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Q95JS1

- PLCZ1_MACFA

UniProt

Q95JS1 - PLCZ1_MACFA

Protein

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

Gene

PLCZ1

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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 similarity1 PublicationCurated

    Catalytic activityi

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

    Cofactori

    Calcium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei170 – 1701By similarityPROSITE-ProRule annotation
    Active sitei215 – 2151By similarityPROSITE-ProRule annotation

    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

    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

    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.By similarity

    GO - Cellular componenti

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

    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

    MEMKWFLSKI QDDFRGGKIN LEKTQRLLEK LDIRCSYIHV KRIFKDNDRL    50
    KQGRITIEEF RAIYRILTHR EEIVEIFNAY SENRKILLEN NLVQFLTQEQ 100
    YTTEMSKTIA FEIIQKYEPI EEVRKARQMS LEGFTRYMDS RECQLFKNEC 150
    RKVYQDMTHP LNDYFISSSH NTYLVSDQLV GPSDLWGYVS ALVKGCRCLE 200
    IDCWDGAQNE PVVYHGYTLT SKLLFKTVIQ AIHKYAFMTS DYPVVLSLEN 250
    HCSPAQQEIM ADNLQTTFGE SLLSDMLADF PDTLPSPEAL KFKVLVKNKK 300
    IGTLKETHER KGSDKRGKVE EWEEEVADLE EEEEEEEKFK ESEIFESVLG 350
    ENQDKETGVK KLSGVTLFKK KKTRKLKIAL ALSDLVIYTK AEKFKSFQHS 400
    RLYQQFNENN SIGETQARKL SKLRAHEFIF HTRKFITRIY PKATRADSSN 450
    FNPQEFWNIG CQMVALNFQT PGLPMDLQNG KFLDNGGSGY ILKPHFLRES 500
    ESYFNPSDIK DSMPITLTIR LISGIQLPLT HSSSNKGDTL VIIEVFGVPN 550
    DQMKQQTRVI KKNAFSPRWN ETFTFIIHVP ELALIRFVVE SQGLIAGNEF 600
    LGQYTLPLLC MNKGYRRVPL FSRMGESLEP ASLFVYVWYV R 641
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB070109 mRNA. Translation: BAB63054.1.
    AB070108 mRNA. Translation: BAB63053.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB070109 mRNA. Translation: BAB63054.1 .
    AB070108 mRNA. Translation: BAB63053.1 .

    3D structure databases

    ProteinModelPortali Q95JS1.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG053610.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    2.60.40.150. 1 hit.
    3.20.20.190. 2 hits.
    InterProi IPR000008. 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 ]
    PANTHERi PTHR10336. PTHR10336. 1 hit.
    PTHR10336:SF29. PTHR10336:SF29. 1 hit.
    Pfami PF00168. C2. 1 hit.
    PF09279. EF-hand_like. 1 hit.
    PF00388. PI-PLC-X. 1 hit.
    PF00387. PI-PLC-Y. 1 hit.
    [Graphical view ]
    PRINTSi PR00390. PHPHLIPASEC.
    SMARTi SM00239. C2. 1 hit.
    SM00148. PLCXc. 1 hit.
    SM00149. PLCYc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF51695. SSF51695. 1 hit.
    PROSITEi PS50004. C2. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS50007. PIPLC_X_DOMAIN. 1 hit.
    PS50008. PIPLC_Y_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 73 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