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Q7YRU3 (PLCZ1_PIG) 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:PLCZ
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length636 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 Ref.2 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

Developmental stage

In testes, detected only when the elongated spermatids have differentiated from 96 days after birth. 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 – 6366361-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1
PRO_0000347247

Regions

Domain35 – 7036EF-hand
Domain155 – 299145PI-PLC X-box
Domain375 – 491117PI-PLC Y-box
Domain496 – 600105C2
Coiled coil318 – 34528 Potential

Sites

Active site1701 By similarity UniProtKB P10688
Active site2151 By similarity UniProtKB P10688

Sequences

Sequence LengthMass (Da)Tools
Q7YRU3 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: A558E05243ECF479

FASTA63673,702
        10         20         30         40         50         60 
MENKWFLSMV RDDFKGGKIN LEKAQKLLEK LDIQCNTIHV KCIFKDNDRL KQGRITIEEF 

        70         80         90        100        110        120 
RTIYRIIAHR EEIIEIFNAY PENRKILFER NLIDFLTQEQ YSLDINRSIV YEIIQKYEPI 

       130        140        150        160        170        180 
EEVKQAHQMS FEGFTRDMGS SECLLFNNEC GSVYQDMTHP LSDYFISSSH NTYLISDQIM 

       190        200        210        220        230        240 
GPSNLWGYVS ALVKGCRCLE IDCWDGSQNE PVVYHGYTLT SKLLFKTVIQ AIHKYAFITS 

       250        260        270        280        290        300 
DYPVVLSLEN HCSLSQQEVM ADNLQSVFGD ALLSDVLDDC PDRLPSPEAL KFKILVRNKK 

       310        320        330        340        350        360 
IGTLKETHER KGFDKHGQVQ ECEEEEEAEQ EEEENEVRDS EILDILQDDL EKEELKRGVG 

       370        380        390        400        410        420 
IKFFKKKKVK IATALSDLVI YTKVEKFRSF HYSRLYQQFN ETNSIGETQA RKLSKLRASE 

       430        440        450        460        470        480 
FILHTRKFIT RIYPKATRAD SSNFNPQEFW NIGCQMVALN FQTPGLPMDL QNGKFLENGN 

       490        500        510        520        530        540 
SGYILKPHFL RDGKSIFNPN KAPINSNPIT LTIRLISGIQ LPPSYHSSSN KADTLVIIEI 

       550        560        570        580        590        600 
FGVPNDQMKQ QTRVIKKNAF SPRWNETFTF IIQVPELALI RFVVENQGLI TGNEFLGQYT 

       610        620        630 
LPVLCMNKGY RRVPLFSKMG ESLEPASLFI YVWYIR 

« Hide

References

[1]"Molecular cloning, testicular postnatal expression, and oocyte-activating potential of porcine phospholipase Czeta."
Yoneda A., Kashima M., Yoshida S., Terada K., Nakagawa S., Sakamoto A., Hayakawa K., Suzuki K., Ueda J., Watanabe T.
Reproduction 132:393-401(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: Landrace.
Tissue: Testis.
[2]"Functional, biochemical, and chromatographic characterization of the complete [Ca2+]i oscillation-inducing activity of porcine sperm."
Kurokawa M., Sato K., Wu H., He C., Malcuit C., Black S.J., Fukami K., Fissore R.A.
Dev. Biol. 285:376-392(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB113581 mRNA. Translation: BAC78817.1.
RefSeqNP_999515.1. NM_214350.1.
UniGeneSsc.17349.

3D structure databases

ProteinModelPortalQ7YRU3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000000621.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397632.
KEGGssc:397632.

Organism-specific databases

CTD397632.

Phylogenomic databases

eggNOGNOG149692.
HOGENOMHOG000006871.
HOVERGENHBG053610.
KOK05861.

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...

Entry information

Entry namePLCZ1_PIG
AccessionPrimary (citable) accession number: Q7YRU3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: October 1, 2003
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