ID A0A218UX42_9PASE Unreviewed; 2303 AA.
AC A0A218UX42;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN Name=PLCE1 {ECO:0000313|EMBL:OWK58208.1};
GN ORFNames=RLOC_00002476 {ECO:0000313|EMBL:OWK58208.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK58208.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK58208.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK58208.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) 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};
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:OWK58208.1}.
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DR EMBL; MUZQ01000106; OWK58208.1; -; Genomic_DNA.
DR STRING; 299123.ENSLSDP00000024093; -.
DR Proteomes; UP000197619; 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 CDD; cd16203; EFh_PI-PLCepsilon; 1.
DR CDD; cd08596; PI-PLCc_epsilon; 1.
DR CDD; cd17229; RA1_PLC-epsilon; 1.
DR CDD; cd01780; RA2_PLC-epsilon; 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; IPR046973; PLC-epsilon1_cat.
DR InterPro; IPR028398; PLC-epsilon1_RA2.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR046974; PLC_epsilon1_EF.
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; 1.
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; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
PE 4: Predicted;
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:UP000197619};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 550..803
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT DOMAIN 1764..1854
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1860..1985
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 2145..2248
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 1073..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1568..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1691..1720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1572..1587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2303 AA; 257920 MW; 53CFF220650A1806 CRC64;
MRIGGEDPPP IPSTHPATRD CVKMTSEEMT ASVLLSVVQG KVIAAQSAGD ENTENALDTS
VIRRHAASSG RQTTHNLSYL HRLEEESLQG SVPKIFPLAK EQLANDKSNE NFWERNSSIS
DSVEFLNINC NVVQKNYKSN ISCSQLYQSC APLAGEEACL ETGIPVSLER AMLAEIQLKM
NGPSLRSQTA VNKNDSSDPD KVAFFHLHCA SERNISKALC GLHNSFILDD CLQPVSDGDG
NTTGSPACTC SIMQLTNNCE NKNGQQLYED ALRDKYLCLE RAPQKVKVAC SGHSFCGNNF
TGRMPSKPFL SHFKDCNDNC EEELEEDFFR NKKERSTLLI RRFCKNDKEV KKSVYTGTRA
IFRTLPLGHI GTVAWNYVEQ RRNNCGMKIS RITTEQLTII QSLIKWKFNS SPEKSLWYEI
FSTVTEEEEG AEDIFEYIPH LLRKLPISVT DCIYKGDGFC VKPCVTGAYC QYRATLQRTA
LSNYITGALL EATTSLGARS GLLNIFGGST GRTMLKERQA CTSMAGSSVL PSSMAGISKE
LLELQHLIQF PEEVASILTE QEQELYRKVL PIDYLCFLTR DLGSAECQSK LPSLKASISA
TILSSHNGEH NAVEDLVTRF NEVSSWVTWL ILTAGSMEEK REVFSYLVHV AKCCWNMGNY
NAVMEFLAGL RSRKVLKMWQ FMDQSDIETM RSLKDAMAQH ESSSEYRKVV NRALNIPGCK
VVPFCGVFLK ELCEVLDGAS SLIRLCPRYN SQDETLEFVS DYSGQDNFLQ RVGQDGLNNP
EKESTTNNIF QTIRSCSRSL ESEEGEDNVS EGSNSRKNSL KDKNRYQFLI GDLSDSESDI
FEQLKEWDTS STEEQQKAFC HGIELIPWYV LSIRADVHQF MQQGATVIHY DQDTHLSARC
FLQLQPDNST LTWTKPTTVC PANAKAKLGV MGNTAELGKY QFLGNTGLVE GFLDLFSAKA
VYMGHSGIDM HTVCVQNKLC NMSLEENGIT LLYGLQTTDN KLLHFVAPKY TARMLYDGLL
ELTKAVRKMR RFPDQRLQWL RKQYVSLYQE DGRFEGPTLA QAVELFGGRR WSARSTGTGS
LTKSTEKPNV QRNNTLGINT AKKKKKVLIR GESGEATDDE MATRKAKSCK EYRNRSGSDP
QDIDEQEEPD QNIIINASPS NNLPSRRAHS LTASGSPNLG ATSSSPARPV SSPVISSSKS
QSSTWSSSSW HGRVKGGMKG FQNFMVSDSN MTFVEFVELF KSFSVRSRKD LKDLFDVYAV
PCNRSGLEPA PLYTNLKIDE NSSGFQPDLD LLTRNVSDLG LFIKSRQQLS DNQRQISDAI
AAASIVTNGT GVESTSLGVF AVGIQQLNDF LVNCQGEHCT YDEILSIIQK FEPSVNMCQQ
GLLSFEGFAR FLMDKDNFAS KNDESQENAE DLQFPLSYYY IESSHNTYLT GHQLKGESSV
ELYSQVLLQG CRSVELDCWD GDDGMPIIYH GHTLTTKISF KEVVEAIERN AFITSDMPVI
ISIENHCSLP QQRKMAEIFK LVTKFLFESD FSDDPMLPSP GQLRRKILLK NKKLKAHQTP
VDILKQKAHQ LAHLQAQASN GASNPTPTNE EEEDEEDEYD YDYESLSDDN ILEDRPENKL
SSDKLQFEYN EENAKRLKKA DTYNNKGKVY DMELGEEFYL PQNKKESRQI APELSDLVIY
CQAVKFPGLS TLNPSGSSRG KERKSRKSIF GNNPGRLSPG ESAALAKASG KGPFDAMRQT
WEDPCSPYNS PASLSAIIRT PKCYHISSLN ENAAKRLCRR YSQKLIQHTT CQLLRTYPAA
TRIDSSNPHP LIFWLHGVQL VALNYQTDDL PLQLNAAMFE ANGGCGYVLK PPVLWDKNCS
MYQHFCPLER DLDNKEPAIY SLTIVSGQNV CPSNSTGSPC IEIDVLGMPL DSCHFRTKPI
HRNTLNPMWN EQFLFRVHFE DLVFLRFAVV ENNCSAVTAQ RIIPLRALKR GYRHVQLHNL
HNETLEISSL FINSRRMEES PSGNSLPASM LFSPGERKAA VTYKVTVHGI PGPEPFTVFS
VSAGATAAQL LHQILATIKG TESCAADYFL MEEKSFISKE KSECKKPPFQ RVIGPEEGLV
QLLNSWFPEE GYVGRIIFKT REENLNERNV FQEAKEEAAI SSEDDSFFVQ VHDVSPEQPR
TVIKAPRLST AQDVIQQTLC KAKYSYSILS NPNPSDYVLL EEVTKEPANK KSSTSKPSQR
ILSDQECVFQ AQSKWKGAGK FILKLKEQVQ AARDDKRKGI SFTSELKKLT KSSKQYRGFV
PAALSDGAQG REERAAAFSD SAE
//