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Protein

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3

Gene

Plcd3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca2+ from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow.1 Publication

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.

Cofactori

Ca2+By similarityNote: Binds 3 Ca2+ ions per subunit. Two of the Ca2+ ions are bound to the C2 domain.By similarity

Enzyme regulationi

Strongly activated by phosphatidic acid. Inhibited by phosphatidylethanolamine (PtdEtn), phosphatidylcholine (PtdCho), sphingomyelin and phosphatidylserine (PtdSer) (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei348PROSITE-ProRule annotation1
Metal bindingi349Calcium 1; catalyticBy similarity1
Metal bindingi378Calcium 1; catalyticBy similarity1
Metal bindingi380Calcium 1; catalyticBy similarity1
Active sitei393PROSITE-ProRule annotation1
Metal bindingi427Calcium 1; catalyticBy similarity1
Binding sitei476SubstrateBy similarity1
Binding sitei478SubstrateBy similarity1
Binding sitei553SubstrateBy similarity1
Binding sitei580SubstrateBy similarity1
Metal bindingi679Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi681Calcium 2By similarity1
Metal bindingi705Calcium 2By similarity1
Metal bindingi734Calcium 3By similarity1
Metal bindingi735Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi736Calcium 3By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi191 – 2021Sequence analysisAdd BLAST12
Calcium bindingi227 – 2382Sequence analysisAdd BLAST12

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: MGI
  • intracellular signal transduction Source: InterPro
  • labyrinthine layer blood vessel development Source: MGI
  • lipid catabolic process Source: UniProtKB-KW
  • regulation of cell proliferation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-1855204. Synthesis of IP3 and IP4 in the cytosol.

Chemistry databases

SwissLipidsiSLP:000001068.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 (EC:3.1.4.11)
Alternative name(s):
Phosphoinositide phospholipase C-delta-3
Phospholipase C-delta-3
Short name:
PLC-delta-3
Gene namesi
Name:Plcd3
Synonyms:Kiaa1964
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:107451. Plcd3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice lacking Plcd1 and Plcd3 die between 11.5 and 13.5 dpc. They exhibit severe disruption of the normal labyrinth architecture in the placenta and decreased placental vascularization, as well as abnormal proliferation and apoptosis of trophoblasts in the labyrinth area. Furthermore, Plcd1 and Plcd3 double knockout embryos supplied with a normal placenta by the tetraploid aggregation method survive beyond 14.5 dpc, indicating that the embryonic lethality is caused by a defect in trophoblasts.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003068221 – 7851-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3Add BLAST785

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei101PhosphoserineBy similarity1
Modified residuei492PhosphoserineCombined sources1
Modified residuei569PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8K2J0.
PaxDbiQ8K2J0.
PeptideAtlasiQ8K2J0.
PRIDEiQ8K2J0.

PTM databases

iPTMnetiQ8K2J0.
PhosphoSitePlusiQ8K2J0.

Expressioni

Gene expression databases

BgeeiENSMUSG00000020937.
CleanExiMM_PLCD3.
ExpressionAtlasiQ8K2J0. baseline and differential.
GenevisibleiQ8K2J0. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000099366.

Structurei

3D structure databases

ProteinModelPortaliQ8K2J0.
SMRiQ8K2J0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini65 – 168PHAdd BLAST104
Domaini178 – 213EF-hand 1Add BLAST36
Domaini214 – 249EF-hand 2Add BLAST36
Domaini246 – 281EF-hand 3Add BLAST36
Domaini333 – 478PI-PLC X-boxPROSITE-ProRule annotationAdd BLAST146
Domaini524 – 640PI-PLC Y-boxPROSITE-ProRule annotationAdd BLAST117
Domaini643 – 748C2PROSITE-ProRule annotationAdd BLAST106

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni69 – 97Substrate bindingBy similarityAdd BLAST29

Domaini

The C2 domain is a Ca2+-dependent membrane-targeting module.By similarity
The PH domain mediates interaction with the surface membrane by binding to PIP2.By similarity

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 3 EF-hand domains.Curated
Contains 1 PH domain.Curated
Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0169. Eukaryota.
ENOG410XPSW. LUCA.
GeneTreeiENSGT00760000118936.
HOGENOMiHOG000006871.
HOVERGENiHBG053610.
InParanoidiQ8K2J0.
KOiK05857.
OMAiNTQQLTR.
OrthoDBiEOG091G02KH.
PhylomeDBiQ8K2J0.
TreeFamiTF313216.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001192. PI-PLC_fam.
IPR028406. PLC-delta3.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF33. PTHR10336:SF33. 1 hit.
PfamiPF00168. C2. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K2J0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLCGGWKRSR RSPEESRVSA QVAAPLAFPP SPASSDSSTK RPGLRALKKM
60 70 80 90 100
GLTEDEDVQA MLRGSRLLKI RSRTWHKERL YRLQEDGLSV WFQRRIPRAA
110 120 130 140 150
SKHIFFVQHI EAVREGHQSE GLRRFGGAFA PACCLTIAFK GRRKNLDLAA
160 170 180 190 200
PTAEEAQRWV RGLAKLRARL DAMSQRERLD HWIHSYLHRA DSDQDSKMSF
210 220 230 240 250
KEIKSLLRMV NVDMNDMYAY RLFKECDHSN NERLEGAEIE AFLRRLLKRP
260 270 280 290 300
ELEEIFRRYS GEDRVLSASE LLEFLEDQGE DGATLACAQQ LIQTYELNET
310 320 330 340 350
AKQHELMTLD GFMMYLLSPE GAALNVAHTC VFQDMGQPLA HYFISSSHNT
360 370 380 390 400
YLTDSQIGGT SSTEAYIRAF AQGCRCVELD CWEGPGGEPV IYHGHTLTSK
410 420 430 440 450
ILFRDVIQAV RDHAFTSSPY PVILSLENHC GLEQQAVMAR HLRSILGDML
460 470 480 490 500
VTQALDSQNP EELPSPEQLK GRILVKGKKL PAARSEDGRI LSDREEEEEE
510 520 530 540 550
EEEAEEALEA AEQRSRAKQI SPELSALAVY CCATRLRTLD PSPGPPQSCT
560 570 580 590 600
VGSLSERKAR KFTREAGTSF VRHNTQQLTR VYPLGLRMNS ANYNPQEMWN
610 620 630 640 650
SGCQLVALNF QTPGYEMDLN TGRFLINGQC GYVLKPAYLR QLNTTFDPEC
660 670 680 690 700
PGPPRTTLAI QVLTAQQLPK LNAEKPSSIV DPLVRVEIHG VPEDCAQKET
710 720 730 740 750
DYVLNNGFNP CWEQTLQFRL RAPELVLVRF VVEDYDTTSP NDFVGQSTLP
760 770 780
LSSLKQGYRH IHLLSKDGAS LAPATLFVHI RIQNS
Length:785
Mass (Da):88,607
Last modified:October 2, 2007 - v2
Checksum:i8B3DE84FB7A52238
GO

Sequence cautioni

The sequence BAC32829 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAD32589 differs from that shown. Intron retention.Curated
The sequence CAM22088 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti199S → N in BAE26150 (PubMed:16141072).Curated1
Sequence conflicti301 – 302AK → GE in BAD32589 (PubMed:15368895).Curated2
Sequence conflicti378E → K in BAE26150 (PubMed:16141072).Curated1
Sequence conflicti540D → E in AAH31392 (PubMed:15489334).Curated1
Sequence conflicti659A → T in BAE26150 (PubMed:16141072).Curated1
Sequence conflicti660I → V in BAE26150 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173311 Transcribed RNA. Translation: BAD32589.1. Sequence problems.
AK046669 mRNA. Translation: BAC32829.1. Different initiation.
AK144950 mRNA. Translation: BAE26150.1.
AL731805 Genomic DNA. Translation: CAM22088.1. Sequence problems.
AL731805 Genomic DNA. Translation: CAM22089.1.
BC031392 mRNA. Translation: AAH31392.1.
CCDSiCCDS25512.1.
RefSeqiNP_690026.2. NM_152813.3.
UniGeneiMm.264743.

Genome annotation databases

EnsembliENSMUST00000103077; ENSMUSP00000099366; ENSMUSG00000020937.
GeneIDi72469.
KEGGimmu:72469.
UCSCiuc007ltf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173311 Transcribed RNA. Translation: BAD32589.1. Sequence problems.
AK046669 mRNA. Translation: BAC32829.1. Different initiation.
AK144950 mRNA. Translation: BAE26150.1.
AL731805 Genomic DNA. Translation: CAM22088.1. Sequence problems.
AL731805 Genomic DNA. Translation: CAM22089.1.
BC031392 mRNA. Translation: AAH31392.1.
CCDSiCCDS25512.1.
RefSeqiNP_690026.2. NM_152813.3.
UniGeneiMm.264743.

3D structure databases

ProteinModelPortaliQ8K2J0.
SMRiQ8K2J0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000099366.

Chemistry databases

SwissLipidsiSLP:000001068.

PTM databases

iPTMnetiQ8K2J0.
PhosphoSitePlusiQ8K2J0.

Proteomic databases

MaxQBiQ8K2J0.
PaxDbiQ8K2J0.
PeptideAtlasiQ8K2J0.
PRIDEiQ8K2J0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103077; ENSMUSP00000099366; ENSMUSG00000020937.
GeneIDi72469.
KEGGimmu:72469.
UCSCiuc007ltf.2. mouse.

Organism-specific databases

CTDi113026.
MGIiMGI:107451. Plcd3.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0169. Eukaryota.
ENOG410XPSW. LUCA.
GeneTreeiENSGT00760000118936.
HOGENOMiHOG000006871.
HOVERGENiHBG053610.
InParanoidiQ8K2J0.
KOiK05857.
OMAiNTQQLTR.
OrthoDBiEOG091G02KH.
PhylomeDBiQ8K2J0.
TreeFamiTF313216.

Enzyme and pathway databases

ReactomeiR-MMU-1855204. Synthesis of IP3 and IP4 in the cytosol.

Miscellaneous databases

PROiQ8K2J0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020937.
CleanExiMM_PLCD3.
ExpressionAtlasiQ8K2J0. baseline and differential.
GenevisibleiQ8K2J0. MM.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001192. PI-PLC_fam.
IPR028406. PLC-delta3.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF33. PTHR10336:SF33. 1 hit.
PfamiPF00168. C2. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPLCD3_MOUSE
AccessioniPrimary (citable) accession number: Q8K2J0
Secondary accession number(s): A2AHR0
, A2AHR1, Q3UME8, Q69Z55, Q8BL19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: November 2, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.