ID A0A3P8VCH3_CYNSE Unreviewed; 2118 AA.
AC A0A3P8VCH3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-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 Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000010150.1, ECO:0000313|Proteomes:UP000265120};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000010150.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|Ensembl:ENSCSEP00000010150.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; 244447.ENSCSEP00000010150; -.
DR Ensembl; ENSCSET00000010273.1; ENSCSEP00000010150.1; ENSCSEG00000006500.1.
DR GeneTree; ENSGT00940000157356; -.
DR InParanoid; A0A3P8VCH3; -.
DR OMA; KKNYMAY; -.
DR Proteomes; UP000265120; Chromosome 8.
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; 2.60.40.150; 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; 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:UP000265120};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 413..670
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT DOMAIN 1595..1685
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1691..1816
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1965..2064
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1401..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2085..2105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..958
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1401..1419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1539..1582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2085..2099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2118 AA; 236657 MW; 7F52FBF085C7EB6B CRC64;
MASENNQTQT GVVVLAHSSS PTSTCSGPEE EARRADNSEV PKNCGRVLQS KQSSSSTHLL
YRKLSCDREK ETVLAEECCC CCLKCSSEPL CNGKTLCPDV SAAHRSGSLP KEEKTGKSLD
RPGEGGDAGA NRACSTCCSC TMSEISMSPN TSTSGPSSHF TPVHCPHLGS MPSRPCLRHI
RRRSLPVTIE PSSLGSSPCG SPQTNRHYRQ PHRNGRLRHQ HLKDGYSSLE RLDRRPRVKK
YSPLDNTDFV RNHKERSTVL VRRYFKNNKK VTKSVCTGTR AIVRTLPSGR ISEEVREVVV
YHPMCRPSKE DVQSILMRRP KEGSRVCREI NTLDMKLLIS LFPIIIMIPL NSFYCFSPLH
ENANANGTFT TSPTSRPPPE RQLANTMTSS SSLPPNVSGI SKELAELRHL VQFPEEIACI
LTEQEQQLYQ QVFPLDYLCF LTRDLGSPEC QNKRHPNLKA SLSAPNMPTQ STQRSNAVEH
LVMRFNEVSS WVTWLVLTAG SMEEKREVFS YLVHVAKCCW NMGNYNSVME FLAGLRSRKV
LKMWQFMDQS DIDTMRSLKD AMAQHESSSE YKKVLTRAMN IPGCKVVPFC GVFLKELSDA
LDGTASIISL KPSPDPAEGS VEFVSDYSGQ HNFVSRSGSN GLHVPEKEAT VSNILQIIRS
CNRSLEAEDP DEASTSPSFS SRMGLWLNSP GINRISFQIN IGDFFFSFYQ RYVLSLQPDV
HQFLLQGATV IHYDQESHLS ARCLLRLQPD NTTLTWGKPQ SGGASPAEHP LGLGQSVVAG
LAEGLLDLGV VKAVFLGHQG VDVHAVCLQN KLSQMTVEEN GLSLLYGLST TDNRLLHFVA
PSHTAQMLHK GLSELVNSTR KLKKFPDQRL QWLRRQYVSL YQEEGRYEGP TLAQAIELFG
GRRWSMSTSG MEKAGSQKNS INEKAKKKKK ALVRGDSGDA TDDEMFSRKT RSCKEGLNRN
GPESDSIDQE DPDDSFPGPF SLSSTKSHGL LASSSSSSSS SSMAGSNPSR PQSSPILSAS
AKGQPVAWSS RSWHGRGKGC FRGFQNLMMS DTTMSFIQFV ELFKSFSIRS RKDLKELFDT
FAVPYSRSSA ESPPLYTNLR IDDKDTGLQP ELDLLTRNGS DLGLFIRTRQ QMSDNQKQIS
DAIAVASIVT NGTGVENVSL GVLGLAIPQL NDFLVNCQRE HLSYDDILSI IQKFEPSSSM
RQMGWMSFEG FARYMMDKEN FASRNEESLA NEEELNYPLS YYFIESSHNT YLTGHQLKGE
SSVELYSQVL LQGCRSVELD CWDGDDGSPV IYHGHTLTTK IPFKDVVEAV NRAAFVNSDM
PVILSIENHC SLPQQRKMAE IFKTVFGERL VTRFLFESDF SDDPHLPSPV QLRGRILLKN
KKLKAHQAPV DLLKQKAHQL AHMQAQATNG SPGATSPSSH ANEDEEEEED EYDYDYESLS
DGNDKFIVFF SIGTNQCNTK RKHLCSRLQF RFYPLPFKVF DMELGEEFYL PQNKKESRQI
AQELSDLVIY CQAVKFPGLS SLSPSGCGRG KDRNKSRKSI FGTTPTRSSM GEVPTQTRTP
KGTLKDRLSW EEQQTSPVLN PPTSLSAIIR TPKCYHISSV NENAAKRLCR RYSQKLIQHT
ASQLLRTYPA ATRIDSTNPN PLLFWLHGIQ LVALNYQTDD LPMQLNTALF EANGGCGYIL
KPAALWDRSC PLYQQFCPVE RDVEKMSPAV YSLTVVSGQN VCPGNSAGSP CIEVDVLGLP
VDSSHFRTKP IHRNTLNPMW SDVFQFSVYF EDMCFLRFAV VENNSSQTTA QRTLPLKALK
AGYRHVQLRT QHNEQLEVSS LFIFSRRVEE GPTGVATPSS LLFSSEEKRA LQQHRVTVHG
APGPEPFTVF TVTEQTTAKQ LLDTNSSNFY LCEDRVPLLK ERSEVKRTAQ ERPLAPEEEV
LRVVSGWNSD EGYVGRICLK TKDENSNEKI TVMEGEEEMG DMFFVQVHEV SPEQPHTVIK
APRYSTAQDI IQQALSKAKY SYSIVSNPHP CDYVLVEEVT KDVGSKKSCT AKPLQRLLLD
SECVYQAQSR WRGAGRFILK LKEQVPREDK KKVMSFASEL KKLTSRNRSM STGSGVDSPA
QSKDDRAACC VALTELQE
//
