1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1

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Q7YRU3 (PLCZ1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 71. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	636 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › perinuclear 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.

Ontologies

Keywords
Biological process	Fertilization Lipid degradation Lipid metabolism
Cellular component	Cytoplasm Nucleus
Domain	Coiled coil
Ligand	Calcium
Molecular function	Developmental protein Hydrolase Transducer
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular signal transduction Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW single fertilization Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro phosphatidylinositol phospholipase C activity Inferred from electronic annotation. Source: EC signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 636

636

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1

PRO_0000347247

Regions

Domain

35 – 70

EF-hand

Domain

155 – 299

145

PI-PLC X-box

Domain

375 – 491

117

PI-PLC Y-box

Domain

496 – 600

105

Coiled coil

318 – 345

Potential

Sites

Active site

170

By similarity UniProtKB P10688

Active site

215

By similarity UniProtKB P10688

Sequences

Sequence

Length

Mass (Da)

Tools

Q7YRU3 [UniParc].

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

636

73,702

        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

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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.
RefSeq	NP_999515.1. NM_214350.1.
UniGene	Ssc.17349.
3D structure databases
HSSP	HSSP built from PDB template 1QAS based on UniProtKB P10688.
ProteinModelPortal	Q7YRU3.
ModBase	Search...
Protein-protein interaction databases
STRING	9823.ENSSSCP00000000621.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	397632.
KEGG	ssc:397632.
Organism-specific databases
CTD	397632.
Phylogenomic databases
eggNOG	NOG149692.
HOGENOM	HOG000006871.
HOVERGEN	HBG053610.
KO	K05861.
OrthoDB	EOG4X0MSB.
Family and domain databases
Gene3D	1.10.238.10. 2 hits. 3.20.20.190. 2 hits.
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR011992. EF-hand-like_dom. IPR001192. Pinositol_PLipase_C. IPR017946. PLC-like_Pdiesterase_TIM-brl. IPR015359. PLipase_C_EF-hand-like. IPR000909. PLipase_C_PInositol-sp_X_dom. IPR001711. PLipase_C_Pinositol-sp_Y. [Graphical view]
PANTHER	PTHR10336. PTHR10336. 1 hit.
Pfam	PF00168. C2. 1 hit. PF09279. efhand_like. 1 hit. PF00388. PI-PLC-X. 1 hit. PF00387. PI-PLC-Y. 1 hit. [Graphical view]
PRINTS	PR00390. PHPHLIPASEC.
SMART	SM00239. C2. 1 hit. SM00148. PLCXc. 1 hit. SM00149. PLCYc. 1 hit. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.
PROSITE	PS50004. C2. 1 hit. PS00018. EF_HAND_1. False negative. PS50222. EF_HAND_2. False negative. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLCZ1_PIG

Accession

Primary (citable) accession number: Q7YRU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	October 1, 2003
Last modified:	April 3, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents