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Q2VRL0 (PLCZ1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. 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

Names and origin

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

EC=3.1.4.11
Alternative name(s):
Phosphoinositide phospholipase C-zeta-1
Phospholipase C-zeta-1
Short name=PLC-zeta-1
Gene names
Name:PLCZ1
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length637 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca2+-dependent manner. Triggers intracellular Ca2+ oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function. Ref.1 UniProtKB Q86YW0 UniProtKB Q8K4D7

Catalytic activity

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. UniProtKB P10688

Cofactor

Calcium By similarity. UniProtKB Q8K4D7

Subunit structure

Interacts via its C2 domain with PtdIns3P and, to a lesser extent, PtdIns5P in vitro By similarity. UniProtKB Q8K4D7

Subcellular location

Nucleus By similarity. Cytoplasmperinuclear region By similarity. Note: Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronucleus at interphase following meiosis and mitosis By similarity. UniProtKB Q8K4D7

Tissue specificity

Expressed specifically in testis. Ref.1

Domain

The EF-hand and C2 domains are essential for triggering Ca2+ oscillating activity and the regulation of PLCZ1 enzyme activity By similarity. UniProtKB Q8K4D7

The X-Y linker region between PI-PLC X-box and Y-box domains may be a target for proteolysis and may play an important regulatory role during fertilization By similarity. UniProtKB Q8K4D7

Sequence similarities

Contains 1 C2 domain.

Contains 1 EF-hand domain.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6376371-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1
PRO_0000347249

Regions

Domain36 – 7237EF-hand
Domain157 – 302146PI-PLC X-box
Domain377 – 493117PI-PLC Y-box
Domain498 – 602105C2

Sites

Active site1721 By similarity UniProtKB P10688
Active site2171 By similarity UniProtKB P10688

Sequences

Sequence LengthMass (Da)Tools
Q2VRL0 [UniParc].

Last modified January 10, 2006. Version 1.
Checksum: 8FFFA824997BA401

FASTA63772,533
        10         20         30         40         50         60 
MEENRWFLNI IQDGFMNGKI DFDSTVKLLE KLHMPFNLAH VKHVFKKTVD KRKIHTINIE 

        70         80         90        100        110        120 
DFRAIYRAIV HRNEFHEIFC AYSENRKNLA DTELTAFLKK EQFKTEGAET TALEVILKYE 

       130        140        150        160        170        180 
PIDEVRKRRQ LSFEGFIRYM SSEDCTIFKK EHRTVYQDMN HPLCDYFISS SHNTYLVSDQ 

       190        200        210        220        230        240 
LIGPSDLNGY ISALLKGCRC LEIDCWDGSN NDPVVYHGHT LTSKITFCSV IHVVDKYAFA 

       250        260        270        280        290        300 
ASDYPVVLSL ENHCSTKQQE RIAQYLLNIL GDKLLTSPIG DIEVTQLPSP EALKFKILVK 

       310        320        330        340        350        360 
NKKCGTIEET MLRKGRDSHG ETGEVSEEEI TSSDEETDEK TPLYPKSGSS KRKSEGRSSP 

       370        380        390        400        410        420 
PPRKKAKVKK MKIAMGLSDL VIYTKSEKFV SFEHSLAHQK CYENNSIGEL KAQKFVKHAA 

       430        440        450        460        470        480 
NQFVSHTSRF ITRIYPKGTR AGSSNYNPQE FWNVGCQMVA LNFQTSGTPM ELQNGKFLDN 

       490        500        510        520        530        540 
GGCGYILKPE FLRNRNSTFN PHNVGRYSNP LSLSIRLISG HQLPPSNLSK SNKADPLVQL 

       550        560        570        580        590        600 
EIYGVPEDQA KRKSSVIKSN ALSPRWDETF SFTVQVPELA LIRFCVQDEI SLVANDFLGQ 

       610        620        630 
YTLPLLSLSK GYCTVPLFSK SGGKLEPASL FVYVWYY 

« Hide

References

[1]"Phospholipase Czeta, the trigger of egg activation in mammals, is present in a non-mammalian species."
Coward K., Ponting C.P., Chang H.-Y., Hibbitt O., Savolainen P., Jones K.T., Parrington J.
Reproduction 130:157-163(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Testis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY843531 mRNA. Translation: AAX48001.1.
RefSeqNP_001034362.1. NM_001039273.1.
UniGeneGga.21947.

3D structure databases

ProteinModelPortalQ2VRL0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000021386.

Proteomic databases

PaxDbQ2VRL0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000021418; ENSGALP00000021386; ENSGALG00000013123.
GeneID418182.
KEGGgga:418182.

Organism-specific databases

CTD89869.

Phylogenomic databases

eggNOGNOG149692.
GeneTreeENSGT00730000110266.
HOGENOMHOG000006871.
HOVERGENHBG053610.
InParanoidQ2VRL0.
KOK05861.
OMAMPEKDDF.
OrthoDBEOG7V49XT.
PhylomeDBQ2VRL0.
TreeFamTF313216.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR001192. PI-PLC_fam.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR028395. PLC-zeta1.
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:SF29. PTHR10336:SF29. 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.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20821385.
PROQ2VRL0.

Entry information

Entry namePLCZ1_CHICK
AccessionPrimary (citable) accession number: Q2VRL0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: January 10, 2006
Last modified: April 16, 2014
This is version 79 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