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Database: UniProt
Entry: A0A218UX42_9PASE
LinkDB: A0A218UX42_9PASE
Original site: A0A218UX42_9PASE 
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
//
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