ID A0A3Q7SMP6_VULVU Unreviewed; 777 AA.
AC A0A3Q7SMP6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
GN Name=PLCD1 {ECO:0000313|RefSeq:XP_025856806.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025856806.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025856806.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025856806.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025856806.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:PIRSR628391-3};
CC Note=Binds 3 Ca(2+) ions per subunit. Two of the Ca(2+) ions are bound
CC to the C2 domain. {ECO:0000256|PIRSR:PIRSR628391-3};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_025856806.1; XM_026001021.1.
DR AlphaFoldDB; A0A3Q7SMP6; -.
DR STRING; 9627.ENSVVUP00000008395; -.
DR GlyCosmos; A0A3Q7SMP6; 2 sites, No reported glycans.
DR KEGG; vvp:112921661; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000286640; Unplaced.
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: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; cd16217; EFh_PI-PLCdelta1; 1.
DR CDD; cd13363; PH_PLC_delta; 1.
DR CDD; cd08593; PI-PLCc_delta; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
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_cat.
DR InterPro; IPR046975; PLC-delta1_EF.
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:SF80; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA-1; 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; PF16457; PH_12; 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; 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; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR628391-3};
KW Glycoprotein {ECO:0000256|PIRSR:PIRSR628391-4};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361133};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR628391-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 42..151
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 161..196
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 513..630
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 630..758
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT ACT_SITE 332
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-1"
FT ACT_SITE 377
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-1"
FT BINDING 51..78
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-2"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-3"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-3"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-3"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-3"
FT BINDING 459
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-2"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-2"
FT BINDING 543
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-2"
FT BINDING 570
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-2"
FT BINDING 672
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-3"
FT BINDING 674
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-3"
FT BINDING 698
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-3"
FT BINDING 727
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-3"
FT BINDING 728
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-3"
FT BINDING 729
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-3"
FT CARBOHYD 212
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-4"
FT CARBOHYD 214
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-4"
SQ SEQUENCE 777 AA; 88296 MW; 3AC06C9485B3847B CRC64;
MQCLGIPSRS RSRERYLQEE SLKVAALNGQ RLGLQHDEDL HALLKGSQLL KVKSNSWRRE
RFYKLQEDCK TIWQESRKVM RTPESQLFSI EDIQEVRKGH RTEGLEKFAR DVPEDRCFSI
VFKDQRNTLD LIAPSPAEAQ HWVQGLRKII HHSGSMDQRQ KLQHWIHSCL RKADKNKDNK
MSFKELQNFL KELNIQVDDS YARKIFRECD HSQTDSLEDD EIEAFYKMLT QRAEIDRTFA
EAAGSGETLS VDQLVSFLQH QQREEAAGPA LALSLIERYE PSETAKAQRQ MTKDGFLMYL
LSADGSAFSL AHRRVYQDMG QPLSHYLMSS SHNTYLLEDQ LTGPSSTEAY IRALCKGCRC
LELDCWDGPN QEPIIYHGYT FTSKILLCDV LRAIRDYAFK ASPYPVILSL ENHCSLEQQR
VMARHLRTIL GPMLLDRPLD GVTTSLPSPE QLKGKILLKG KKLGGLLPPG GEGGPEATVV
SDEDEAAEME DEAVRSRVQR KPREDKLRLV KELSDMVIYC KSVHFGGFSS PGTSGQAFYE
MVSFSENRAL RLLQESGNSF VRHNVNHLSR IYPAGWRTDS SNYSPVEMWN GGCQIVALNF
QTPGPEMDVY QGRFQDNGAC GYVLKPAFLR DLNSTFNSRA LAQGPWWTRK RLSIRVISGQ
QLPKVNKNKN SIVDPKVTVE IHGVGRDMAS RQTAVVTNNG FNPWWDTEFE FEVAVPELAL
VRFVVEDYDA SSKNDFIGQS TIPLGSLKQG YRHVHLLSKN GDQHPSATLF VKVSLQD
//
