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Q5RET0 (PLCD4_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 57. 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
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length762 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 upregulates 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 – 7627621-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
PRO_0000306828

Regions

Domain16 – 124109PH
Domain134 – 16936EF-hand 1
Domain170 – 20536EF-hand 2
Domain203 – 23735EF-hand 3
Domain290 – 435146PI-PLC X-box
Domain493 – 609117PI-PLC Y-box
Domain614 – 719106C2
Calcium binding147 – 158121 Potential
Calcium binding183 – 194122 Potential
Region26 – 5328Substrate binding By similarity
Motif731 – 7344PDZ-binding
Compositional bias440 – 47334Glu-rich
Compositional bias479 – 4868Poly-Lys

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 binding6501Calcium 2; via carbonyl oxygen By similarity
Metal binding6521Calcium 2 By similarity
Metal binding6761Calcium 2 By similarity
Metal binding7051Calcium 3 By similarity
Metal binding7061Calcium 3; via carbonyl oxygen By similarity
Metal binding7071Calcium 3 By similarity
Binding site4331Substrate By similarity
Binding site4351Substrate By similarity
Binding site5221Substrate By similarity
Binding site5491Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RET0 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 89B03949861987C2

FASTA76287,625
        10         20         30         40         50         60 
MASLLQDQLT TDQDLLLMQE GMPMRKVRSK SWKKLRYFRL QNDGMTVWHA RQARGSAKPS 

        70         80         90        100        110        120 
FSISDVDTIR NGHDSELLRS LAEELPLEQG FTVVFHGRRS NLDLVANSVE EAQMWMRGLQ 

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

       190        200        210        220        230        240 
AADTSQSGTL EGEEFVQFYK ALTKRAEVQE LFESFSADGQ KLTLLEFLDF LREEQKERDC 

       250        260        270        280        290        300 
TSELALELID HYEPSDSGKL 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 
PSPEELRRRI LVKGKKLTLE EDLEYEEEEA EPELEESELA LESQFETEPE PQEQNLQSKD 

       490        500        510        520        530        540 
KKKKSKPILC PALSSLVIYL KSVSFRSFTH SKEHYHFYEI SSFSETKAER LIKEAGNEFV 

       550        560        570        580        590        600 
QHNTWQLSRV YPSGLRTDSS NYNPQELWNA GCQMVAMNMQ TAGLEMDICD GHFRQNGGCG 

       610        620        630        640        650        660 
YVLKPDFLRD IQSSFHPERP ISPFKAQTLL IQVISGQQLP KVDKTKEGSI VDPLVKVQIF 

       670        680        690        700        710        720 
GVRLDTARQE TNYVENNGFN PYWGETLCFR VLVPELAMLR FVVMDYDWKS RNDFIGQYTL 

       730        740        750        760 
PWTCMQQGYR HIHLLSKVGI SLRPASIFVY ICIQEDLEGD ES

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR857436 mRNA. Translation: CAH89727.1.
RefSeqNP_001124787.1. NM_001131315.1.
UniGenePab.12236.

3D structure databases

HSSPHSSP built from PDB template 1QAS based on UniProtKB P10688.
ProteinModelPortalQ5RET0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100171640.
KEGGpon:100171640.

Organism-specific databases

CTD84812.

Phylogenomic databases

HOVERGENHBG053610.

Family and domain databases

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.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca-bd.
IPR011993. PH_type.
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]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 2 hits.
G3DSA:2.30.29.30. PH_type. 1 hit.
G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 2 hits.
KOK05857.
PfamPF00168. C2. 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_PONAB
AccessionPrimary (citable) accession number: Q5RET0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 21, 2004
Last modified: November 16, 2011
This is version 57 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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