ID A0A158Q9V1_ENTVE Unreviewed; 1894 AA.
AC A0A158Q9V1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN ORFNames=EVEC_LOCUS2884 {ECO:0000313|EMBL:VDD87741.1};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000317601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0000317601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDD87741.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-2018) 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|RuleBase:RU361133};
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DR EMBL; UXUI01007465; VDD87741.1; -; Genomic_DNA.
DR STRING; 51028.A0A158Q9V1; -.
DR WBParaSite; EVEC_0000317601-mRNA-1; EVEC_0000317601-mRNA-1; EVEC_0000317601.
DR Proteomes; UP000038041; Unplaced.
DR Proteomes; UP000274131; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00275; C2_PLC_like; 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; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR001192; PI-PLC_fam.
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 InterPro; IPR000159; RA_dom.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
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; PF09279; EF-hand_like; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF00788; RA; 2.
DR Pfam; PF00617; RasGEF; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SMART; SM00314; RA; 2.
DR SMART; SM00147; RasGEF; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR SUPFAM; SSF48366; Ras GEF; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR PROSITE; PS50200; RA; 2.
DR PROSITE; PS50009; RASGEF_CAT; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Guanine-nucleotide releasing factor {ECO:0000256|PROSITE-ProRule:PRU00168};
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:UP000274131};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 44..307
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT DOMAIN 1214..1384
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1390..1515
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1582..1675
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1761..1857
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 391..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1629..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1852..1879
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 559..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1143
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1894 AA; 212459 MW; 228FDA88A5A3F5A9 CRC64;
MILDIFKTSS GASDLSASQG FIVNDEPITI FRLELERLQF MLQFPEEIAF QLTATEYQLF
YSIQPMDFVR YVSCELTSVP MMENPSPVKN LIKRLSEVSS WITHIIISSP NHDDRKAALL
SIIRMVDTCW NIGNFNGAVE ILMGLKSEKL RPFWLTLSRE EKKRFDQLCE ILLPSNQAAA
SGIYIEAVQR ALNMPQCRVI PFFGIFLRDL YAIVNDMPNV VIMGHERKKE KLEFLNDCNG
EDHFSTRIGV GGLLNADKIQ LVAVVLENIG AFHKHIRKIV KHVDDYVVTH ANGEQIEIKG
YEPVQPVKGG AHGISLIPLD TSLFDLDTVQ RMHHGMTVIN HDLASGRSVL CMMKLDASCS
ILSWHKVHYA SDNHDKETVS TKPSNDKQVV QTQDNVSCAP SPTPSSRPTS GTTVNLEEGF
LDLLSVKSVE RIDSYDIDVE TIYRKHSSED NAVPVYCWAI TYGSHISENE FLYFIGLQET
AHYWLSGLTG VVKHLREQLK QPDRRVLWLK KLYLQLYSES EACVSVSTNE GKGLGGPRPL
DALSAFGGQV DKYRELTETM STKTQGTEPA TPDSSGPKSR LMQMTMAVTR RMRGNSRDCS
RSQSPQPVSS SLRNKPLNMS IRSQASSHSG TVGPNSPALY LKPRSVAAWS EEGGDADSIC
TTRSRSPTAS SYGGRSLGAR STRSWNHTGN LSELLFTPRP RTATNSSFTG RSTGGRSLRS
WKSKGGDISN SGSVSSSGFT SINTQVEKEY HERPLTFVEF IELYRLFSAR LRKDIKDIFN
DCVTTFGVNS HVSKKEKERH SPRVQSRLDS TTSVCPNSSL HDFIPNDVLT RNRLAAQKFT
EKQQKIYKAL AMASVNSMVD MQQTPYLTPT MLKQFCAAYQ MELIDENYAT KLIQEHEPDA
YCRNKQQMTF EGFVRFLNDS RNFAFVPEEI EAECETFNHP LSHYYISSSH NTYLTAHQLK
GESSPEMYRQ ILLTGCRCVE LDCWDGDDGF PQIFHGHTLT SKIFLRQVLD VIKKSAFITS
SLPVILSLEN HCSLQQQAKM AQMIQNYLGD KLVTNFLFES DYSDNPHLPT PYQLQYRILI
KNKKMVFEPS TGLIERSLSR NALRDFPRDQ SKMSYESSLY EDGEDDDLDE FLDDEPDEED
DRTDNADSDK RTMKQPEECK GDTMSSDRDS RRDGRNGLSN FDRSDASTAG SQQFLAPKQV
QRKRIAAGPL APELSDLVIY LQAVKFKGFP KPTTTGGELD EAESTRPPGP VTLRTRANTL
LPTPSPRRTK GGQIENNQKL STDPSSGPRP NVSASCYQVT SLNENAARKK HRSKCTAYSR
NHVVRTYPGG MRIDSSNFNP TQFWAYGFQM VALNFQTSDV PMAVNTAMFE QTGNCGYVLK
PRVLWDEKHP LYGRYNPVSK DPSCYSAMIL TLNIISGQHV FPKQPVGSPY LEVEVIGMPC
DSVKYKSKAE HRNAVNPIWN FLSVFRITCV DLAFLRVAVC DASNGRCYAQ RVVPVRCLRP
GYRHLPLRDG ANHPLDQSML FLFSKFEQEE IIYLFDDNQD FPSNYEQQLT WQTLKADPAA
KVEMIPVLKK QIFILKIIGF YPDDTPIIVR VESSSTVKKV IQSALVKSGK NSDAAEDYVL
IEERVKSPGT STSLDISDGT ENSNQRILPS NEPIMDAVAC WNGFTMRFII RKKNADPGSK
AWISSLIKSG SGQSPLTTNA SASHHELMTY ETGAHFKSHS STQIYEISEL EKSNETLGAP
AGGIHPRARS MGETFLVCIH NVSADQPYAI IRACTSSTAA DIIHQVFLKT SSADLNYNDY
VLVEETADSG RFGTKKICLP SSLSRTTCRV LSPDENVWKA QSKWKSAGRF VLENRKQTVN
QALEKVRSLI EEMEIAQLKA IAVGKSQALQ FSLQ
//
