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Reviewed, UniProtKB/Swiss-Prot Q8SPR7 (PLCD4_PIG)

Last modified October 13, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
      Short name=Phospholipase C-delta-4
      Short name=PLC-delta-4
Gene names
Name: PLCD4
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length772 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7727721-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
PRO_0000306827

Regions

Domain23 – 131109PH
Domain141 – 17636EF-hand 1
Domain177 – 21236EF-hand 2
Domain210 – 24435EF-hand 3
Domain297 – 442146PI-PLC X-box
Domain503 – 619117PI-PLC Y-box
Domain624 – 729106C2
Calcium binding154 – 165121 Potential
Calcium binding190 – 201122 Potential
Region33 – 6028Substrate binding By similarity
Motif741 – 7444PDZ-binding
Compositional bias448 – 48336Glu-rich
Compositional bias489 – 4968Poly-Lys

Sites

Active site3121 By similarity
Active site3571 By similarity
Metal binding3131Calcium 1; catalytic By similarity
Metal binding3421Calcium 1; catalytic By similarity
Metal binding3441Calcium 1; catalytic By similarity
Metal binding3911Calcium 1; catalytic By similarity
Metal binding6601Calcium 2; via carbonyl oxygen By similarity
Metal binding6621Calcium 2 By similarity
Metal binding6861Calcium 2 By similarity
Metal binding7151Calcium 3 By similarity
Metal binding7161Calcium 3; via carbonyl oxygen By similarity
Metal binding7171Calcium 3 By similarity
Binding site4401Substrate By similarity
Binding site4421Substrate By similarity
Binding site5321Substrate By similarity
Binding site5591Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q8SPR7-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 86E5706A74247548

FASTA77288,075
        10         20         30         40         50         60 
MASLLQGLSA SPGSGLPINQ DLLLMQKGML MRKVRSKSWK KLRYYRLQDD GMTVWHARQA 

        70         80         90        100        110        120 
GGRAKPSFSI SDVETVRGGH ESELLRNLAE EFPLEQGFTI VFHGRRSNLD LVANSVEEAQ 

       130        140        150        160        170        180 
VWMQGLQLLV DFVTNMDQQE RLDQWLSDWF QRGDKNQDGR MSFGEVQRLL HLMNVEMDQE 

       190        200        210        220        230        240 
HAFQLFQTAD TSQSGTLEGE EFVEFYKSLT KRAEVQELFE NFSSDGQKLT LLEFVDFLQE 

       250        260        270        280        290        300 
EQKEGERASD LALELIDRHE PSDSGKLRHV LSLDGFLSYL CSKDGDIFNP TCLPIYQDMT 

       310        320        330        340        350        360 
QPLNHYFINS SHNTYLVGDQ LCGQSSVEGY IRALKRGCRC VEVDIWDGPN GEPVVYHGHT 

       370        380        390        400        410        420 
LTSRIPFKDV VAAIAQYAFQ TSDYPVILSL ENHCSWEQQE MIAHHLTEIL GEQLLSTTLD 

       430        440        450        460        470        480 
GQLPTQLPSP EELRRKILVK GKKLRTLEED LEEEEEEPEE SELEGEQEAE LELEAQFESE 

       490        500        510        520        530        540 
PQELSPRSKD KKKKVKAILC PALSALVVYL KAVSFYSFAH SREHYRFYEI SSFSEAKAKS 

       550        560        570        580        590        600 
LIKESGNEFV QHNTWQLSRV YPGGLRTDSS NYNPQEFWNA GCQMVAMNMQ TAGLEMDLCD 

       610        620        630        640        650        660 
GLFRQNAGCG YVLKPDFLRD AQSSFHPERP ISPSKAQTLL IQVISGQQLP KVDDSKEGSI 

       670        680        690        700        710        720 
VDPLVRVEIF GVRPDTARQE TSYVENNGFN PYWGQTLCFR VLVPELALLR FVVKDYDWKS 

       730        740        750        760        770 
RNDFVGQYTL PWNCMQQGYR HIHLLSKDGI SLHPASIFVH ICIREGIEGV ES

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References

[1]Smith T.P.L.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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Cross-references

Sequence databases

AF498759 mRNA. Translation: AAM18122.1.
RefSeqNP_999217.1.
UniGeneSsc.191
Ssc.42249

3D structure databases

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

Genome annotation databases

GeneID397119.
KEGGssc:397119.

Organism-specific databases

CTD397119.

Phylogenomic databases

HOVERGENQ8SPR7.

Enzyme and pathway databases

BRENDA3.1.4.11. 249.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR018029. C2_membr_targeting.
IPR011992. EF-Hand_type.
IPR018247. EF_HAND_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
IPR011993. PH_type.
IPR015359. Phospholipase_C_EF-hand-like.
IPR001192. Phospholipase_C_Pinositol-sp_C.
IPR000909. Phospholipase_C_Pinositol-sp_X.
IPR001711. Phospholipase_C_Pinositol-sp_Y.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR001849. Pleckstrin_homology.
[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. 1 hit.
PfamPF00168. C2. 1 hit.
PF09279. efhand_like. 1 hit.
PF00169. PH. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSPR00390. PHPHLIPASEC.
ProDomPD000012. EF-hand. 1 hit.
PD001202. PI_PLC_Y. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00239. C2. 1 hit.
SM00054. EFh. 3 hits.
SM00233. PH. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
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...

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Entry information

Entry namePLCD4_PIG
AccessionPrimary (citable) accession number: Q8SPR7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2002
Last modified: October 13, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents