ID A0A091DKX6_FUKDA Unreviewed; 776 AA.
AC A0A091DKX6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
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 ORFNames=H920_07681 {ECO:0000313|EMBL:KFO30950.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO30950.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO30950.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO30950.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; KN122353; KFO30950.1; -; Genomic_DNA.
DR RefSeq; XP_010628002.1; XM_010629700.2.
DR AlphaFoldDB; A0A091DKX6; -.
DR STRING; 885580.ENSFDAP00000022683; -.
DR GeneID; 104865913; -.
DR CTD; 5333; -.
DR eggNOG; KOG0169; Eukaryota.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
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:UP000028990};
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 512..629
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 629..757
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 542
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-2"
FT BINDING 569
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-2"
FT BINDING 671
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-3"
FT BINDING 673
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-3"
FT BINDING 697
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR628391-3"
FT BINDING 726
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
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 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 776 AA; 88440 MW; 8F89C1EAA5D6215A CRC64;
MQCLGVRSRR RSRELYLREQ SLKVAALNGQ RLGLQDDKDL QALLKGSQLL KVKSSTWRRE
RFYKLQEDCK TIWQESRKVM RSPESQLFSI EDIQEVRMGH HTEGLEKFAR DVPEDRCFSI
VFKDQRNTLD LIAPSPADAQ HWVLGLRKII HHSGSMDQRQ KLQHWIHSCL RKADKNKDNK
MSFKELQNFL KELNIQVDDS YARKIFRECD HSQTDSLEDE EIEVFYKMLT QREEIDYTFA
EAAGSGETLS VDQLVTFLKH QQKEEEAGPA LALSLIERYE PSETAKAQHQ MTKDGFLMYL
LSADGNAFNL LHRRVYQDMS QPLSHYLVSS SHNTYLLEDQ LTGPSSTEAY IRALCKGCRC
LELDCWDGPN QEPIIYHGYT FTSKILFCDV LRAIRDYAFK ASTYPVILSL ENHCSLEQQR
VMARHLCAIL GSMLLDQPLD GVTSDLPSPE QLKGKILLKG KKLGGLLPPG GEGGPEATVS
DEDEAAEMED EAVRSRVQHK PKEDKLRLVQ ELSDMVIYCK SVHFGGFSGA GPSRQAFYEM
ASFSENRALR MLQESGNSFV RHNVGHLSRI YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ
TPGQEMDVYQ GRFQDNGACG YVLKPDFLRN LNTTFSARAL TQGPWWAPKR LTVKIISGQQ
LPKVNKNKNS IVDPKVTVEI HGVGRDMASR QTAVITNNGF NPRWNTEFEF EVVVPELALI
RFVVEDYDAS SKNDFIGQST IPWNSLKQGY RHIHLLSKNG DQHPSATLFV KIALRD
//
