ID W5QG18_SHEEP Unreviewed; 1206 AA.
AC W5QG18;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase {ECO:0000256|PIRNR:PIRNR000956};
DE EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000956};
GN Name=PLCB2 {ECO:0000313|Ensembl:ENSOARP00000021666.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000021666.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000021666.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000021666.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000021666.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|PIRNR:PIRNR000956}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O =
CC 1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433;
CC Evidence={ECO:0000256|ARBA:ARBA00023726};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000256|ARBA:ARBA00023726};
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:0000256|ARBA:ARBA00023674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000256|ARBA:ARBA00023674};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR000956-2};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000956-2};
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DR EMBL; AMGL01102672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01102673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9940.ENSOARP00000021666; -.
DR PaxDb; 9940-ENSOARP00000021666; -.
DR Ensembl; ENSOART00000021968.1; ENSOARP00000021666.1; ENSOARG00000020162.1.
DR eggNOG; KOG1265; Eukaryota.
DR Proteomes; UP000002356; Chromosome 7.
DR Bgee; ENSOARG00000020162; Expressed in leukocyte and 51 other cell types or tissues.
DR ExpressionAtlas; W5QG18; baseline.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16209; EFh_PI-PLCbeta2; 1.
DR CDD; cd13361; PH_PLC_beta; 1.
DR CDD; cd08624; PI-PLCc_beta2; 1.
DR Gene3D; 2.30.29.240; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR Gene3D; 1.20.1230.10; Phospholipase C beta, distal C-terminal domain; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR016280; PLC-beta.
DR InterPro; IPR028403; PLC-beta2_cat.
DR InterPro; IPR014815; PLC-beta_C.
DR InterPro; IPR042531; PLC-beta_C_sf.
DR InterPro; IPR037862; PLC-beta_PH.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR046969; PLCbeta2_EF.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF10; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-2; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF17787; PH_14; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF08703; PLC-beta_C; 1.
DR PIRSF; PIRSF000956; PLC-beta; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF69989; C-terminal domain of PLC-beta; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR000956-2};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000956};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR000956};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000956,
KW ECO:0000256|RuleBase:RU361133};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000956-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT DOMAIN 544..660
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 660..788
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 439..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1031..1074
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1101..1165
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 464..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..519
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 326
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 373
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 356
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 358
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ SEQUENCE 1206 AA; 136540 MW; EC9AD2212729A842 CRC64;
MSLLNPVLLP PTVKAYLSQG ERFIKWDDET TIASPVILRV DPKGYYLYWT YQSKEMELLD
ITSIRDTRFG KFAKMPKSQK LREVFNMNTP DNFLLKTLTV VSGPDMVDLT FHNFVSYKEN
VGKDWAEDVL ALAKHPLTAN ASRSTFLDKI LVKLKMQLNP EGKIPVKNFF QMFPADRKRV
EAALSTCHLP KGKNDAINPE DFPESVYKSF LMSLCPRPEI DEIFTSYHSK AKPYMTKEHL
AKFINQKQRD SRLNSLLFPP ARPDQVQGLI DKYEPSGINV QRGQLSPEGM VWFLCGPENS
VLAQDKLLLH HDMTQPLNHY FINSSHNTYL TAGQFSGLSS AEMYRQVLLA GCRCVELDCW
KGKPPDEEPI ITHGFTMTTD IYFKEAIEAI AESAFKTSPY PVILSFENHV DSPRQQAKMA
EYCRTMFGDM LLTEPLEKFP LKPGIPLPSP EDLRGKILIK NKKNQFSGPA SPSTEPDGEA
EGSSPPNGPV GEDTVWAGEE GAELEEEEVE EEEEESGNLD EEEIKKMQSD EGTAGLEVTA
YKEMSSLVNY IQPTKFISFE FSAQKNRSYV ISSFTELKAY DLLSKSSVQF VDYNKRQMSR
IYPKGTRMDS SNYMPQMFWN AGCQMVALNF QTMDLPMQQN MALFEFNGQS GYLLKHEFMR
RSDKQFNPFS VDRIDVVVAT TLSITVISGQ FLSERSVRTY VEVELFGLPG DPKRRYRTKL
SPSTNSINPV WKEEPFVFEK ILMPELASLR VAVMEEGNKF LGHRIIPISA LNSGYHHLCL
HNESNMPLTM PALFVFLEMK DYVPDTWADL TVALANPIKF FSAHDKKAVK LKEAMGGQPE
GPFPLGNHPA SQVNGASAPT SNGSAAAGAK AREEATKEVA EPQTASLEEL RELKGVVKLQ
RRQEKELREL GRRGXXXXXX XXAGRGGQRR VQGPQARPGQ GIPQKEVRAV AVATAAAPCP
RRRGWPGAHS LFPRGGLRTL PGEDTAGAAS AEGPEGEDVR LREMRDRLEL ELLQLGEEQC
ECVLKLKEQH AAQQMTKMME LAREKQAAER KTLKETLETD TKEMKKKLEA KRLERIQAMM
KVTTDKMAQE RLKREINNSH IQEVVQVINQ MKENLERHQE KLEEKQAACL EQIQEMEKQF
QQEAMAEYEV KMKGLEMEVK ESVRTCLRAC FSSEEEDKPE RPCVVSRELC EQDTLTEQAE
TQESHL
//
