ID A0A401H5W9_9APHY Unreviewed; 1044 AA.
AC A0A401H5W9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SCP_1701610 {ECO:0000313|EMBL:GBE89836.1};
OS Sparassis crispa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Sparassidaceae; Sparassis.
OX NCBI_TaxID=139825 {ECO:0000313|EMBL:GBE89836.1, ECO:0000313|Proteomes:UP000287166};
RN [1] {ECO:0000313|EMBL:GBE89836.1, ECO:0000313|Proteomes:UP000287166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30375506; DOI=10.1038/s41598-018-34415-6;
RA Kiyama R., Furutani Y., Kawaguchi K., Nakanishi T.;
RT "Genome sequence of the cauliflower mushroom Sparassis crispa
RT (Hanabiratake) and its association with beneficial usage.";
RL Sci. Rep. 8:16053-16053(2018).
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|RuleBase:RU361133};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBE89836.1}.
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DR EMBL; BFAD01000017; GBE89836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401H5W9; -.
DR STRING; 139825.A0A401H5W9; -.
DR InParanoid; A0A401H5W9; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000287166; 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; cd13360; PH_PLC_fungal; 1.
DR CDD; cd08598; PI-PLC1c_yeast; 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; 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; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR037755; Plc1_PH.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF36; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA PLC-3; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 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; 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; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000287166};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 301..336
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 743..859
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 854..1024
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1044 AA; 116074 MW; 979EBF33AB6F1912 CRC64;
MLKGTTQLFT HKSAEEAMGP DTGVRSSAGG EGRSTSTLGS TIRQKLQEVK DASRSIAGRR
RSTSSKRSST STQSAGSESS LARSDTPDSL KPHQSAQWRA HESVSMPELP IVEDKEQLSE
HQVLTSSPPP MSPPVADVAV PQLLQQGVPM LKVSAKKQKR FVFRLDADQG QIVWQSKKLK
IIPIENIKEL RAGVDARYYR EQFQLAAEYE ERWLTIVYVL DGGYKTLHLI AATRDVFHLW
DTTLRRLYAV RQKLMSGLGY AEVRQAVWEK QFWRGAGGET EDQKLNFEAV ERMCRRLNIN
PSKEDLMRRF EEADSQGLGY LNFDDFKQFV KALKARPEVD RLYKKITANS GGLMTYGQFE
HFMLSTQKSS LGDSEMQRVF LRFASSPTDE SQDVPSSSLR NSLDLSVQSD FLPAESTERV
PSSSSPVGAD LNTAPSLPPS TVSLSPTIET AVTTLKGFTS FLLSTENSAF ADQHGKICHD
MTRPLPEYFI ASSHNTYLVG HQLVGASTVE GYIRALLHSC RSVELDIYDG DAEPVVYHGR
TLTSKVPLRD VCIAIAKYAF VVSPYPVIIS AEVHCSMPQQ DMIASIMCEE FGAALVRAPI
DGRIEITALP SPEELKGKIL LKAKNLYVSD TDNIREKEVS VDTESSSTEM SASDSDFPSE
VQQEWRKARE NEAEVIKDLK TELQKARGVL GRVRTPRSDS ALSSVSALAS SSVAVLATSP
RLEALDAPAA PQQKVKVRMS LALVALLVYT VGVKCRGLNK KEAYAPVHVF SLSERTANRI
MKQGSTMDLV KHNRGHLVRI YPKGTRIGST NYEPHRFWAT GAQLVAINWQ TFDLGYMINH
AMFQRNGRTG YVLKPLALRS TDKQLLSKRT NHFLDVTIIS AQQLPKPKDT LGRELIEKTV
LDPLVEVSIY IPDWLHISPH ATATFPPVGS KSRQTPSPSS GAAGTQVPAR TVTCRTSVVK
NNGFNPVWEQ RLSLPFDLVG DMRDLVFVRF TVKQEDRLEE EPLAVYCASL GSLNMGYRHL
PLHDSQLSQY LFSTLFVRLN IRDV
//
