Skip Header

Contribute Send feedback
Read comments (?) or add your own

P21671 (PLCD4_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
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-4
EC=3.1.4.11
Alternative name(s):
PLC-85
Phosphoinositide phospholipase C-delta-4
Phospholipase C-delta-2
Short name=PLC-delta-2
Phospholipase C-delta-4
Short name=PLC-delta-4
Gene names
Name:PLCD4
Synonyms:PLCD2
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length791 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 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.

Caution

Was initially (Ref.2) named PLCD2 and was thought to be a new member of the PLC-delta family. It was later shown that it corresponds to PLCD4 (Ref.3).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7917911-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
PRO_0000088508

Regions

Domain16 – 124109PH
Domain134 – 16936EF-hand 1
Domain170 – 20536EF-hand 2
Domain203 – 23735EF-hand 3
Domain290 – 435146PI-PLC X-box
Domain522 – 638117PI-PLC Y-box
Domain643 – 748106C2
Calcium binding147 – 158121 Potential
Calcium binding183 – 194122 Potential
Region26 – 5328Substrate binding By similarity
Motif760 – 7634PDZ-binding
Compositional bias440 – 45516Poly-Glu

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 binding6791Calcium 2; via carbonyl oxygen By similarity
Metal binding6811Calcium 2 By similarity
Metal binding7051Calcium 2 By similarity
Metal binding7341Calcium 3 By similarity
Metal binding7351Calcium 3; via carbonyl oxygen By similarity
Metal binding7361Calcium 3 By similarity
Binding site4331Substrate By similarity
Binding site4351Substrate By similarity
Binding site5511Substrate By similarity
Binding site5781Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P21671 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: 33E4C4278F280CD2

FASTA79190,581
        10         20         30         40         50         60 
MAYLLQGRLP INQDLLLMQK GTMMRKVRSK SWKKLRFFRL QDDGMTVWHA RQAGGRAKPS 

        70         80         90        100        110        120 
FSISDVDTVR EDHESELLRN LAEEFPLEQG FTIVFHGRRS NLDLVANSVQ EAQTWMQGLQ 

       130        140        150        160        170        180 
LLVGFVTNMD QQERLDQWLS DWFQRGDKNQ DGRMSFGEVQ RLLHLMNVEM DQEYAFQLFQ 

       190        200        210        220        230        240 
TADTSQSGTL EGEEFVEFYK SLTQRPEVQE LFEKFSSDGQ KLTLLEFVDF LQEEQKEGER 

       250        260        270        280        290        300 
ASDLALELID RYEPSESGKL RHVLSMDGFL GYLCSKDGDI FNPTCHPLYQ DMTQPLNHYY 

       310        320        330        340        350        360 
INSSHNTYLV GDQLCGQSSV EGYIRALKRG CRCVEVDIWD GPSGEPIVYH GHTLTSRIPF 

       370        380        390        400        410        420 
KDVVAAIGQY AFQTSDYPVI LSLENHCSWE QQEIIVRHLT EILGDQLLTT ALDGQPPTQL 

       430        440        450        460        470        480 
PSPEDLRGKI LVKGKKLMLE EEEEEPEAEL EAEQEARLDL EAQLESEPQD LSPRSEDKKK 

       490        500        510        520        530        540 
VVMCPLLCRP LCCQIMAQAP ISKPGLLLFP KQKPKAILCP ALSALVVYLK AVTFYSFTHS 

       550        560        570        580        590        600 
REHYHFYETS SFSETKAKSL IKEAGDEFVQ HNAWQLSRVY PSGLRTDSSN YNPQEFWNAG 

       610        620        630        640        650        660 
CQMVAMNMQT AGLEMDLCDG LFRQNAGCGY VLKPDFLRDA QSSFHPERPI SPFKAQTLII 

       670        680        690        700        710        720 
QVISGQQLPK VDNTKEQSIV DPLVRVEIFG VRPDTTRQET SYVENNGFNP YWGQTLCFRI 

       730        740        750        760        770        780 
LVPELALLRF VVKDYDWKSR NDFIGQYTLP WSCMQQGYRH IHLLSKDGLS LHPASIFVHI 

       790 
CTQEVSEEAE S

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Liver.
[2]"A novel inositol-phospholipid-specific phospholipase C. Rapid purification and characterization."
Meldrum E., Katan M., Parker P.
Eur. J. Biochem. 182:673-677(1989) [PubMed: 2753038] [Abstract]
Cited for: PROTEIN SEQUENCE OF 560-584 AND 685-696.
[3]"Phospholipase C delta-type consists of three isozymes: bovine PLCdelta2 is a homologue of human/mouse PLCdelta4."
Irino Y., Cho H., Nakamura Y., Nakahara M., Furutani M., Suh P.-G., Takenawa T., Fukami K.
Biochem. Biophys. Res. Commun. 320:537-543(2004) [PubMed: 15219862] [Abstract]
Cited for: IDENTIFICATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC112449 mRNA. Translation: AAI12450.1.
IPIIPI00696142.
RefSeqNP_001039954.1. NM_001046489.1.
UniGeneBt.45064.

3D structure databases

ProteinModelPortalP21671.
ModBaseSearch...

Protein-protein interaction databases

STRINGP21671.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID540771.
KEGGbta:540771.

Organism-specific databases

CTD84812.

Phylogenomic databases

eggNOGmaNOG16685.
GeneTreeENSGT00570000078720.
HOVERGENHBG053610.
InParanoidP21671.
OrthoDBEOG4868BW.
PhylomeDBP21671.

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.
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. 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_BOVIN
AccessionPrimary (citable) accession number: P21671
Secondary accession number(s): Q2KIZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: October 2, 2007
Last modified: November 16, 2011
This is version 89 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents