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Q4R6L3 (PLCD4_MACFA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:PLCD4
ORF Names:QtsA-17742
OrganismMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca

Protein attributes

Sequence length799 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

Binds 3 calcium ions per subunit. Two of the calcium ions are bound to the C2 domain By similarity.

Subunit structure

Interacts with GRIP1 By similarity.

Subcellular location

Membrane; Peripheral membrane protein By similarity. Nucleus By similarity. Cytoplasm By similarity. Endoplasmic reticulum By similarity. Note: Localizes primarily to intracellular membranes mostly to the endoplasmic reticulum By similarity.

Domain

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 similarities

Contains 1 C2 domain.

Contains 3 EF-hand domains.

Contains 1 PH domain.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7997991-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4
PRO_0000306825

Regions

Domain16 – 124109PH
Domain134 – 16936EF-hand 1
Domain170 – 20536EF-hand 2
Domain203 – 23735EF-hand 3
Domain290 – 435146PI-PLC X-box
Domain530 – 646117PI-PLC Y-box
Domain651 – 756106C2
Calcium binding147 – 158121 Potential
Calcium binding183 – 194122 Potential
Region26 – 5328Substrate binding By similarity
Motif768 – 7714PDZ-binding
Compositional bias440 – 47839Glu-rich

Sites

Active site3051 By similarity
Active site3501 By similarity
Metal binding3061Calcium 1; catalytic By similarity
Metal binding3351Calcium 1; catalytic By similarity
Metal binding3371Calcium 1; catalytic By similarity
Metal binding3841Calcium 1; catalytic By similarity
Metal binding6871Calcium 2; via carbonyl oxygen By similarity
Metal binding6891Calcium 2 By similarity
Metal binding7131Calcium 2 By similarity
Metal binding7421Calcium 3 By similarity
Metal binding7431Calcium 3; via carbonyl oxygen By similarity
Metal binding7441Calcium 3 By similarity
Binding site4331Substrate By similarity
Binding site4351Substrate By similarity
Binding site5591Substrate By similarity
Binding site5861Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4R6L3 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: FE30A582F5FB7FAF

FASTA79991,437
        10         20         30         40         50         60 
MASLLQDRLT TDQDLLLMQE GMPMRKVRSK SWKKLRYFRL QNDGMTVWHA RQARGSAKPS 

        70         80         90        100        110        120 
FSISDVETIR NGHDSELLRS LTEELPLEQG FTVVFHGRRS NLDLVANSVE EAQIWMRGLH 

       130        140        150        160        170        180 
LLVDLVTSMD HQERLDQWLS DWFQRGDKNQ DGKMSFQEVQ RLLHLMNVEM DQEYAFSLFQ 

       190        200        210        220        230        240 
AADTSQSGTL EGEEFVEFYK ALTKRAEVQE LFESFSADGQ KLTLLEFSDF LREEQKERDC 

       250        260        270        280        290        300 
TSELALELID RYEPSDSGKL RHVLSMDGFL SYLCSKDGDI FNPACLPIYQ DMTQPLNHYF 

       310        320        330        340        350        360 
ICSSHNTYLV GDQLCGQSSV EGYIRALKRG CRCVEVDVWD GPSGEPVVYH GHTLTSRILF 

       370        380        390        400        410        420 
KDVVATVAQY AFQTSDYPVI LSLETHCSWE QQQTMARHLT EILGEQLLST TLDGVLPTQL 

       430        440        450        460        470        480 
PSPEELRRKI LVKGKKLTLE EDLEYEEEEV EPGLEGEHES ELALESQFET ESEPEPQEQN 

       490        500        510        520        530        540 
LQIKDKKKVV TCPLFCPSIC CQIVAQAPIS KPGSLLLSQQ KSKTILCPAL SSLVIYLKSV 

       550        560        570        580        590        600 
SFRSFTHSKK HYHFYEISSF SETKAKRLIK EAGNEFVQHN TWQLSRVYPS GLRTDSSNYN 

       610        620        630        640        650        660 
PQELWNAGCQ MVAMNMQTAG LEMDICDGHF RQNGGCGYVL KPDFLRDNQS SFHPERPISP 

       670        680        690        700        710        720 
FKAQTLLIQV ISGQQLPKLN KTKEGSIVDP LVKVQIFGVR LDTARQETNY VENNGFNPYW 

       730        740        750        760        770        780 
GQTLCFRVLV PELAMLRFVV MDYDWKSRND FIGQYTLPWS CMQQGYRHIH LLSKDGISLC 

       790 
PASIFVYICI REGLEGDES

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References

[1]"DNA sequences of macaque genes expressed in brain or testis and its evolutionary implications."
International consortium for macaque cDNA sequencing and analysis
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB169170 mRNA. Translation: BAE01262.1.

3D structure databases

HSSPHSSP built from PDB template 1QAS based on UniProtKB P10688.
ProteinModelPortalQ4R6L3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG053610.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
2.30.29.30. 1 hit.
3.20.20.190. 2 hits.
InterProIPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR011993. PH_like_dom.
IPR001192. Pinositol_PLipase_C.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR001849. Pleckstrin_homology.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERPTHR10336. PTHR10336. 1 hit.
PfamPF00168. C2. 1 hit.
PF13202. EF_hand_3. 1 hit.
PF09279. efhand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSPR00390. PHPHLIPASEC.
SMARTSM00239. C2. 1 hit.
SM00054. EFh. 3 hits.
SM00233. PH. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 1 hit.
SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.
PROSITEPS50004. 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]
ProtoNetSearch...

Entry information

Entry namePLCD4_MACFA
AccessionPrimary (citable) accession number: Q4R6L3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: July 19, 2005
Last modified: May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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