ID A0A0N1PIM8_PAPXU Unreviewed; 515 AA.
AC A0A0N1PIM8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 22-FEB-2023, entry version 28.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN ORFNames=RR46_00180 {ECO:0000313|EMBL:KPJ20609.1};
OS Papilio xuthus (Asian swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPJ20609.1, ECO:0000313|Proteomes:UP000053268};
RN [1] {ECO:0000313|EMBL:KPJ20609.1, ECO:0000313|Proteomes:UP000053268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPJ20609.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ20609.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
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:KPJ20609.1}.
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DR EMBL; LADI01005407; KPJ20609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1PIM8; -.
DR STRING; 66420.A0A0N1PIM8; -.
DR Proteomes; UP000053268; Unassembled WGS sequence.
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 Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10336:SF6; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE EPSILON-1; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF00788; RA; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00149; PLCYc; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR PROSITE; PS50200; RA; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000053268}.
FT DOMAIN 81..249
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 251..381
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 415..503
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 57323 MW; BEC4DAA950AAB7C8 CRC64;
MSNQSAGSSL TEYFSDEDYD EDDEDIDEKE LHKILNSMEE KVGRTSLSFY QSLRRSDGDG
DAGGSIKHAN RKRSNQIARE LSDMVTYVQA IKFRGLNPLS PRSSVKHAGG AGSAGRHVTD
TSAPASSFES SESSDIAQSQ SATPRARCLN APAVHHPCYR CSSINEAMGR KICRKHPLAL
IAHTETQLVR TYPAGLRIDS SNFDPVTFWS CGVQLVALNY QTEDAAMAVN AAMFEGHGCA
GYVRKPHVMW DPGHIAYRRF NPMDKEFDGI HAAHLTLAVI SGQYVAENVY SFYNAFVEVE
ILGVPADCKK IRTKVARRNA LNPVWNETFN FKINFPELAF VRFEIYDADT NYMLSQRVIP
LHCLRPGYRH VRLRSPTNQP LNMASLLIFS RCSEESAGES WRGDAEPGSP RQRRRIHFLV
VYAVARHEPY SILKVTQDTT ANEAIAQCLS KGGVCRSARG SYVLVEEVAS RAPTQRVLGP
HERVLRAATA RPAARLLLKR VGDDPSSRAW LTSIR
//
