PLCZ1_MACFA
ID PLCZ1_MACFA Reviewed; 641 AA.
AC Q95JS1; Q95JS0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1;
DE EC=3.1.4.11;
DE AltName: Full=Phosphoinositide phospholipase C-zeta-1;
DE AltName: Full=Phospholipase C-zeta-1 {ECO:0000250|UniProtKB:Q86YW0};
DE Short=PLC-zeta-1 {ECO:0000250|UniProtKB:Q86YW0};
GN Name=PLCZ1 {ECO:0000312|EMBL:BAB63053.1}; ORFNames=QtsA-14035, QtsA-14094;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB63054.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Testis {ECO:0000312|EMBL:BAB63054.1};
RX PubMed=12416999; DOI=10.1530/rep.0.1240611;
RA Cox L.J., Larman M.G., Saunders C.M., Hashimoto K., Swann K., Lai F.A.;
RT "Sperm phospholipase Czeta from humans and cynomolgus monkeys triggers Ca2+
RT oscillations, activation and development of mouse oocytes.";
RL Reproduction 124:611-623(2002).
RN [2] {ECO:0000312|EMBL:BAB63053.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:BAB63053.1};
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
CC -!- FUNCTION: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC by activated phosphatidylinositol-specific phospholipase C enzymes. In
CC vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers
CC intracellular Ca(2+) oscillations in oocytes solely during M phase and
CC is involved in inducing oocyte activation and initiating embryonic
CC development up to the blastocyst stage. Is therefore a strong candidate
CC for the egg-activating soluble sperm factor that is transferred from
CC the sperm into the egg cytoplasm following gamete membrane fusion. May
CC exert an inhibitory effect on phospholipase-C-coupled processes that
CC depend on calcium ions and protein kinase C, including CFTR trafficking
CC and function. {ECO:0000250|UniProtKB:Q86YW0,
CC ECO:0000250|UniProtKB:Q8K4D7, ECO:0000269|PubMed:12416999,
CC ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC ChEBI:CHEBI:203600; EC=3.1.4.11;
CC Evidence={ECO:0000250|UniProtKB:Q8K4D7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000250|UniProtKB:Q8K4D7};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q8K4D7};
CC -!- SUBUNIT: Interacts via its C2 domain with PtdIns(3)P and, to a lesser
CC extent, PtdIns(5)P in vitro. {ECO:0000250|UniProtKB:Q8K4D7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8K4D7}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K4D7}.
CC Note=Exhibits alternative cytoplasmic/nuclear localization during
CC development. Translocates from the pronucleus into cytoplasm upon
CC nuclear envelope breakdown for mitosis and localizes again to the
CC pronucleus at interphase following meiosis and mitosis (By similarity).
CC {ECO:0000250|UniProtKB:Q8K4D7}.
CC -!- DOMAIN: The EF-hand and C2 domains are essential for triggering Ca(2+)
CC oscillating activity and the regulation of PLCZ1 enzyme activity.
CC {ECO:0000250|UniProtKB:Q8K4D7}.
CC -!- DOMAIN: The X-Y linker region between PI-PLC X-box and Y-box domains
CC may be a target for proteolysis and may play an important regulatory
CC role during fertilization. {ECO:0000250|UniProtKB:Q8K4D7}.
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DR EMBL; AB070109; BAB63054.1; -; mRNA.
DR EMBL; AB070108; BAB63053.1; -; mRNA.
DR RefSeq; NP_001306483.1; NM_001319554.1.
DR AlphaFoldDB; Q95JS1; -.
DR SMR; Q95JS1; -.
DR STRING; 9541.XP_005570328.1; -.
DR PRIDE; Q95JS1; -.
DR GeneID; 102122753; -.
DR CTD; 89869; -.
DR eggNOG; KOG0169; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0006816; P:calcium ion transport; IEA:InterPro.
DR GO; GO:0007343; P:egg activation; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR028395; PLC-zeta1.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR PANTHER; PTHR10336:SF29; PTHR10336:SF29; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cytoplasm; Developmental protein; Fertilization; Hydrolase;
KW Lipid degradation; Lipid metabolism; Nucleus; Reference proteome;
KW Transducer.
FT CHAIN 1..641
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase zeta-1"
FT /id="PRO_0000347245"
FT DOMAIN 35..70
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 155..299
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 382..498
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 498..622
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ACT_SITE 170
FT /evidence="ECO:0000250|UniProtKB:P10688,
FT ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 215
FT /evidence="ECO:0000250|UniProtKB:P10688,
FT ECO:0000255|PROSITE-ProRule:PRU00270"
FT CONFLICT 337..338
FT /note="EK -> R (in Ref. 2; BAB63054)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 74551 MW; 2C54E37BDD3C72E4 CRC64;
MEMKWFLSKI QDDFRGGKIN LEKTQRLLEK LDIRCSYIHV KRIFKDNDRL KQGRITIEEF
RAIYRILTHR EEIVEIFNAY SENRKILLEN NLVQFLTQEQ YTTEMSKTIA FEIIQKYEPI
EEVRKARQMS LEGFTRYMDS RECQLFKNEC RKVYQDMTHP LNDYFISSSH NTYLVSDQLV
GPSDLWGYVS ALVKGCRCLE IDCWDGAQNE PVVYHGYTLT SKLLFKTVIQ AIHKYAFMTS
DYPVVLSLEN HCSPAQQEIM ADNLQTTFGE SLLSDMLADF PDTLPSPEAL KFKVLVKNKK
IGTLKETHER KGSDKRGKVE EWEEEVADLE EEEEEEEKFK ESEIFESVLG ENQDKETGVK
KLSGVTLFKK KKTRKLKIAL ALSDLVIYTK AEKFKSFQHS RLYQQFNENN SIGETQARKL
SKLRAHEFIF HTRKFITRIY PKATRADSSN FNPQEFWNIG CQMVALNFQT PGLPMDLQNG
KFLDNGGSGY ILKPHFLRES ESYFNPSDIK DSMPITLTIR LISGIQLPLT HSSSNKGDTL
VIIEVFGVPN DQMKQQTRVI KKNAFSPRWN ETFTFIIHVP ELALIRFVVE SQGLIAGNEF
LGQYTLPLLC MNKGYRRVPL FSRMGESLEP ASLFVYVWYV R
