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

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Reviewed, UniProtKB/Swiss-Prot Q1RML2 (PLCZ1_BOVIN)

Last modified February 9, 2010. Version 33. History...

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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 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:	PLCZ1
Synonyms:	PLCZ

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length	634 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

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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.3 Ref.4 UniProtKB Q8K4D7 UniProtKB Q86YW0
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.
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
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.

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Ontologies

Keywords
Biological process	Fertilization Lipid degradation
Cellular component	Cytoplasm Nucleus
Ligand	Calcium
Molecular function	Developmental protein Hydrolase Transducer
Gene Ontology (GO)
Biological process	intracellular signaling cascade 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
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: UniProtKB-KW phosphoinositide phospholipase C activity Inferred from electronic annotation. Source: EC signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 634

634

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

PRO_0000347243

Regions

Domain

35 – 70

EF-hand

Domain

155 – 299

145

PI-PLC X-box

Domain

376 – 492

117

PI-PLC Y-box

Domain

497 – 598

102

Sites

Active site

170

By similarity UniProtKB P10688

Active site

215

By similarity UniProtKB P10688

Experimental info

Sequence conflict

188

Y → H in AAV54518. Ref.1

Sequence conflict

436

K → Q in AAV54518. Ref.1

Sequence conflict

506

D → G in AAV54518. Ref.1

Sequence conflict

606

R → K in AAV54518. Ref.1

Sequence conflict

633

I → V in AAV54518. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q1RML2-1 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 84D721F03B8AE720
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FASTA

634

73,732

        10         20         30         40         50         60 
MENKWFLLMV RDDFKGGKIT LEKALKLLEK LDIQCNTIHV KYIFKDNDRL KQGRITIEEF 

        70         80         90        100        110        120 
RTIYRIITYR EEIIEIFNTY SENRKILLEK NLVEFLMREQ YTLDFNKSIA SEIIQKYEPI 

       130        140        150        160        170        180 
EEVKQAHQMS FEGFRRYMDS SECLLFDNKC DHVYQDMTHP LTDYFISSSH NTYLISDQLW 

       190        200        210        220        230        240 
GPSDLWGYIS ALVKGCRCLE IDCWDGSQNE PVVYHGYTFT SKLLFKTVIQ AINKYAFLAS 

       250        260        270        280        290        300 
EYPVVLSLEN HCSPSQQEVM ADSLLATFGD ALLSYTLDNF SDRLPSPEAL KFKILVRNKK 

       310        320        330        340        350        360 
IGTLHETLER KGSDMHGKVE EFEEEEEIEQ EEDGSGAKEP EPVGDFQDDL AKEEQLKRVV 

       370        380        390        400        410        420 
GIPLFRKKKI KISMALSDLV IYTKVEKFKS FHHSHLYQQF NESNSIGESQ ARKLTKLAAR 

       430        440        450        460        470        480 
EFILHTRRFI TRVYPKALRA DSSNFNPQEF WNVGCQMVAL NFQTPGVPMD LQNGKFLDNG 

       490        500        510        520        530        540 
CSGYVLKPRF LRDKKTKFNP HKVQIDSNPL TLTIRLISGI QLPPSYQNKA DTLVIVEIFG 

       550        560        570        580        590        600 
VPNDQMKQQS RVIKKNAFNP RWNETFTFVI QVPELALIRF VAENQGLIAG NEFLGQYTLP 

       610        620        630 
VLCMNRGYRR VPLFSKMGES LEPASLFIYV WYIR

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of PLC-zeta in cattle." Kumar K.G., Chomdej S., Wimmers K., Schellander K. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Liver.
[3]	"Fertilization and inositol 1,4,5-trisphosphate (IP3)-induced calcium release in type-1 inositol 1,4,5-trisphosphate receptor down-regulated bovine eggs." Malcuit C., Knott J.G., He C., Wainwright T., Parys J.B., Robl J.M., Fissore R.A. Biol. Reprod. 73:2-13(2005) [PubMed: 15744020] [Abstract] Cited for: FUNCTION.
[4]	"Parthenogenetic activation of bovine oocytes using bovine and murine phospholipase C zeta." Ross P.J., Beyhan Z., Iager A.E., Yoon S.-Y., Malcuit C., Schellander K., Fissore R.A., Cibelli J.B. BMC Dev. Biol. 8:16-16(2008) [PubMed: 18284699] [Abstract] Cited for: FUNCTION.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AY646356 mRNA. Translation: AAV54518.1. BC114836 mRNA. Translation: AAI14837.1.
IPI	IPI00715247.
RefSeq	NP_001011680.2.
UniGene	Bt.37187
3D structure databases
SMR	Q1RML2. Positions 4-631.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1RML2.
Genome annotation databases
Ensembl	ENSBTAT00000017574; ENSBTAP00000017574; ENSBTAG00000013202; Bos taurus. [Genome view]
GeneID	497026.
KEGG	bta:497026.
Organism-specific databases
CTD	497026.
Phylogenomic databases
eggNOG	maNOG13414.
HOVERGEN	Q1RML2.
InParanoid	Q1RML2.
PhylomeDB	Q1RML2.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR011992. EF-hand-like_dom. IPR018249. EF_HAND_2. IPR015359. Phospholipase_C_EF-hand-like. IPR001192. Phospholipase_C_Pinositol-sp_C. IPR001711. Phospholipase_C_Pinositol-sp_Y. IPR017946. PLC-like_Pdiesterase_TIM-brl. IPR000909. PLipase_C_PInositol-sp_X_dom. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 2 hits. G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 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]
PROSITE	PS50004. C2. 1 hit. PS00018. EF_HAND_1. False negative. PS50222. EF_HAND_2. 1 hit. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

PLCZ1_BOVIN

Accession

Primary (citable) accession number: Q1RML2
Secondary accession number(s): Q5IT24

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	May 16, 2006
Last modified:	February 9, 2010
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (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)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents