PLCD1_BOVIN
ID PLCD1_BOVIN Reviewed; 756 AA.
AC P10895; A2VDM2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000250|UniProtKB:P51178};
DE AltName: Full=Phosphoinositide phospholipase C-delta-1;
DE AltName: Full=Phospholipase C-III;
DE Short=PLC-III;
DE AltName: Full=Phospholipase C-delta-1;
DE Short=PLC-delta-1;
GN Name=PLCD1;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 62-756.
RX PubMed=3390863; DOI=10.1016/0092-8674(88)90548-x;
RA Suh P.-G., Ryu S.H., Moon K.H., Suh H.W., Rhee S.G.;
RT "Cloning and sequence of multiple forms of phospholipase C.";
RL Cell 54:161-169(1988).
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 (By
CC similarity). Essential for trophoblast and placental development (By
CC similarity). Binds phosphatidylinositol 4,5-bisphosphate (By
CC similarity). {ECO:0000250|UniProtKB:P51178,
CC ECO:0000250|UniProtKB:Q8R3B1}.
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:P51178};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000250|UniProtKB:P51178};
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:0000250|UniProtKB:P51178};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000250|UniProtKB:P51178};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P51178};
CC Note=Binds 5 Ca(2+) ions per subunit. Two of the Ca(2+) ions are bound
CC to the C2 domain. {ECO:0000250|UniProtKB:P51178};
CC -!- SUBUNIT: Interacts with TGM2. {ECO:0000250|UniProtKB:P10688}.
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DR EMBL; BC133304; AAI33305.1; -; mRNA.
DR EMBL; M20638; AAA30710.1; -; mRNA.
DR PIR; C28821; C28821.
DR RefSeq; NP_001075045.1; NM_001081576.1.
DR AlphaFoldDB; P10895; -.
DR SMR; P10895; -.
DR STRING; 9913.ENSBTAP00000049395; -.
DR PaxDb; P10895; -.
DR PeptideAtlas; P10895; -.
DR PRIDE; P10895; -.
DR Ensembl; ENSBTAT00000052073; ENSBTAP00000049395; ENSBTAG00000037726.
DR GeneID; 281986; -.
DR KEGG; bta:281986; -.
DR CTD; 5333; -.
DR VEuPathDB; HostDB:ENSBTAG00000037726; -.
DR VGNC; VGNC:32984; PLCD1.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000158392; -.
DR HOGENOM; CLU_002738_0_2_1; -.
DR InParanoid; P10895; -.
DR OrthoDB; 368239at2759; -.
DR TreeFam; TF313216; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000037726; Expressed in esophagus and 104 other tissues.
DR ExpressionAtlas; P10895; baseline and differential.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR028391; PLC-delta1.
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; PTHR10336; 1.
DR PANTHER; PTHR10336:SF80; PTHR10336:SF80; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF00169; PH; 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; SM00233; PH; 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; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Calcium; Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transducer.
FT CHAIN 1..756
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase delta-1"
FT /id="PRO_0000088503"
FT DOMAIN 21..130
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 140..175
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 176..211
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 296..440
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 492..609
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 609..737
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ACT_SITE 311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 312
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 440
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 522
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 549
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 651
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 653
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 677
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 706
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 707
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 708
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT MOD_RES 457
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R3B1"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51178"
FT CARBOHYD 191
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 193
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CONFLICT 291
FT /note="H -> D (in Ref. 2; AAA30710)"
FT /evidence="ECO:0000305"
FT CONFLICT 664..665
FT /note="SR -> TG (in Ref. 2; AAA30710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 86073 MW; EBA47E8BAEE2D398 CRC64;
MDSGRDFLTL HGLQDDKDLQ ALLKGGQLLK VKSNSWRRER FYKLQEDCKT IWQESRKVMR
TPESQLFSIE DIQEVRMGHR TEGLEKFARD VPENRCFSIV FKDQRNTLDL IAPSPADAQH
WVQGLGKIIH HSGSMDQQQK LRHWIHSCLR KADKNKDNKM SFKELQNFLK ELNIQVDDSY
ARKIFKECDH SQTDSLEDEE IETFYKILTQ RKEIDRTFEE ATGSKETLSV DQLVTFLQHQ
QREEEAGPAL ALSLIERYEP SETAKAQRQM TKDGFLMYLL SADGSAFDLA HRRVYQDMDQ
PLSHYLVSSS HNTYLLEDQL TGPSSTEAYI RALCKGCRCL ELDCWDGPNQ EPIIYHGYTF
TSKILFCDVV RAIRDYAFKA SPYPVILSLE NHCSLEQQRV MARHLRTLLG PMLLDRPLDG
VVTSLPSPEQ LRGKILLKGK KLGGLFPPGG EGGPEATVVS DEDEAAEMED EAVRSQVQHK
SKEDKLRLAK ELSDMVIYCK SVHFRGFPSS GTSGQAFYEM SSFSENRALR LLQESGNSFV
RHNVNHLSRI YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ TPGSEMDVYQ GRFLDNGACG
YVLKPAFLRD PNSTFNSRAL AHGPWWTPKR LNVRVISGQQ LPKVNKNKNS IVDPKVTVEI
HGVSRDVASR QTAVVTNNGF NPWWDTELEF EVAVPELALV RFVVEDYDAS SKNDFIGQST
IPLKSLKQGY RHIHLLSKNG DQHPSATLFV KVALQD
