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Q1RML2 (PLCZ1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. 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
Synonyms:PLCZ
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length634 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.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. 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

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 – 6346341-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1
PRO_0000347243

Regions

Domain35 – 7036EF-hand
Domain155 – 299145PI-PLC X-box
Domain376 – 492117PI-PLC Y-box
Domain497 – 598102C2

Sites

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

Experimental info

Sequence conflict1881Y → H in AAV54518. Ref.1
Sequence conflict4361K → Q in AAV54518. Ref.1
Sequence conflict5061D → G in AAV54518. Ref.1
Sequence conflict6061R → K in AAV54518. Ref.1
Sequence conflict6331I → V in AAV54518. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q1RML2 [UniParc].

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

FASTA63473,732
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY646356 mRNA. Translation: AAV54518.1.
BC114836 mRNA. Translation: AAI14837.1.
RefSeqNP_001011680.2. NM_001011680.3.
XP_005207032.1. XM_005206975.1.
UniGeneBt.37187.

3D structure databases

ProteinModelPortalQ1RML2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000017574.

Proteomic databases

PRIDEQ1RML2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000017574; ENSBTAP00000017574; ENSBTAG00000013202.
GeneID497026.
KEGGbta:497026.

Organism-specific databases

CTD89869.

Phylogenomic databases

eggNOGNOG149692.
GeneTreeENSGT00730000110266.
HOGENOMHOG000006871.
HOVERGENHBG053610.
InParanoidQ1RML2.
KOK05861.
OMAMPEKDDF.
OrthoDBEOG7V49XT.
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.
IPR002048. EF_hand_dom.
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.
PS50222. EF_HAND_2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20865839.

Entry information

Entry namePLCZ1_BOVIN
AccessionPrimary (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: April 16, 2014
This is version 70 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