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Protein

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

Gene

PLCD4

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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. Required for acrosome reaction in sperm during fertilization, probably by acting as an important enzyme for intracellular Ca2+ mobilization in the zona pellucida-induced acrosome reaction. May play a role in cell growth. Modulates the liver regeneration in cooperation with nuclear PKC. Overexpression up-regulates the Erk signaling pathway and proliferation (By similarity).By similarity

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei305PROSITE-ProRule annotation1
Metal bindingi306Calcium 1; catalyticBy similarity1
Metal bindingi335Calcium 1; catalyticBy similarity1
Metal bindingi337Calcium 1; catalyticBy similarity1
Active sitei350PROSITE-ProRule annotation1
Metal bindingi384Calcium 1; catalyticBy similarity1
Binding sitei433SubstrateBy similarity1
Binding sitei435SubstrateBy similarity1
Binding sitei559SubstrateBy similarity1
Binding sitei586SubstrateBy similarity1
Metal bindingi687Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi689Calcium 2By similarity1
Metal bindingi713Calcium 2By similarity1
Metal bindingi742Calcium 3By similarity1
Metal bindingi743Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi744Calcium 3By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi147 – 1581PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi183 – 1942PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 (EC:3.1.4.11)
Alternative name(s):
Phosphoinositide phospholipase C-delta-4
Phospholipase C-delta-4
Short name:
PLC-delta-4
Gene namesi
Name:PLCD4
ORF Names:QtsA-17742
OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifieri9541 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003068251 – 7991-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4Add BLAST799

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei460PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Interacts with GRIP1.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ4R6L3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 124PHPROSITE-ProRule annotationAdd BLAST109
Domaini134 – 169EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini170 – 205EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini203 – 237EF-hand 3PROSITE-ProRule annotationAdd BLAST35
Domaini290 – 435PI-PLC X-boxPROSITE-ProRule annotationAdd BLAST146
Domaini530 – 646PI-PLC Y-boxPROSITE-ProRule annotationAdd BLAST117
Domaini651 – 756C2PROSITE-ProRule annotationAdd BLAST106

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni26 – 53Substrate bindingBy similarityAdd BLAST28

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi768 – 771PDZ-binding4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi440 – 478Glu-richAdd BLAST39

Domaini

The PDZ-binding motif mediates the interaction with GRIP1.By similarity
The C2 domain mediates pre-localization to the membrane prior to Ca2+ import and non-selective Ca2+-mediated targeting to various cellular membranes.By similarity
The PH domain is not a critical determinant of the membrane localization.By similarity

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 3 EF-hand domains.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
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

HOVERGENiHBG053610.
KOiK05857.

Family and domain databases

CDDicd00051. EFh. 1 hit.
Gene3Di1.10.238.10. 3 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.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001192. PI-PLC_fam.
IPR028387. PLC-delta4.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLC_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF31. PTHR10336:SF31. 1 hit.
PfamiPF00168. C2. 1 hit.
PF13202. EF-hand_5. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00169. PH. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00054. EFh. 3 hits.
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. 2 hits.
PROSITEiPS50004. C2. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS50003. PH_DOMAIN. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4R6L3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLLQDRLT TDQDLLLMQE GMPMRKVRSK SWKKLRYFRL QNDGMTVWHA
60 70 80 90 100
RQARGSAKPS FSISDVETIR NGHDSELLRS LTEELPLEQG FTVVFHGRRS
110 120 130 140 150
NLDLVANSVE EAQIWMRGLH LLVDLVTSMD HQERLDQWLS DWFQRGDKNQ
160 170 180 190 200
DGKMSFQEVQ RLLHLMNVEM DQEYAFSLFQ AADTSQSGTL EGEEFVEFYK
210 220 230 240 250
ALTKRAEVQE LFESFSADGQ KLTLLEFSDF LREEQKERDC TSELALELID
260 270 280 290 300
RYEPSDSGKL RHVLSMDGFL SYLCSKDGDI FNPACLPIYQ DMTQPLNHYF
310 320 330 340 350
ICSSHNTYLV GDQLCGQSSV EGYIRALKRG CRCVEVDVWD GPSGEPVVYH
360 370 380 390 400
GHTLTSRILF KDVVATVAQY AFQTSDYPVI LSLETHCSWE QQQTMARHLT
410 420 430 440 450
EILGEQLLST TLDGVLPTQL PSPEELRRKI LVKGKKLTLE EDLEYEEEEV
460 470 480 490 500
EPGLEGEHES ELALESQFET ESEPEPQEQN LQIKDKKKVV TCPLFCPSIC
510 520 530 540 550
CQIVAQAPIS KPGSLLLSQQ KSKTILCPAL SSLVIYLKSV SFRSFTHSKK
560 570 580 590 600
HYHFYEISSF SETKAKRLIK EAGNEFVQHN TWQLSRVYPS GLRTDSSNYN
610 620 630 640 650
PQELWNAGCQ MVAMNMQTAG LEMDICDGHF RQNGGCGYVL KPDFLRDNQS
660 670 680 690 700
SFHPERPISP FKAQTLLIQV ISGQQLPKLN KTKEGSIVDP LVKVQIFGVR
710 720 730 740 750
LDTARQETNY VENNGFNPYW GQTLCFRVLV PELAMLRFVV MDYDWKSRND
760 770 780 790
FIGQYTLPWS CMQQGYRHIH LLSKDGISLC PASIFVYICI REGLEGDES
Length:799
Mass (Da):91,437
Last modified:July 19, 2005 - v1
Checksum:iFE30A582F5FB7FAF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB169170 mRNA. Translation: BAE01262.1.
RefSeqiNP_001306482.1. NM_001319553.1.
UniGeneiMfa.3769.

Genome annotation databases

GeneIDi102122144.
KEGGimcf:102122144.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB169170 mRNA. Translation: BAE01262.1.
RefSeqiNP_001306482.1. NM_001319553.1.
UniGeneiMfa.3769.

3D structure databases

ProteinModelPortaliQ4R6L3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102122144.
KEGGimcf:102122144.

Organism-specific databases

CTDi84812.

Phylogenomic databases

HOVERGENiHBG053610.
KOiK05857.

Family and domain databases

CDDicd00051. EFh. 1 hit.
Gene3Di1.10.238.10. 3 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.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001192. PI-PLC_fam.
IPR028387. PLC-delta4.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLC_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF31. PTHR10336:SF31. 1 hit.
PfamiPF00168. C2. 1 hit.
PF13202. EF-hand_5. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00169. PH. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00054. EFh. 3 hits.
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. 2 hits.
PROSITEiPS50004. C2. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS50003. PH_DOMAIN. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPLCD4_MACFA
AccessioniPrimary (citable) accession number: Q4R6L3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: July 19, 2005
Last modified: November 30, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. 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.