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P10688 (PLCD1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-1

EC=3.1.4.11
Alternative name(s):
Phosphoinositide phospholipase C-delta-1
Phospholipase C-III
Short name=PLC-III
Phospholipase C-delta-1
Short name=PLC-delta-1
Gene names
Name:Plcd1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length756 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Essential for trophoblast and placental development.

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.

Sequence similarities

Contains 1 C2 domain.

Contains 2 EF-hand domains.

Contains 1 PH domain.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Transducer
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 8663582. Source: RGD

cytosolic calcium ion homeostasis

Inferred from mutant phenotype PubMed 21767260. Source: RGD

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway

Inferred from mutant phenotype PubMed 16709602. Source: RGD

positive regulation of inositol trisphosphate biosynthetic process

Inferred from mutant phenotype PubMed 16709602. Source: RGD

positive regulation of norepinephrine secretion

Inferred from mutant phenotype PubMed 10473563. Source: RGD

regulation of phospholipase C activity

Inferred from mutant phenotype PubMed 21767260. Source: RGD

response to aluminum ion

Inferred from expression pattern PubMed 10814511. Source: RGD

response to calcium ion

Inferred from mutant phenotype PubMed 10473563. Source: RGD

response to hyperoxia

Inferred from expression pattern PubMed 12850505. Source: RGD

response to organonitrogen compound

Inferred from expression pattern PubMed 12850505. Source: RGD

response to peptide hormone

Inferred from mutant phenotype PubMed 16709602. Source: RGD

response to prostaglandin F

Inferred from expression pattern PubMed 11517196. Source: RGD

   Cellular_componentcytosol

Inferred from direct assay PubMed 16709602. Source: RGD

membrane

Inferred from direct assay PubMed 16709602. Source: RGD

membrane raft

Inferred from direct assay PubMed 18157946. Source: RGD

mitochondrial membrane

Inferred from direct assay PubMed 15107298. Source: RGD

nucleus

Inferred from direct assay PubMed 16115628. Source: RGD

   Molecular_functioncalcium ion binding

Inferred from direct assay PubMed 9538021. Source: RGD

phosphatidylinositol phospholipase C activity

Inferred from direct assay PubMed 9287165. Source: RGD

phosphatidylinositol-4,5-bisphosphate binding

Inferred from direct assay PubMed 9804818. Source: RGD

phospholipid binding

Inferred from direct assay PubMed 15755258. Source: RGD

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7567561-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1
PRO_0000088506

Regions

Domain21 – 130110PH
Domain140 – 17536EF-hand 1
Domain176 – 21136EF-hand 2
Domain296 – 440145PI-PLC X-box
Domain492 – 609118PI-PLC Y-box
Domain630 – 72091C2
Calcium binding153 – 164121 Potential
Calcium binding189 – 200122 Potential
Region30 – 5728Substrate binding

Sites

Active site3111
Active site3561
Metal binding3121Calcium 1; catalytic
Metal binding3411Calcium 1; catalytic
Metal binding3431Calcium 1; catalytic
Metal binding3901Calcium 1; catalytic
Metal binding6511Calcium 2; via carbonyl oxygen
Metal binding6531Calcium 2
Metal binding6771Calcium 2
Metal binding7061Calcium 3
Metal binding7071Calcium 3; via carbonyl oxygen
Metal binding7081Calcium 3
Binding site4381Substrate
Binding site4401Substrate
Binding site5221Substrate
Binding site5491Substrate

Natural variations

Natural variant4121I → M in SHR. Ref.2
Natural variant4231T → S in SHR. Ref.2
Natural variant4631V → D in SHR. Ref.2
Natural variant6681G → A in SHR. Ref.2

Experimental info

Mutagenesis3111H → A: Lowers activity 10000-fold. Ref.5
Mutagenesis3121N → A: Lowers activity 10000-fold. Ref.5
Mutagenesis3201L → A: Lowers activity 3-fold. Ref.5
Mutagenesis3411E → A, H or Q: Lowers activity 200000-fold. Ref.5
Mutagenesis3431D → A: Lowers activity 1000-fold. Ref.5
Mutagenesis3431D → R: Lowers activity 100000-fold. Ref.5
Mutagenesis3561H → A: Lowers activity 1000-fold. Ref.5
Mutagenesis3601F → A: Lowers activity 4-fold. Ref.5
Mutagenesis3901E → A, H or K: Lowers activity 1000-fold. Ref.5
Mutagenesis3901E → Q: Lowers activity 200-fold. Ref.5
Mutagenesis4381K → A: Lowers activity very slightly. Ref.5
Mutagenesis4401K → A: No effect on activity towards phosphatidylinositol 4-monophosphate. Lowers activity 5-fold towards phosphatidylinositol 4,5-bisphosphate. Ref.5
Mutagenesis5221S → A: Lowers activity 10000-fold. Ref.5
Mutagenesis5491R → A: Lowers activity 600-fold. Ref.5
Mutagenesis5511Y → A: Lowers activity 600-fold. Ref.5
Mutagenesis5551W → A: Lowers activity very slightly. Ref.5
Sequence conflict627 – 6293RPE → APK in AAP31521. Ref.2

Secondary structure

............................................................................................................................ 756
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10688 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: E33F2313AC81E9F9

FASTA75685,962
        10         20         30         40         50         60 
MDSGRDFLTL HGLQDDPDLQ ALLKGSQLLK VKSSSWRRER FYKLQEDCKT IWQESRKVMR 

        70         80         90        100        110        120 
SPESQLFSIE DIQEVRMGHR TEGLEKFARD IPEDRCFSIV FKDQRNTLDL IAPSPADAQH 

       130        140        150        160        170        180 
WVQGLRKIIH HSGSMDQRQK LQHWIHSCLR KADKNKDNKM NFKELKDFLK ELNIQVDDGY 

       190        200        210        220        230        240 
ARKIFRECDH SQTDSLEDEE IETFYKMLTQ RAEIDRAFEE AAGSAETLSV ERLVTFLQHQ 

       250        260        270        280        290        300 
QREEEAGPAL ALSLIERYEP SETAKAQRQM TKDGFLMYLL SADGNAFSLA HRRVYQDMDQ 

       310        320        330        340        350        360 
PLSHYLVSSS HNTYLLEDQL TGPSSTEAYI RALCKGCRCL ELDCWDGPNQ EPIIYHGYTF 

       370        380        390        400        410        420 
TSKILFCDVL RAIRDYAFKA SPYPVILSLE NHCSLEQQRV MARHLRAILG PILLDQPLDG 

       430        440        450        460        470        480 
VTTSLPSPEQ LKGKILLKGK KLGGLLPAGG ENGSEATDVS DEVEAAEMED EAVRSQVQHK 

       490        500        510        520        530        540 
PKEDKLKLVP ELSDMIIYCK SVHFGGFSSP GTSGQAFYEM ASFSESRALR LLQESGNGFV 

       550        560        570        580        590        600 
RHNVSCLSRI YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ TPGPEMDVYL GCFQDNGGCG 

       610        620        630        640        650        660 
YVLKPAFLRD PNTTFNSRAL TQGPWWRPER LRVRIISGQQ LPKVNKNKNS IVDPKVIVEI 

       670        680        690        700        710        720 
HGVGRDTGSR QTAVITNNGF NPRWDMEFEF EVTVPDLALV RFMVEDYDSS SKNDFIGQST 

       730        740        750 
IPWNSLKQGY RHVHLLSKNG DQHPSATLFV KISIQD 

« Hide

References

[1]"Cloning and sequence of multiple forms of phospholipase C."
Suh P.-G., Ryu S.H., Moon K.H., Suh H.W., Rhee S.G.
Cell 54:161-169(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Phospholipase C-delta gene of the spontaneously hypertensive rat harbors point mutations causing amino acid substitutions in a catalytic domain."
Yagisawa H., Tanase H., Nojima H.
J. Hypertens. 9:997-1004(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SHR MET-412; SER-423; ASP-463 AND ALA-668.
Tissue: Aorta.
[3]"Putative inositol 1,4,5-trisphosphate binding proteins in rat brain cytosol."
Kanematsu T., Takeya H., Watanabe Y., Ozaki S., Yoshida M., Koga T., Iwanaga S., Hirata M.
J. Biol. Chem. 267:6518-6525(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 50-57; 128-140 AND 728-738.
Tissue: Brain.
[4]Lubec G., Diao W.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 61-76, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
[5]"Catalytic domain of phosphoinositide-specific phospholipase C (PLC). Mutational analysis of residues within the active site and hydrophobic ridge of plcdelta1."
Ellis M.V., James S.R., Perisic O., Downes C.P., Williams R.L., Katan M.
J. Biol. Chem. 273:11650-11659(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-311; ASN-312; LEU-320; GLU-341; ASP-343; HIS-356; PHE-360; GLU-390; LYS-438; LYS-440; SER-522; ARG-549; TYR-551 AND TRP-555.
[6]"Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain."
Ferguson K.M., Lemmon M.A., Schlessinger J., Sigler P.B.
Cell 83:1037-1046(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-130.
[7]"C2 domain conformational changes in phospholipase C-delta 1."
Grobler J.A., Essen L.-O., Williams R.L., Hurley J.H.
Nat. Struct. Biol. 3:788-795(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 205-756.
[8]"Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta."
Essen L.-O., Perisic O., Cheung R., Katan M., Williams R.L.
Nature 380:595-602(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 133-756.
[9]"A ternary metal binding site in the C2 domain of phosphoinositide-specific phospholipase C-delta1."
Essen L.-O., Perisic O., Lynch D.E., Katan M., Williams R.L.
Biochemistry 36:2753-2762(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 133-756, CALCIUM-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20637 mRNA. Translation: AAA41886.1.
S74591 mRNA. Translation: AAP31521.1.
PIRB28821.
RefSeqNP_058731.1. NM_017035.1.
UniGeneRn.12324.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DJGX-ray2.60A/B133-756[»]
1DJHX-ray2.50A/B133-756[»]
1DJIX-ray2.50A/B133-756[»]
1DJWX-ray2.45A/B133-756[»]
1DJXX-ray2.30A/B133-756[»]
1DJYX-ray2.80A/B133-756[»]
1DJZX-ray2.95A/B133-756[»]
1MAIX-ray1.90A11-140[»]
1QASX-ray2.40A/B135-756[»]
1QATX-ray3.00A/B135-756[»]
2ISDX-ray2.50A/B133-756[»]
DisProtDP00055.
ProteinModelPortalP10688.
SMRP10688. Positions 12-130, 158-756.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246790. 1 interaction.
MINTMINT-245440.

Chemistry

BindingDBP10688.
ChEMBLCHEMBL1914273.

PTM databases

PhosphoSiteP10688.

Proteomic databases

PaxDbP10688.
PRIDEP10688.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24655.
KEGGrno:24655.
UCSCRGD:3346. rat.

Organism-specific databases

CTD5333.
RGD3346. Plcd1.

Phylogenomic databases

eggNOGNOG149692.
HOGENOMHOG000006871.
HOVERGENHBG053610.
InParanoidP10688.
KOK05857.
PhylomeDBP10688.

Enzyme and pathway databases

BRENDA3.1.4.11. 5301.

Gene expression databases

GenevestigatorP10688.

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.
IPR028391. PLC-delta1.
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:SF30. PTHR10336:SF30. 1 hit.
PfamPF00168. C2. 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]
PRINTSPR00390. PHPHLIPASEC.
SMARTSM00239. C2. 1 hit.
SM00054. EFh. 2 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. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10688.
NextBio603990.
PROP10688.

Entry information

Entry namePLCD1_RAT
AccessionPrimary (citable) accession number: P10688
Secondary accession number(s): Q80WI4 expand/collapse secondary AC list , Q9QVD3, Q9QVD4, Q9QVD5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 150 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references