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Q9BRC7 (PLCD4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4

Short name=hPLCD4
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length762 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.1

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. Endoplasmic reticulum By similarity. Note: Localizes primarily to intracellular membranes mostly to the endoplasmic reticulum. Ref.1

Tissue specificity

Highly expressed in skeletal muscle and kidney tissues, and at moderate level in intestinal tissue. Expressed in corneal epithelial cells. Ref.1 Ref.5

Domain

The PDZ-binding motif mediates the interaction with GRIP1.

The C2 domain mediates pre-localization to the membrane prior to Ca2+ import and non-selective Ca2+-mediated targeting to various cellular membranes.

The PH domain is not a critical determinant of the membrane localization.

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BRC7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Acceptor splice site between exons 4 and 5 is non-canonical but conserved through species for that particular gene.
Isoform 2 (identifier: Q9BRC7-2)

Also known as: PLCD4b;

The sequence of this isoform differs from the canonical sequence as follows:
     259-272: KLRHVLSMDGFLSY → ASEEDPGEGEEVNT
     273-762: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7627621-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4
PRO_0000306824

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

Natural variations

Alternative sequence259 – 27214KLRHV…GFLSY → ASEEDPGEGEEVNT in isoform 2.
VSP_028501
Alternative sequence273 – 762490Missing in isoform 2.
VSP_028502

Experimental info

Sequence conflict981R → H in BAD96923. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 5444BE5CE2AEA3EF

FASTA76287,585
        10         20         30         40         50         60 
MASLLQDQLT TDQDLLLMQE GMPMRKVRSK SWKKLRYFRL QNDGMTVWHA RQARGSAKPS 

        70         80         90        100        110        120 
FSISDVETIR NGHDSELLRS LAEELPLEQG FTIVFHGRRS NLDLMANSVE EAQIWMRGLQ 

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

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

       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 EDLEYEEEEA EPELEESELA LESQFETEPE PQEQNLQNKD 

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

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

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

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

       730        740        750        760 
PWTCMQQGYR HIHLLSKDGI SLRPASIFVY ICIQEGLEGD ES 

« Hide

Isoform 2 (PLCD4b) [UniParc].

Checksum: C3A83C9C8E411D88
Show »

FASTA27231,448

References

« Hide 'large scale' references
[1]"Phospholipase C delta-4 overexpression upregulates ErbB1/2 expression, Erk signaling pathway, and proliferation in MCF-7 cells."
Leung D.W., Tompkins C., Brewer J., Ball A., Coon M., Morris V., Waggoner D., Singer J.W.
Mol. Cancer 3:15-15(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Kidney proximal tubule.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Assignment of the human PLC delta4 gene (PLCD4) to human chromosome band 2q35 by fluorescence in situ hybridization."
Kim H., Suh P.-G., Ryu S.H., Park S.H.
Cytogenet. Cell Genet. 87:254-255(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[5]"Expression of phospholipases A2 and C in human corneal epithelial cells."
Landreville S., Coulombe S., Carrier P., Gelb M.H., Guerin S.L., Salesse C.
Invest. Ophthalmol. Vis. Sci. 45:3997-4003(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY512961 mRNA. Translation: AAS82574.1.
AK223203 mRNA. Translation: BAD96923.1.
BC006355 mRNA. Translation: AAH06355.1.
CCDSCCDS46516.1. [Q9BRC7-1]
RefSeqNP_116115.1. NM_032726.3. [Q9BRC7-1]
UniGeneHs.632528.

3D structure databases

ProteinModelPortalQ9BRC7.
SMRQ9BRC7. Positions 9-123, 149-755.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124273. 3 interactions.
IntActQ9BRC7. 2 interactions.
MINTMINT-1482361.
STRING9606.ENSP00000388631.

PTM databases

PhosphoSiteQ9BRC7.

Polymorphism databases

DMDM74732863.

Proteomic databases

PaxDbQ9BRC7.
PRIDEQ9BRC7.

Protocols and materials databases

DNASU84812.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000417849; ENSP00000396942; ENSG00000115556. [Q9BRC7-1]
ENST00000450993; ENSP00000388631; ENSG00000115556. [Q9BRC7-1]
GeneID84812.
KEGGhsa:84812.
UCSCuc021vwx.1. human. [Q9BRC7-1]

Organism-specific databases

CTD84812.
GeneCardsGC02P219436.
H-InvDBHIX0002832.
HIX0030357.
HGNCHGNC:9062. PLCD4.
HPACAB009914.
MIM605939. gene.
neXtProtNX_Q9BRC7.
PharmGKBPA33390.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG149692.
HOGENOMHOG000006871.
HOVERGENHBG053610.
InParanoidQ9BRC7.
KOK05857.
OrthoDBEOG7V49XT.
PhylomeDBQ9BRC7.
TreeFamTF313216.

Gene expression databases

ArrayExpressQ9BRC7.
BgeeQ9BRC7.
CleanExHS_PLCD4.
GenevestigatorQ9BRC7.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR028387. PLC-delta4.
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.
PTHR10336:SF31. PTHR10336:SF31. 1 hit.
PfamPF00168. C2. 1 hit.
PF09279. EF-hand_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. SSF49562. 1 hit.
SSF51695. SSF51695. 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...

Other

ChiTaRSPLCD4. human.
GeneWikiPLCD4.
GenomeRNAi84812.
NextBio74997.
PROQ9BRC7.
SOURCESearch...

Entry information

Entry namePLCD4_HUMAN
AccessionPrimary (citable) accession number: Q9BRC7
Secondary accession number(s): Q53FS8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM