ID A0A3B3I6D7_ORYLA Unreviewed; 2269 AA.
AC A0A3B3I6D7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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|Ensembl:ENSORLP00000039359.1};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000039359.1, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000039359.1, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000039359.1,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000039359.1}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000039359.1};
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; 8090.ENSORLP00000039359; -.
DR Ensembl; ENSORLT00000040602.1; ENSORLP00000039359.1; ENSORLG00000005200.3.
DR GeneTree; ENSGT00940000157356; -.
DR InParanoid; A0A3B3I6D7; -.
DR Proteomes; UP000001038; Chromosome 19.
DR Bgee; ENSORLG00000005200; Expressed in bone element and 14 other cell types or tissues.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
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; 2.60.40.150; 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; 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:UP000001038};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 505..760
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT DOMAIN 1732..1822
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1828..1953
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 2119..2215
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1530..1567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1585..1610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1657..1719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1534..1551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1677..1719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2269 AA; 252498 MW; 07A1782A416AF7FD CRC64;
MMATEEHQMQ AGPDMLSKRS SPPSIGSRPL RDKALTSSGQ EVWRGCDQLW LSKQRSSPSL
LFYRKLSCES VNGVHSAEEC VEYSYSSQIL STKEKPLPEP SADKNCEGMK NILGDSESTK
PDRTSSSHVP SDHSTSVYTN SDSKSSPSFC TSCPNKRHIR RGSLPVSMLA FYKTSSHRSF
PGEPSSEPGS LASSPCGSPR LNHRQHPHQG NLKDGFSSLE RLNRRPRVQK CPLEKLFLPR
SLAATMTLDS SFPGTISCGR DSSNEEEDEE APLDEAEFLR NRKDRSTVLV RRFFKNNQKV
TKSVCAGTIA IVRTLPSGHI SDDVWGIVVD HRCWHPSKKD VWSVLQRGEE LRGCRGILHF
DKAKLQQVNN YVKSREECSL IHPANKLLLS WPGCVHLRDP PRPLNVVNNS SARPDLHHRC
DPARFYLACG WRTSLCSLLT GAILEATVAI GARSSLLCPP PQCPNSHAVL KERQLANSMT
SSISLPQNVS GISKELAELR HLIQFPEEIA CILTEQEQQL YQQVLPLDYL CFLTQDLGSP
ECQIKRHPNL KASLSAPNMP TQSPRRSNAV EDLVARFNEV SSWVTWLVLT AGTMEEKREV
FSYLVHVAKC CWNMGNYNGV MEFLAGLRSR KVLKMWQFMD QSDIETIRSL KDAMAQHETS
SEYKKVMTRA LNIPGCKVVP FCGVFLKELS DALDGTASII SLKQSPDNTD DSVEFMSDYS
GQHHFMTRSG PDGLHVPEKE ATVSNILQII RSCNRSLEAD DPDDTSSSPS SGTTLAFRSN
SLKDRYRNQM APDTSCVLFT VGDLSDSDGD LSVEPVIKEV EFQGTEETHK AFSHGTELIP
WYVLSLQPDV HQFLLQGATV IHYDQDSHLT ARCLLRLQPD NTTLTWGKPQ SGGASPTEQP
LGLGQTVMAG LAEGLLDLGV VKAVFLGHQG VDVQAVCLQN KLSQMTVEEN GLSLLYGLST
TDNRLLHFVA PNHTARMLHR GLSELVNASR KMKRFPDQRL QWLRRQYVSL YQEDGRYEGP
TLAQAIELFG GRRWNMGTAG VEKPGGQKNS PLSINDKSKK KKKVLARGDS GDATDDEMVS
RKTRSCKEAL NRNGPESESV DHEDPDDSFP GTLSLSSSKS PGLLASSSSS SSSSSMTGSN
HCRPQSSPVL SGTSKSQPGA WSSRSWHGRG KGCFKSFQNL MISDSTMSFI EFVELFKSFS
IRSRKDLKEL FDTFAVPCSR SCSESPPLYT KLRIDDNDTG LQSDLDLLTR NGSDLGLFIR
TRQHMSDNQK QISDAIAAAS IVTNGTGVEN ASLGVLGLAI PQLNDFLVNC QREHLSYDEI
LSIIQKFEPS SVMRQMGWMS FEGFARFLMD KDNSASRNEE SQMNPEGLQY PLSYYYIESS
HNTYLTGHQL KGESSVELYS HVLLQGCRSV ELDCWDGDDG MPVIYHGHTL TTKIPFKDVV
EAVNRSAFVN SDMPVILSIE NHCSLPQQRK MAEIFKNVFG ERLVTRFLFE SDFSDDPHLP
SPLQLRGKIL LKNKKLKAHQ APVDILKQKA HQLAHMQAQA SNGSPGVSSP HNHNNEDEEE
EEDEYDYDYE SLSDDNLLDD KADAKNSVDK EELHADDIPK RMKKPDSAVQ SKGKVFDMEL
GQEFYLPQNK KESRQIAQEL SDLVIYCQAV KFPGLSTLSP AGSSRGKDRG KSRKSIFSAA
PSRSSAAGEV TSQSRTPGKG SSERLSWEEQ QTSPVLNPPT SLSAIIRTPK CYHISSVNEN
AAKRLCRRYS QKLIQHTACQ LLRTYPAATR IDSTNPNPLQ FWLHGIQLVA LNYQTDDLSM
QLNTALFELN GGCGYVLKPA VLWDRTCPLY QQFCPMERDT ENMSPASYSL TVVSGQNVCP
GNSSGSPCIE VDVLGMPVDS HHFRTKPIHR NTLNPMWSEQ FHFAVHFEEL CFLRFAVVEN
NSSQTTAQRT LPLTALKPGY RHVQLRTQHN ESLEVSSLFI YSRRTDEGPI GGATPSSLLF
SSEERHLSQQ HKVTVHGAPG PEPFAVFCIT DQTTAKQLLD TVVATTGNPS AHILCEEKVP
LLKERSEVKR CAQYRFLAPE EEVVRLVSSW DMEEGYVGRI CLKTKEENLN EKNTELETEE
ETTAGSKDGA AGEEDMFFVQ VHEVSPEQPH TVIKAPRYST AQDIIQQTLS KAKYSLSNSN
PSEYVLVEEV TKDSASKKSS ATKPLQRVLL DHECVFQAQS RWRGAGKFIL KLKDQVVRED
KKKVISFASE LKKLTSRSRS MTTGVGVDGP GQSKEERAAC CVALTELQE
//
