ID A0A3Q1EEJ2_9TELE Unreviewed; 1844 AA.
AC A0A3Q1EEJ2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000002711.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000002711.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 STRING; 80966.ENSAPOP00000002711; -.
DR Ensembl; ENSAPOT00000012989.1; ENSAPOP00000002711.1; ENSAPOG00000004229.1.
DR GeneTree; ENSGT00940000157356; -.
DR InParanoid; A0A3Q1EEJ2; -.
DR Proteomes; UP000257200; Unplaced.
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; cd01780; RA2_PLC-epsilon; 1.
DR Gene3D; 2.30.29.240; -; 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; SM00147; RasGEF; 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 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:UP000257200};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1844
FT /note="Phosphoinositide phospholipase C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018792978"
FT DOMAIN 108..363
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT DOMAIN 1314..1404
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1410..1535
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1689..1788
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 619..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1155
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1844 AA; 205902 MW; 33E802C29BA0F2E4 CRC64;
MTTWLTVLHL RLFVLHLFEC PTYSSVEVVI SSKRACENGV CGCVPKNEGC PRFLSFDSFK
FIILSLLPVL SVHPERQLAN SMTSSSSLPP SVSGISKELA ELRHLVQFPE EIACILTEQE
QQLYQQVFPL DYLCFLTRDL GSPECHVKRH PNLKGSLSAP TMPTQSAQRS NAVEDLVARF
NEVSSWVTWL ILTAGSMEEK REVFSYLVHV AKCCWNMGNY NGVMEFLAGL RSRKVLKMWQ
FMDQSDIETM RSLKDAMAQH ESSSEYKKVV TRALNIPGCK VVPFCGVFLK ELSDALDGTA
SIISLKPPPD NTEDSIEFVS DYSGQHNFMS RSGPDGLHVP DKEATVSNIL QIIRSCNRSL
EAEDPDESST SPSSTVSFLP GKNRVLFVVG DLSDSEGDLS LEPIVKEVEF QGTEETHRAF
CHGTELIPWY VLSLQPDVHQ FLLQGATVIH YDQDSHLTAR CLLRLQPDNT TLTWGASPTE
QPPGLGQTVV AGLAEGLLDL SVVKAVFLGH QGVDVHAVCL QNKLCQMTVE ENGLSLLYGV
STTDNRLLHF VAPNYTAQML HKGLSELVNA TRKLKKFPDQ RLQWLRKQYV SLYQEDGRYE
GPTLAQAIEL FGGRRWNMGT GGVEKPGTQK NSPLGINDKS KKKKKVLVRG DSGDATDDEM
VSRKTRSCKE GLYRNGPESD SIDQEDPEDS FPGPFSLSSS KGSGLLASSS SSSSSSSMVG
SNQSRPQSSP ILSGTAKSQP GAWSSRSWHG RGKGCFKGFQ NLMISDSTMS FIEFVELFKS
FSIRSRKDLK ELFDTFAVPC SRSSPESPPL YTNLRIDDKD TGLQPDLDLL TRNGSDLGLF
IRTRQQMSDN QKQISDAIAA ASIVTNGTGV ENASLGVLGL AIPQLNDFLV NCQREHLSYD
EILSIIQKFE PSSTMKQMGW MSFEGFARFL MDKENFASRN EESQMNPEEL QYPLSYYYIE
SSHNTYLTGH QLKGESSVEL YSQVLLQGCR SVELDCWDGD DGMPVIYHGH TLTTKIPFKD
VVEAINRAAF VNSDMPVVLS IENHCSLPQQ RKMAEIFKTV FGERLVTRFL FESDFSDDPH
LPSPLQLRGR ILLKNKKLKA HQAPVDILKQ KAHQLAHMQA QASNGSPGVT SPNNHTNEEE
EEEEDEYDYD YESLSDDNIL DDKPEGKSSA DKEEQPVDEL PKRMKKADNA VQSKGKVFDM
ELGEEFYLPQ NKKESRQIAQ ELSDLVIYCQ AVKFPGLSTL SPAGSGRGKD RGKSRKSIFG
TAPSRCSTTG EVVTQSRTPG RGGSERLSWE EQQTSPVLNP PTSLSAIIRT PKCYHISSVN
ENAAKRLCRR YSQKLIQHTV CQLLRTYPAA TRIDSTNPNP LLFWLHGIQL VALNYQTDDL
PMQLNTALFE ANGGCGYVLK PAVLWDRSCP LYQQFCPMER DVEKMSPAVY SLTIVSGQNV
CPANSAGSPC IEVDVLGMPI DSCHFRTKPI HRNTLNPMWS EHFQFTVHFE EMCFLRFAVV
ENNSSQTTAQ RTLPLKALKS GYRHVQLRTQ HNEPLEVSSL FIYSRRNEEG PTGGATPSSM
LFVSEEKHAS QQHRVTVHGA PGPEPFTVFS VTEQTTAKQL LDMVRNPSEC FLCEEKVPLL
KERSEVKRCA QFRCLAPEEE VVRLVCSWST EEGYVGRICL KTREENLNEK NTVLEGEEDM
TVGYDMFFVQ VHEVSPEQPH TVIKAPRYST AQDIIQQTLS KAKYSYSILS NPNPCDYVLM
EEVTKDAGSK KSSATKPVQR MLLDHECVYQ AQNRWRGAGK FILKLKEQVV MREDNKKKAI
SFTSELKKLT SRSRSMTTGG GVDGPAQSKD DRAACCVALT ELQE
//
