ID A0A287AG06_PIG Unreviewed; 2302 AA.
AC A0A287AG06;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:ENSSSCP00000042904.1,
GN ECO:0000313|VGNC:VGNC:91519};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000042904.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000042904.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000042904.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000042904.1}
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|ARBA:ARBA00023674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000256|ARBA:ARBA00023674};
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DR PaxDb; 9823-ENSSSCP00000011172; -.
DR Ensembl; ENSSSCT00000052725.2; ENSSSCP00000042904.1; ENSSSCG00000010483.5.
DR VGNC; VGNC:91519; PLCE1.
DR GeneTree; ENSGT00940000157356; -.
DR Proteomes; UP000008227; Chromosome 14.
DR Bgee; ENSSSCG00000010483; Expressed in omentum and 42 other cell types or tissues.
DR ExpressionAtlas; A0A287AG06; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; IEA:Ensembl.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0032835; P:glomerulus development; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16203; EFh_PI-PLCepsilon; 1.
DR CDD; cd08596; PI-PLCc_epsilon; 1.
DR CDD; cd17229; RA1_PLC-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|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 531..790
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT DOMAIN 1755..1845
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1851..1976
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 2135..2238
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 1052..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1566..1591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1683..1741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2260..2302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2287..2302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2302 AA; 258150 MW; C9E647F8495CBDBC CRC64;
MTSEEMAASV LLPVTQRKVV SAQLAVDESS EKGTDINFPK SLPIRQCGET SHTISQLNTL
TEESSGSNLH TNLSAAKETI MSDENSNEKC WERSMPDSVK NLNINCNNIL KNHQRGLPQS
QFYETCESIT EEDLCLETGI PSPLERKVFP GIQLEMDRPP MGMGPLGTQS AIIEMGRAHP
DSNPTVIHFR YEVDRRMPDT FCPLSDNLVL DDCGNCVLPG VGGEPKKNYL AYTCKLMELA
NNCDNKNRQL QYDPCDPLND KSLCFEASFP KANVLCSRDS FCREDFTDNP PAKTFLSHFE
DFPDNCEDVE EDFLKSKRER STWLVRRFCK NDREVKKSVY TGTRAIVRTL PSGHIGLGAW
SYIDQKRNGL SLPFRRVMGR LSTVVIRQDG RQCLSEAHWY PIYSAVRRGE ETEETIGSLL
HFFTKPSASE TAHERISIGP CLKQCVRDTV CEYRATLQRT SISQYITGSL LEATTSLGAR
SSLLSSFGGS TGRMMLKERQ PGISMANSSA LPSSSAGISK ELIDLQPLIQ FPEEVASILM
EQEQTIYRRV LPVDYLCFLT RDLGTPECQR SLPCLKASIS ASILTSQNGE HNALEDLVMR
FNEVSSWVTW LILTAGSMEE KREVFSYLVH VAKCCWNMGN YNAVMEFLAG LRSRKVLKMW
QFMDQSDLET MRSLKDAMAQ HESSCEYKKV VTRALHIPGC KVVPFCGVFL KELCEVLDGA
SGLMKLCPRY NSQEEALEFV ADYSGQDNFL QRVGQNGLKN SEKESTVNSI FQIIRSCSRS
LEIEEEDSPS EGSSSRKNSL KDKARWQFII GDLLDSENDI FEQPKDWDPH GSEEPQKAFD
HGTELIPWYV LSIQADVHQF LLQGATVIHY DQDTHLSARC FLQLQPDNST LTWIKPTTAS
LASAKAKLGV LSNTSEPGKF PLLGNAGLSG LVEGVLDLFS AKAVYMGHPN IDIHTVCVQN
KLSNMSLSET GVTLLYGLQT TDNRLLHFVA PKHTAKMLFS GLLELTRAVR KMRKFPDQRQ
QWLRKQYVSL YQEDGRYEGP TLAHAVELFG GRRWSTRNPS PGTSAKSAEK PNMQRNNTLG
ISTTKKKKKI LMRGESGEAT DDEMAMRKAK THKECRSRSG SDPQDINEQE ESEANTITSP
PNPLPSRRAH SLTTAGSPNV AAGTSSPIRP VSSPVLSSSN KSPSSAWSSS SWHGRIKGGM
KGFQSFMVSD SNMSFVEFVE LFKSFSVRSR KDLKDLFDIY AVPCDRAGSE PAPLYTNLTI
DENTSGLQPD LDLLTRNVSD LGLFIKSKQQ LSDNQRQISD AIAAASIVTN GTGVESTSLG
VFGIGILQLN DFLVNCQGEH CTYDEILSII QKFEPSVSMC HQGLMSFEGF ARFLMDKDNF
ASKNDESQEN IKELQLPLSY YYIESSHNTY LTGHQLKGES SVELYSQVLL QGCRSVELDC
WDGDDGMPII YHGHTLTTKI PFKEVVEAID RSAFITSDLP IIISIENHCS LPQQRKMAEI
FKTVFGEKLV AKFLFESDFS DDPMLPSPDQ LRRKVLLKNK KLKAHQTPVD ILKQKAHQLA
SMQAQAYNGG SANPPPANNE EEEDEEDEYD YDYESLSDDN ILEDRPENKS CNDKLQFEYN
EEIPKRIKKA DNSACNKGKV YDMELGEEFY LPQNKKESRQ IAPELSDLVI YCQAVKFPGL
STLNASGSSR GKERKSRKSI FGNNPGRMSP GETASFNKTS GKSSCEGMRQ AWEDSSSSVN
PTTSLSAIIR TPKCYHISSL NENAAKRLCR RYSQKLIQHT ACQLLRTYPA ATRIDSSNPN
PLMFWLHGIQ LVALNYQTDD LPLHLNAAMF EANGGCGYVL KPPVLWDKNC PMYQKFSPLE
RDLDSMEPAI YSLTIVSGQN VCPSNSTGSP CIEVDVLGMA LDSCHFRTKP IHRNTLNPMW
NEQFLFRVHF EDLLFLRFAV VENNSSAVTA QRIIPLKALK RGYRHLQLRN LHNEVLEISS
LFINSRRMEE NSSGSPMPAS LMFNTEERKC LQTHRVTVHG VPGPEPFTVF SINGGTKAKQ
LLQQILTIDQ DTKPIATDYF LMEEKYFISK EKNECRKQPF QRAIGPEEEI MQILSSWFPE
EGYVGRIVLK TQQENLEEKS IVQDDKEMIL SSEEESFFVQ VHDVSPEQPR TVIKAPRVST
AQDVIQQTLC KAKYSYSILS NPNPSDYVLL EEVVKDTTNK KSSTPKSSQR VLLDQECVFQ
AQSKWKGAGK FILKLKEQVQ ASREDKRKGI SFASELKKLT KSTKQPRGLT SPAPVLASES
VQNKEEKPAG GLSSSDTVDY RQ
//
