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Database: UniProt
Entry: A0A1S3Q470_SALSA
LinkDB: A0A1S3Q470_SALSA
Original site: A0A1S3Q470_SALSA 
ID   A0A1S3Q470_SALSA        Unreviewed;      1515 AA.
AC   A0A1S3Q470;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
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_014034737.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014034737.1};
RN   [1] {ECO:0000313|RefSeq:XP_014034737.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014034737.1};
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_014034737.1; XM_014179262.1.
DR   OrthoDB; 2900494at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa28.
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   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; IPR017946; PLC-like_Pdiesterase_TIM-brl.
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; 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; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 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   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; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 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:UP000087266};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..1515
FT                   /note="Phosphoinositide phospholipase C"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010370305"
FT   DOMAIN          1..176
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50009"
FT   DOMAIN          1105..1195
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          1201..1326
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          435..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          915..972
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1034..1075
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..475
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        930..948
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        949..972
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1515 AA;  169536 MW;  F3590E94EC95212F CRC64;
     MVSLWVTWLI LTAGTMEKKR EVFSYLVHVA KCCWNMGNYN AVMEFLAGLR SRKVLKMWQF
     MDQSDIETMR SLKDAMAQHK SLSEYRKVAL KIPGCKVVPF CGIFLKELSD ALDGAASIIS
     LRHSPHDSPE FVTDYGGQEH FLQRVGPDGL HSHEKEATVS NILQIIRSCN RSLETEKGGH
     HKGFSTSHRN YFMDRNQFVE GDLSDSEGDL SEQAKEVAFQ GTEETHRAFG HGTELIPWYV
     LSLQPDVHQF LLQGSTVIHY DQESHLTARC FLRLEPDNCS LTWANPQSGS TPTDPPGLGQ
     PVVSGLAEGL LDLSVVKAVF MGHQGVDMFA VCLQNKLCNT MRAEENGVSL LYGLHTTDNR
     LLHFVAPRHT ACILYEGLVE LVNAIRKLKK FPDKRLHWLR RQYVRLYWDE GRYEGPTLAQ
     AVKLFGGRCW DMGTEGTEKP SAQKNSSTTK KKKNALVRKY SGDATDDETS QRKTKSCKDT
     LCRNGPELYD SVHQEELEDG FPGPFPAPSC KSPGSLTSGS LAFSPILSGS TKAQPGAWSS
     KSWHGLGKGY FKGFQDLMSS DSTMSFIEFV ELFKSFSIRS RKDLKELFDT YAVPCSSPGP
     ESAPLYTTLR IDDKETGLQP DLDLLTRNGS DLGLFIRTRQ QMSENQKQIS NAIAAASIVT
     NGTGVENASL GVLGMAVPQL NDFLVNCQRK HLTYDGILSI IQTFEPCVSI RQMGWMSFEG
     FARFLMDKEN FASKNEESQV NAEELQYPMS YYYIESSHNT YLTGHQLKGE SSVELYSQVL
     LQGCRSVELD CWDGDDGSPI IYHGYTLTTK IPFKDVVEAI NRTAFVNSDM PVILSIENHC
     SLPQQRKMAE IFKVVFGVKL VSNFLFESDF SDDPLLPSPL QLKGKILLKN KKLTAHQAPV
     DILKQKTHQL AHIKAQTSNG APGGSSPGNH DDDEEEEDEY EDDCESLSDD NILNDKPERK
     SSGDKEDHPI TDEMAKRMKK ADNAVTKYKG KVLDIELEEE LYPPQNKKES RQIAQELSDL
     IIYCQAVKFP GLSTLSHSAS GRRKDRKNRK SVFGMDPGRS GSSPKEAVPG KGSVEGTRLS
     WEEQTSPVLS PNPSVSAVIH TPKCYHISSV NENTAKRLCR RNSEKLILHT TCQLLRTYPA
     ATRIDSANPN PLPFWLHGIQ VVALNYQTDD LPMQLNTALF EANGHCGYVL KPPVLWDRCC
     PLYQQLCSLE RDVESISPTL YSLTIVSGQN VCPANSAGSP CVEVDVMGMP VDSFQFRTKP
     IHRNTLNPMW SEHFRFPVHF EDACFLRIAV VENNSYQTTA QRILPLRALK PGYRHIQLRT
     QHNEPLEVSS LFIYSRRVEE SPTGTALPAA VLFSSEERRA AQQHKVTVHG GPGREPFTVV
     SVKEQTTAGQ LLDTLLMSTD GASEYFLCEE KVSLGKERSD RKRCPQQRPV APEEEIIRVI
     NSWQPEEGYV GRICLKTKEE MAREDKRKGI SFASELKKVT SFSQSVIAPA TQESSRSTDE
     SSRAAYCVPL TEAHE
//
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