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Protein

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

Gene

PLCZ1

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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.By similarityCurated1 Publication

Catalytic activityi

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

Cofactori

Ca2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei170 – 1701PROSITE-ProRule annotationBy similarity
Active sitei215 – 2151PROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. phosphatidylinositol phospholipase C activity Source: UniProtKB-EC
  3. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. calcium ion transport Source: InterPro
  2. egg activation Source: InterPro
  3. intracellular signal transduction Source: InterPro
  4. lipid catabolic process Source: UniProtKB-KW
  5. multicellular organismal development Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Transducer

Keywords - Biological processi

Fertilization, Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
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-1By similarity
Short name:
PLC-zeta-1By similarity
Gene namesi
Name:PLCZ1Imported
ORF Names:QtsA-14035, QtsA-14094
OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifieri9541 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Subcellular locationi

  1. Nucleus By similarity
  2. Cytoplasmperinuclear region By similarity

  3. 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).By similarity

GO - Cellular componenti

  1. cytosol Source: InterPro
  2. nucleus Source: UniProtKB-SubCell
  3. perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6416411-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1PRO_0000347245Add
BLAST

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ95JS1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 7036EF-handPROSITE-ProRule annotationAdd
BLAST
Domaini155 – 299145PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini382 – 498117PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini502 – 605104C2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi320 – 35637Glu-richSequence AnalysisAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 EF-hand domain.PROSITE-ProRule annotation
Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG053610.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR000008. 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]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF29. PTHR10336:SF29. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q95JS1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMKWFLSKI QDDFRGGKIN LEKTQRLLEK LDIRCSYIHV KRIFKDNDRL
60 70 80 90 100
KQGRITIEEF RAIYRILTHR EEIVEIFNAY SENRKILLEN NLVQFLTQEQ
110 120 130 140 150
YTTEMSKTIA FEIIQKYEPI EEVRKARQMS LEGFTRYMDS RECQLFKNEC
160 170 180 190 200
RKVYQDMTHP LNDYFISSSH NTYLVSDQLV GPSDLWGYVS ALVKGCRCLE
210 220 230 240 250
IDCWDGAQNE PVVYHGYTLT SKLLFKTVIQ AIHKYAFMTS DYPVVLSLEN
260 270 280 290 300
HCSPAQQEIM ADNLQTTFGE SLLSDMLADF PDTLPSPEAL KFKVLVKNKK
310 320 330 340 350
IGTLKETHER KGSDKRGKVE EWEEEVADLE EEEEEEEKFK ESEIFESVLG
360 370 380 390 400
ENQDKETGVK KLSGVTLFKK KKTRKLKIAL ALSDLVIYTK AEKFKSFQHS
410 420 430 440 450
RLYQQFNENN SIGETQARKL SKLRAHEFIF HTRKFITRIY PKATRADSSN
460 470 480 490 500
FNPQEFWNIG CQMVALNFQT PGLPMDLQNG KFLDNGGSGY ILKPHFLRES
510 520 530 540 550
ESYFNPSDIK DSMPITLTIR LISGIQLPLT HSSSNKGDTL VIIEVFGVPN
560 570 580 590 600
DQMKQQTRVI KKNAFSPRWN ETFTFIIHVP ELALIRFVVE SQGLIAGNEF
610 620 630 640
LGQYTLPLLC MNKGYRRVPL FSRMGESLEP ASLFVYVWYV R
Length:641
Mass (Da):74,551
Last modified:December 1, 2001 - v1
Checksum:i2C54E37BDD3C72E4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti337 – 3382EK → R in BAB63054 (PubMed:12498619).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB070109 mRNA. Translation: BAB63054.1.
AB070108 mRNA. Translation: BAB63053.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB070109 mRNA. Translation: BAB63054.1.
AB070108 mRNA. Translation: BAB63053.1.

3D structure databases

ProteinModelPortaliQ95JS1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG053610.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR000008. 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]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF29. PTHR10336:SF29. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sperm phospholipase Czeta from humans and cynomolgus monkeys triggers Ca2+ oscillations, activation and development of mouse oocytes."
    Cox L.J., Larman M.G., Saunders C.M., Hashimoto K., Swann K., Lai F.A.
    Reproduction 124:611-623(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: TestisImported.
  2. "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in the human genome sequence."
    Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M., Terao K., Sugano S., Hashimoto K.
    BMC Genomics 3:36-36(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: TestisImported.

Entry informationi

Entry nameiPLCZ1_MACFA
AccessioniPrimary (citable) accession number: Q95JS1
Secondary accession number(s): Q95JS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: December 1, 2001
Last modified: January 7, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.