ID W5PIH3_SHEEP Unreviewed; 1208 AA.
AC W5PIH3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=PLCB4 {ECO:0000313|Ensembl:ENSOARP00000010242.1};
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:ENSOARP00000010242.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000010242.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000010242.1,
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:ENSOARP00000010242.1}
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; AMGL01023467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01023468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01023469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01023470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01023471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01023472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01023473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01023474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01023475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01023476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5PIH3; -.
DR SMR; W5PIH3; -.
DR STRING; 9940.ENSOARP00000010242; -.
DR PaxDb; 9940-ENSOARP00000010242; -.
DR Ensembl; ENSOART00000010392.1; ENSOARP00000010242.1; ENSOARG00000009536.1.
DR eggNOG; KOG1265; Eukaryota.
DR HOGENOM; CLU_002738_2_1_1; -.
DR OMA; AMQKAHC; -.
DR Proteomes; UP000002356; Chromosome 13.
DR Bgee; ENSOARG00000009536; Expressed in gastric lymph node and 55 other cell types or tissues.
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; cd16211; EFh_PI-PLCbeta4; 1.
DR CDD; cd13361; PH_PLC_beta; 1.
DR CDD; cd08591; PI-PLCc_beta; 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; IPR042531; PLC-beta_C_sf.
DR InterPro; IPR009535; PLC-beta_CS.
DR InterPro; IPR037862; PLC-beta_PH.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
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:SF211; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-4; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF06631; DUF1154; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT DOMAIN 577..693
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 696..821
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 875..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 934..964
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 891..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 328
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 375
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 329
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 360
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ SEQUENCE 1208 AA; 137735 MW; ECFB106EEE5ED5DB CRC64;
MAKPYEFNWQ KEVPSFLQEG AVFDRYEEES FVFEPNCLFK VDEFGFFLTW RSEGKEGQVL
ECSLINSVRL GATPKDPKIL AALEALGKSE NDLEGRIVCV CSGADLVNIS FTYMVAENPE
ITKQWVEGLR SIIHNFRANN VSPMTCLKKH WMKLAFMTNT NGKIPVRSIT RTFASGKTEK
VIFQALKELG LPSGKNDEIE PAAFTYEKFY ELTQKICPRT DIEDLFKKIN GDKTDYLTVD
QLVSFLNEHQ RDPRLNEILF PFYDAKRAMQ IIEMYEPDED LKKQGLISSD GFCRYLMSDE
NAPVFLDRLE LYQEMDHPLA HYFISSSHNT YLTGRQFGGK SSVEMYRQVL LAGCRCVELD
CWDGKGEDQE PIITHGKAMC TDILFKDVIQ AIKETAFVTS EYPVILSFEN HCSKYQQYKM
SKYCEDLFGD LLLKQALESH PLEPGRPLPS PNDLKRKILI KNKRLKPEVE KKQLEALKSV
MEAGESAAPV NILEDDNEEE IESAEQEEEA HPEYKYGNEL SADDLGHKEA IANSVKKASD
DLEHENSKKG LVTVEDEQAW MASYKYVGAT TNIHPYLSTM INYAQPVKFQ GFHVAEERNI
HYNMSSFNES VGLGYLKTHA IEFVNYNKRQ MSRIYPKGGR VDSSNYMPQI FWNAGCQMVS
LNYQTPDLAM QLNQGKFEYN GSCGYLLKPD FMRRPDRTFD PFSETPVDGV IAATCSVQVI
SGQFLSDKKI GTYVEVDMYG LPTDTIRKEF RTRMVMNNGL NPVYNEESFV FRKVILPDLA
VLRIAVYDDN NKLIGQRILP LDGLQAGYRH ISLRNEGNKP LSLPTIFCNI VLKTYVPDGF
GDIVDALSDP KKFLSITEKR ADQMRAMGIE TSDIADVPSD TSKNDKKGKA NTAKANVTPQ
SSSELRPTTT AALGAGLEAK KGIELIPQVR IEDLKQMKAY LKHLKKQQKE LNSLKKKHAK
EHSTMQKLHC TQVDKIVAQY DKEKLTHEKI LEKAMKKKGG SNCLEMKKET EIKIQTLTSD
HKSKVKEIVA QHTKEWSDMI NTHSAEEQEV RDLHLSQQCE LLRKLLISAH EQQTQQLKLS
HDRESKEMRA HQAKISMENS KAISQDKSIK NKAERERRVR ELNSSNTKKF LEERKRLAMK
QSKEMDQLKK VQLEHLEFLE KQNEQKQLLK SCHAVSQTQG EGDAADGEIG SRDGPQTSNS
CVKLQDTN
//
