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Q8N3E9 (PLCD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PLCD3
Synonyms:KIAA1964
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length789 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. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow.

Catalytic activity

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. Ref.9

Cofactor

Binds 3 calcium ions per subunit. Two of the calcium ions are bound to the C2 domain Probable. Ref.7

Enzyme regulation

Strongly activated by phosphatidic acid. Inhibited by phosphatidylethanolamine (PtdEtn), phosphatidylcholine (PtdCho), sphingomyelin and phosphatidylserine (PtdSer). Ref.7 Ref.9

Subcellular location

Membrane; Peripheral membrane protein. Cytoplasm. Cleavage furrow. Note: Localizes at the cleavage furrow during cytokinesis. Ref.7 Ref.13

Tissue specificity

Present in corneal epithelial cells (at protein level). Ref.12

Induction

Down-regulated by Ca2+ and cAMP. Ref.7 Ref.9 Ref.10

Domain

The C2 domain is a Ca2+-dependent membrane-targeting module. Ref.9 Ref.11

The PH domain mediates interaction with the surface membrane by binding to PIP2. Ref.9 Ref.11

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.

Biophysicochemical properties

Kinetic parameters:

KM=105.3 µM for PIP2 Ref.9

Vmax=28.5 µmol/min/mg enzyme

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7897891-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3
PRO_0000306821

Regions

Domain63 – 172110PH
Domain182 – 21736EF-hand 1
Domain218 – 25336EF-hand 2
Domain250 – 28536EF-hand 3
Domain337 – 482146PI-PLC X-box
Domain528 – 644117PI-PLC Y-box
Domain647 – 752106C2
Calcium binding195 – 206121 Potential
Calcium binding231 – 242122 Potential
Region73 – 10129Substrate binding By similarity

Sites

Active site3521 By similarity
Active site3971 By similarity
Metal binding3531Calcium 1; catalytic By similarity
Metal binding3821Calcium 1; catalytic By similarity
Metal binding3841Calcium 1; catalytic By similarity
Metal binding4311Calcium 1; catalytic By similarity
Metal binding6831Calcium 2; via carbonyl oxygen By similarity
Metal binding6851Calcium 2 By similarity
Metal binding7091Calcium 2 By similarity
Metal binding7381Calcium 3 By similarity
Metal binding7391Calcium 3; via carbonyl oxygen By similarity
Metal binding7401Calcium 3 By similarity
Binding site4801Substrate By similarity
Binding site4821Substrate By similarity
Binding site5571Substrate By similarity
Binding site5841Substrate By similarity

Amino acid modifications

Modified residue1051Phosphoserine Ref.15
Modified residue4961Phosphoserine By similarity

Natural variations

Natural variant6521P → L.
Corresponds to variant rs734921 [ dbSNP | Ensembl ].
VAR_035316

Experimental info

Sequence conflict2071I → T in CAD39054. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8N3E9 [UniParc].

Last modified October 2, 2007. Version 3.
Checksum: C6901404D2C9D070

FASTA78989,258
        10         20         30         40         50         60 
MLCGRWRRCR RPPEEPPVAA QVAAQVAAPV ALPSPPTPSD GGTKRPGLRA LKKMGLTEDE 

        70         80         90        100        110        120 
DVRAMLRGSR LRKIRSRTWH KERLYRLQED GLSVWFQRRI PRAPSQHIFF VQHIEAVREG 

       130        140        150        160        170        180 
HQSEGLRRFG GAFAPARCLT IAFKGRRKNL DLAAPTAEEA QRWVRGLTKL RARLDAMSQR 

       190        200        210        220        230        240 
ERLDHWIHSY LHRADSNQDS KMSFKEIKSL LRMVNVDMND MYAYLLFKEC DHSNNDRLEG 

       250        260        270        280        290        300 
AEIEEFLRRL LKRPELEEIF HQYSGEDRVL SAPELLEFLE DQGEEGATLA RAQQLIQTYE 

       310        320        330        340        350        360 
LNETAKQHEL MTLDGFMMYL LSPEGAALDN THTCVFQDMN QPLAHYFISS SHNTYLTDSQ 

       370        380        390        400        410        420 
IGGPSSTEAY VRAFAQGCRC VELDCWEGPG GEPVIYHGHT LTSKILFRDV VQAVRDHAFT 

       430        440        450        460        470        480 
LSPYPVILSL ENHCGLEQQA AMARHLCTIL GDMLVTQALD SPNPEELPSP EQLKGRVLVK 

       490        500        510        520        530        540 
GKKLPAARSE DGRALSDREE EEEDDEEEEE EVEAAAQRRL AKQISPELSA LAVYCHATRL 

       550        560        570        580        590        600 
RTLHPAPNAP QPCQVSSLSE RKAKKLIREA GNSFVRHNAR QLTRVYPLGL RMNSANYSPQ 

       610        620        630        640        650        660 
EMWNSGCQLV ALNFQTPGYE MDLNAGRFLV NGQCGYVLKP ACLRQPDSTF DPEYPGPPRT 

       670        680        690        700        710        720 
TLSIQVLTAQ QLPKLNAEKP HSIVDPLVRI EIHGVPADCA RQETDYVLNN GFNPRWGQTL 

       730        740        750        760        770        780 
QFQLRAPELA LVRFVVEDYD ATSPNDFVGQ FTLPLSSLKQ GYRHIHLLSK DGASLSPATL 


FIQIRIQRS 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]"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].
Tissue: Colon and Pancreas.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-789.
Tissue: Amygdala.
[4]"Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins."
Nagase T., Kikuno R., Ohara O.
DNA Res. 8:319-327(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-789.
Tissue: Brain.
[5]"Expression, purification and kinetic properties of human recombinant phospholipase C delta 3."
Pawelczyk T., Matecki A.
Acta Biochim. Pol. 44:221-229(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PURIFICATION.
[6]"Phospholipase C isoforms delta 1 and delta 3 from human fibroblasts. High-yield expression in Escherichia coli, simple purification, and properties."
Ghosh S., Pawelczyk T., Lowenstein J.M.
Protein Expr. Purif. 9:262-278(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PURIFICATION.
[7]"Localization of phospholipase C delta3 in the cell and regulation of its activity by phospholipids and calcium."
Pawelczyk T., Matecki A.
Eur. J. Biochem. 257:169-177(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, COFACTOR, ENZYME REGULATION.
[8]"Assignment of the human PLC delta3 gene (PLCD3) to human chromosome band 17q21 by fluorescence in situ hybridization."
Kim H., Suh P.-G., Ryu S.H., Park S.H.
Cytogenet. Cell Genet. 87:209-210(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[9]"Phospholipase C-delta3 binds with high specificity to phosphatidylinositol 4,5-bisphosphate and phosphatidic acid in bilayer membranes."
Pawelczyk T., Matecki A.
Eur. J. Biochem. 262:291-298(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, DOMAIN PH.
[10]"Downregulation of phospholipase C delta3 by cAMP and calcium."
Lin F.-G., Cheng H.-F., Lee I.-F., Kao H.-J., Loh S.-H., Lee W.-H.
Biochem. Biophys. Res. Commun. 286:274-280(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[11]"Membrane targeting of C2 domains of phospholipase C-delta isoforms."
Ananthanarayanan B., Das S., Rhee S.-G., Murray D., Cho W.
J. Biol. Chem. 277:3568-3575(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN C2.
[12]"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.
[13]"Phospholipase C isoforms are localized at the cleavage furrow during cytokinesis."
Naito Y., Okada M., Yagisawa H.
J. Biochem. 140:785-791(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK074240 mRNA. Translation: BAB85029.1.
BC010668 mRNA. Translation: AAH10668.2.
BC072384 mRNA. Translation: AAH72384.1.
AL834392 mRNA. Translation: CAD39054.2.
AB075844 mRNA. Translation: BAB85550.1.
RefSeqNP_588614.1. NM_133373.4.
UniGeneHs.380094.

3D structure databases

ProteinModelPortalQ8N3E9.
SMRQ8N3E9. Positions 55-788.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125222. 2 interactions.
IntActQ8N3E9. 1 interaction.
MINTMINT-1193970.
STRING9606.ENSP00000313731.

Chemistry

DrugBankDB00144. Phosphatidylserine.

Polymorphism databases

DMDM158706388.

Proteomic databases

PaxDbQ8N3E9.
PeptideAtlasQ8N3E9.
PRIDEQ8N3E9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322765; ENSP00000313731; ENSG00000161714.
GeneID113026.
KEGGhsa:113026.
UCSCuc002iib.3. human.

Organism-specific databases

CTD113026.
GeneCardsGC17M043197.
HGNCHGNC:9061. PLCD3.
HPAHPA025711.
HPA053665.
MIM608795. gene.
neXtProtNX_Q8N3E9.
PharmGKBPA33389.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG149692.
HOGENOMHOG000006871.
HOVERGENHBG053610.
InParanoidQ8N3E9.
KOK05857.
OrthoDBEOG7V49XT.
PhylomeDBQ8N3E9.
TreeFamTF313216.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ8N3E9.
BgeeQ8N3E9.
CleanExHS_PLCD3.
GenevestigatorQ8N3E9.

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.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR028406. PLC-delta3.
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:SF33. PTHR10336:SF33. 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.
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. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLCD3. human.
GeneWikiPLCD3.
GenomeRNAi113026.
NextBio78735.
PROQ8N3E9.
SOURCESearch...

Entry information

Entry namePLCD3_HUMAN
AccessionPrimary (citable) accession number: Q8N3E9
Secondary accession number(s): Q8TEC1, Q8TF37, Q96FL6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: April 16, 2014
This is version 118 of the entry and version 3 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM