		PANTR		779
+636

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U09117 mRNA Translation: AAA73567.1 AK090774 mRNA Translation: BAG52226.1 AC144536 Genomic DNA No translation available. CH471055 Genomic DNA Translation: EAW64507.1 BC050382 mRNA Translation: AAH50382.2
CCDSⁱ	CCDS2671.1 [P51178-1] CCDS46793.1 [P51178-2]
PIRⁱ	A55943
RefSeqⁱ	NP_001124436.1, NM_001130964.1 [P51178-2] NP_006216.2, NM_006225.3 [P51178-1]

3D structure databases

SMRⁱ	P51178
ModBaseⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	111349, 26 interactors
IntActⁱ	P51178, 14 interactors
MINTⁱ	P51178
STRINGⁱ	9606.ENSP00000430344

Chemistry databases

BindingDBⁱ	P51178
ChEMBLⁱ	CHEMBL3727
DrugBankⁱ	DB03401, 1D-myo-inositol 1,4,5-trisphosphate DB03956, Inositol 2,4,5-trisphosphate
SwissLipidsⁱ	SLP:000001065

PTM databases

GlyGenⁱ	P51178, 2 sites
iPTMnetⁱ	P51178
PhosphoSitePlusⁱ	P51178
SwissPalmⁱ	P51178

Genetic variation databases

BioMutaⁱ	PLCD1
DMDMⁱ	206729887

2D gel databases

REPRODUCTION-2DPAGEⁱ	IPI00746030

REPRODUCTION-2DPAGEⁱ

IPI00746030

Proteomic databases

EPDⁱ	P51178
jPOSTⁱ	P51178
MassIVEⁱ	P51178
MaxQBⁱ	P51178
PaxDbⁱ	P51178
PeptideAtlasⁱ	P51178
PRIDEⁱ	P51178
ProteomicsDBⁱ	56300 [P51178-1] 56301 [P51178-2]

Protocols and materials databases

Antibodypediaⁱ	4086, 171 antibodies
The DNASU plasmid repository More...DNASUⁱ	5333

Genome annotation databases

Ensemblⁱ	ENST00000334661; ENSP00000335600; ENSG00000187091 [P51178-1] ENST00000463876; ENSP00000430344; ENSG00000187091 [P51178-2]
GeneIDⁱ	5333
KEGGⁱ	hsa:5333
UCSCⁱ	uc003chm.4, human [P51178-1]

Organism-specific databases

CTDⁱ	5333
DisGeNETⁱ	5333
GeneCardsⁱ	PLCD1
HGNCⁱ	HGNC:9060, PLCD1
HPAⁱ	ENSG00000187091, Low tissue specificity
MalaCardsⁱ	PLCD1
MIMⁱ	151600, phenotype 602142, gene
neXtProtⁱ	NX_P51178
OpenTargetsⁱ	ENSG00000187091
Orphanetⁱ	2387, Leukonychia totalis
PharmGKBⁱ	PA33388
VEuPathDBⁱ	HostDB:ENSG00000187091.13
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0169, Eukaryota
GeneTreeⁱ	ENSGT00940000158392
HOGENOMⁱ	CLU_002738_0_2_1
InParanoidⁱ	P51178
OMAⁱ	VCQNLHI
OrthoDBⁱ	368239at2759
PhylomeDBⁱ	P51178
TreeFamⁱ	TF313216

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS07195-MONOMER
BRENDAⁱ	3.1.4.11, 2681
PathwayCommonsⁱ	P51178
Reactomeⁱ	R-HSA-1855204, Synthesis of IP3 and IP4 in the cytosol

Miscellaneous databases

BioGRID-ORCSⁱ	5333, 7 hits in 997 CRISPR screens
GeneWikiⁱ	PLCD1
GenomeRNAiⁱ	5333
Pharosⁱ	P51178, Tchem
Protein Ontology More...PROⁱ	PR:P51178
RNActⁱ	P51178, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000187091, Expressed in male germ cell and 238 other tissues
ExpressionAtlasⁱ	P51178, baseline and differential
Genevisibleⁱ	P51178, HS

Family and domain databases

Gene3Dⁱ	2.30.29.30, 1 hit 2.60.40.150, 1 hit 3.20.20.190, 2 hits
InterProⁱ	View protein in InterPro IPR000008, C2_dom IPR035892, C2_domain_sf IPR011992, EF-hand-dom_pair IPR018247, EF_Hand_1_Ca_BS IPR002048, EF_hand_dom IPR011993, PH-like_dom_sf IPR001849, PH_domain IPR001192, PI-PLC_fam IPR028391, PLC-delta1 IPR017946, PLC-like_Pdiesterase_TIM-brl IPR015359, PLC_EF-hand-like IPR000909, PLipase_C_PInositol-sp_X_dom IPR001711, PLipase_C_Pinositol-sp_Y
PANTHERⁱ	PTHR10336, PTHR10336, 1 hit PTHR10336:SF80, PTHR10336:SF80, 1 hit
Pfamⁱ	View protein in Pfam PF00168, C2, 1 hit PF09279, EF-hand_like, 1 hit PF00388, PI-PLC-X, 1 hit PF00387, PI-PLC-Y, 1 hit
PRINTSⁱ	PR00390, PHPHLIPASEC
SMARTⁱ	View protein in SMART SM00239, C2, 1 hit SM00054, EFh, 2 hits SM00233, PH, 1 hit SM00148, PLCXc, 1 hit SM00149, PLCYc, 1 hit
SUPFAMⁱ	SSF47473, SSF47473, 1 hit SSF51695, SSF51695, 1 hit
PROSITEⁱ	View protein in PROSITE PS50004, C2, 1 hit PS00018, EF_HAND_1, 2 hits PS50222, EF_HAND_2, 2 hits PS50003, PH_DOMAIN, 1 hit PS50007, PIPLC_X_DOMAIN, 1 hit PS50008, PIPLC_Y_DOMAIN, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PLCD1_HUMAN
Accessionⁱ	P51178Primary (citable) accession number: P51178 Secondary accession number(s): B3KR14, Q86VN8
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
	Last sequence update:	September 23, 2008
	Last modified:	June 2, 2021
	This is version 209 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

Reference proteome

Documents

Human chromosome 3
Human chromosome 3: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P51178 (PLCD1_HUMAN)

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

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Chemistry databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted

Plasma Membrane

Other locations

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

P51178

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Genetic variation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ