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Database: UniProt
Entry: A0A2D0S920_ICTPU
LinkDB: A0A2D0S920_ICTPU
Original site: A0A2D0S920_ICTPU 
ID   A0A2D0S920_ICTPU        Unreviewed;      2222 AA.
AC   A0A2D0S920;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
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|RefSeq:XP_047015538.1,
GN   ECO:0000313|RefSeq:XP_047015539.1, ECO:0000313|RefSeq:XP_047015540.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_047015539.1};
RN   [1] {ECO:0000313|RefSeq:XP_047015538.1, ECO:0000313|RefSeq:XP_047015539.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_047015538.1,
RC   ECO:0000313|RefSeq:XP_047015539.1};
RG   RefSeq;
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   RefSeq; XP_017338936.1; XM_017483447.1.
DR   RefSeq; XP_047015538.1; XM_047159582.2.
DR   RefSeq; XP_047015539.1; XM_047159583.2.
DR   RefSeq; XP_047015540.1; XM_047159584.2.
DR   STRING; 7998.ENSIPUP00000016635; -.
DR   KEGG; ipu:108273837; -.
DR   Proteomes; UP000221080; Chromosome 13.
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; 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; 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   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          467..720
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50009"
FT   DOMAIN          1691..1781
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          1787..1912
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          2064..2169
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   REGION          248..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          979..1077
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1089..1117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1533..1563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1618..1679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2192..2222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..767
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        979..1001
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1045
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1052..1077
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1089..1112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1539..1563
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1664..1679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2222 AA;  247205 MW;  9F31E665CFAF61D7 CRC64;
     MRVCVEEQVG IGLPSISVSS EKAAVILGVG MEARAASSLT KFRNQMLSFG YEAHERRNSD
     PLMFCSCSHS LHPAEDCCDS KSSEQIRMDC GTRSPLDSRS KSLDSLDYLH KDCCCSTVSC
     RRVEGLCCSQ PCSTCGPVET DGCCQEAAVH SGGWESGFPR RTEGFSSAAT RLAGESPSLD
     EERLGTRRIS LATLFLSRFH CTCAYGARLE AGTQGQVNFN SAHCHNGVFS SLERLNKRSK
     VRCSRMPCQA STTSKPSLAH QHSDGEATAS DSEFTHKKER STVLVRRYLK NNQKVLKKVC
     TGTRAIVRTG HISDRAWQAA YGRRCRLSKA YTFVDTEYSR VLHAIQLQVS RALLSYSGVR
     LEQLQYAFPA LNAEVHLLHP SRKLLARAVA WLPTCVQHTE HRVCSCRTRL AAHLSGALME
     ATAAITTSTP MFKERQLCGS TASSGSLSSG VMGISKELAD LRQLIQFPEE IASILTEQEQ
     QLYRRVLPLD YLCFLTRDLA SPDCHKSHPH LKASLSAPVM PTQSSQHNVV EDLVARFNEV
     SSWVTWLILT AGSMEEKREV FSYLVHIAKC CWNMGNYNAV MEFLAGLRSR KVLKMWQFMD
     QADIETMRGL KDAMAQHESS SEYKKVVNRA LNIPGCKVVP FCGVFLKELS EALDGAASLI
     GLRPAFDSQE DSIEFVSDYN GQQHFLQRAG ADGLHNSEKE ATVSNILQTI RSCNRSLEAD
     EPEDAFRDRS KNQRASDSGR VLFLVGDLSD SEGDLTEQPR ESDLQSPEEP EGAFSHGTEV
     VPWYILSLSA DMHRFLLQGA TVIHYEQESH LTARCLLRLQ PDNCTLTWIK PPSSRSRGVV
     PDSLLQGQVA VCGLAEGILD LSAVKAVFMG HPGVDINVVR LQHKLCGLSA EENGVTLLYG
     LHTTDNRLLH FVAPWHTASV LYEGLRELIS GIRKMKRFPD QRLQWLRRQY VSLYQEDGRF
     EGPTLAQAIE LFGGRRWNMG SGSRSTEKTT TQKNSPLGIS SNVKKKKKAL VRGDSGDGTD
     DEMVSRKTKS CKEGLSRRSS DPVDSVEQEE NDDSSSFGTP GSSFSSSTKT QSPGSSSFSS
     PFCSSSINSS TPIRPHSSPV LPCTSKGQPG AWSSRSWHGR GKGCFRGFQN LMISDSIMSF
     VEFVELFKSF SIRSRKDIKE LFDTYAVPCT RSGPDSVPLY TTLRIDDKIT GLQPDLDLLT
     RNGSDLGLFI RTRQQMSENQ KQISDAIAAA SIVSNGTGVE HSSLGVLGLA IPQLNDFLVN
     CQREHLTYDE ILTIIQKFEP SSSMRQMGWM SFEGFARFLM DKDNFASKNE ESQVNSDELQ
     YPLSYYYIES SHNTYLTGHQ LKGESSVELY SQVLLQGCRS VELDCWDGDD GMPVIYHGHT
     LTTKIPFKDV VEAINRSAFV NSEMPVILSI ENHCSLPQQR KMADIFKVVF GDKLVTKFLF
     ESDFSDDPLL PSPWQLRGKI LLKNKKLKAH QAPVDILKQK ALQLAHMQAQ ANNCTVAAGS
     LGNNEEEEEE EDEYDYDYES LSDADVLNAS TASYSQEDNI LDDKPEGKSS TEKLQYESND
     EMPKRIKKAG SKGKMFDMEL GEEFYLPQNE KESRQIAQEL SDLVIYCQAI KFPGLSTHSP
     SCSNRGKERK SRKSIFGNAP VRGSPGEPVT LVRGSGKASM DGARSSWEEQ TMPTTGTTPS
     LSAIIRTPKC YHISSVNENA AKRLCRRYSA KLIGHTERQL LRTYPAATRI DSANPNPLCF
     WLHGIQLVAL NYQTDDLPMQ LNTALFEVNG HCGFVLKPPV LWDRTCYLYH QFSPLERDLE
     HMSPTVYSLT VVSGQNVCPG NSNGSPCVEV EVLSLPADAC HFRTKPIHRN TLNPMWSESF
     TFQVHFEDLT FLRLAVVENN SSQVTAQRIL PLKALKPGYR HLQLRNQHNE ALEVSTLFLF
     SRKTEESPDG GARPAVVLFS SEERRVAQQH KVTVHGAPGP EPFTVLSMKE HTTAKQLLNV
     LVPDASADYF LMEEKIPLSK EKCDAKKVPQ QRPLASDERV LKVLHSWQPE EGYVGRLCLK
     AKEENLNEKN DKMERAEEAS SGGDEDVFFV QVHDVSPEQP RTVIKAPRYS TAQDIIQQAL
     SKAKYSVSIL SNPNPSDYVL MEEVGREAPG KKVSSAKPAQ RVLPDHECVF QAQSKWKGPG
     KFILKLKEQI GREDKRKCVS FASELWKLTG RSRSVTMNGP GSSEAAHSKE ERGAPPPPDT
     LD
//
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