PLCZ1_BOVIN
ID PLCZ1_BOVIN Reviewed; 634 AA.
AC Q1RML2; Q5IT24;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
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:0000250|UniProtKB:Q86YW0};
GN Synonyms=PLCZ {ECO:0000312|EMBL:AAI14837.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAV54518.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kumar K.G., Chomdej S., Wimmers K., Schellander K.;
RT "Molecular cloning and characterization of PLC-zeta in cattle.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAV54518.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI14837.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAI14837.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=15744020; DOI=10.1095/biolreprod.104.037333;
RA Malcuit C., Knott J.G., He C., Wainwright T., Parys J.B., Robl J.M.,
RA Fissore R.A.;
RT "Fertilization and inositol 1,4,5-trisphosphate (IP3)-induced calcium
RT release in type-1 inositol 1,4,5-trisphosphate receptor down-regulated
RT bovine eggs.";
RL Biol. Reprod. 73:2-13(2005).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=18284699; DOI=10.1186/1471-213x-8-16;
RA Ross P.J., Beyhan Z., Iager A.E., Yoon S.-Y., Malcuit C., Schellander K.,
RA Fissore R.A., Cibelli J.B.;
RT "Parthenogenetic activation of bovine oocytes using bovine and murine
RT phospholipase C zeta.";
RL BMC Dev. Biol. 8:16-16(2008).
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:15744020,
CC ECO:0000269|PubMed:18284699, 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}.
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; AY646356; AAV54518.1; -; mRNA.
DR EMBL; BC114836; AAI14837.1; -; mRNA.
DR RefSeq; NP_001011680.2; NM_001011680.3.
DR AlphaFoldDB; Q1RML2; -.
DR SMR; Q1RML2; -.
DR STRING; 9913.ENSBTAP00000017574; -.
DR PaxDb; Q1RML2; -.
DR PRIDE; Q1RML2; -.
DR Ensembl; ENSBTAT00000017574; ENSBTAP00000017574; ENSBTAG00000013202.
DR GeneID; 497026; -.
DR KEGG; bta:497026; -.
DR CTD; 89869; -.
DR VEuPathDB; HostDB:ENSBTAG00000013202; -.
DR VGNC; VGNC:32995; PLCZ1.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000159950; -.
DR HOGENOM; CLU_002738_0_3_1; -.
DR InParanoid; Q1RML2; -.
DR OMA; YLTCTLV; -.
DR OrthoDB; 368239at2759; -.
DR TreeFam; TF313216; -.
DR Reactome; R-BTA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000013202; Expressed in semen and 10 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045120; C:pronucleus; IEA:Ensembl.
DR GO; GO:0061827; C:sperm head; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:Ensembl.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IEA:Ensembl.
DR GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
DR GO; GO:0007343; P:egg activation; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0060470; P:positive regulation of cytosolic calcium ion concentration involved in egg activation; IBA:GO_Central.
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..634
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase zeta-1"
FT /id="PRO_0000347243"
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 376..492
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 492..615
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 312..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..334
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 188
FT /note="Y -> H (in Ref. 1; AAV54518)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="K -> Q (in Ref. 1; AAV54518)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="D -> G (in Ref. 1; AAV54518)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="R -> K (in Ref. 1; AAV54518)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="I -> V (in Ref. 1; AAV54518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 634 AA; 73732 MW; 84D721F03B8AE720 CRC64;
MENKWFLLMV RDDFKGGKIT LEKALKLLEK LDIQCNTIHV KYIFKDNDRL KQGRITIEEF
RTIYRIITYR EEIIEIFNTY SENRKILLEK NLVEFLMREQ YTLDFNKSIA SEIIQKYEPI
EEVKQAHQMS FEGFRRYMDS SECLLFDNKC DHVYQDMTHP LTDYFISSSH NTYLISDQLW
GPSDLWGYIS ALVKGCRCLE IDCWDGSQNE PVVYHGYTFT SKLLFKTVIQ AINKYAFLAS
EYPVVLSLEN HCSPSQQEVM ADSLLATFGD ALLSYTLDNF SDRLPSPEAL KFKILVRNKK
IGTLHETLER KGSDMHGKVE EFEEEEEIEQ EEDGSGAKEP EPVGDFQDDL AKEEQLKRVV
GIPLFRKKKI KISMALSDLV IYTKVEKFKS FHHSHLYQQF NESNSIGESQ ARKLTKLAAR
EFILHTRRFI TRVYPKALRA DSSNFNPQEF WNVGCQMVAL NFQTPGVPMD LQNGKFLDNG
CSGYVLKPRF LRDKKTKFNP HKVQIDSNPL TLTIRLISGI QLPPSYQNKA DTLVIVEIFG
VPNDQMKQQS RVIKKNAFNP RWNETFTFVI QVPELALIRF VAENQGLIAG NEFLGQYTLP
VLCMNRGYRR VPLFSKMGES LEPASLFIYV WYIR
