ID A0A3B3CU13_ORYME Unreviewed; 1449 AA.
AC A0A3B3CU13;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000021337.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000021337.1}
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 Ensembl; ENSOMET00000030980.1; ENSOMEP00000021337.1; ENSOMEG00000023278.1.
DR GeneTree; ENSGT00940000157356; -.
DR Proteomes; UP000261560; Unplaced.
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 5..242
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT DOMAIN 856..1019
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1025..1150
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1299..1395
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 261..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1449 AA; 162499 MW; B5AAADC7938881BB CRC64;
LPLDYLCFLT QDLGSPECQI KRHPNLKASL SAPNMPTRSP RRSNAVEDLV ARFNEVSSWV
TWLVLTAGTM EEKREVFSYL VHVAKCCWNM GNYNGVMEFL AGLRSRKVLK MWQFMDQSDI
ETIRSLKDAM AQHESSSEYK KVMTRALNIP GCFMSDYSGQ HHFLTRSGPD GLHVPDKEAT
VSNILQILHF VAPNHTARTL HRGLSELVNA SRRMKKFPDQ RLQWLRRQYV SLYQEDGRYE
GPTLAQAIEL FGGRRWNMGT AGVEKPGAQK NSPLSINDKS KKKKKVLARG DSGDATDDEM
VSRKTRSCKE ALYRNGPESE SVDQEDPDSF PGPFSLSSSK SPGLLASSSS SSSSSSMTGS
NHSRPQSSPV LSGTSKSQPA WSSRSWHGRG KGCFKSFQNL MISDSTMSFI EFVELFKSFI
RSRKDLKELF DTFAVPCSRS CPESPPLYTK LRIDDSDTGL QSDLLLTRNG SDLGLFIRTR
QHMSDNQKQI SDAIAAASIV TNGTGVENAS LGVLGLAIPQ LNDFLVNCQR EHLSYDEILS
IIQKFEPSPA MRQMGWMSFE GFAFLMDKDN CASRNEESQM NPEELQYPLS YYYIESSHNT
YLTGHQLKGE SSVELYSHVL LQGCRSVELD CWDGDDGMPV IYHGHTLTTK IPFKDVVEAV
NRSAFVNSDM PVILSIENHC SLPQQRKMAE IFKNVFGERL VTRFLFESDF SDDPHLPSPL
QLRGKILLKN KKLKAHQAPV DILKQKAHQL AHMQAQASNG SPGVSSPNTH NNEDEEEEED
EYDYDYESLS DNILDDKLDA KNSVDKEELP ADDIPKRMKK PDSAVQSKGK VFDMELGQEF
YLPQNKKESR QIAQELSDLV IYCQAVKFPL STLSPAGSGR AKDRGKSRKS IFSAAPSRSS
AAGEVTTQSR TPGKNPPTSL SAIIRTPKCY HISSVNENAA KRLCRRYSQK LIQHTVCQLL
RTYPAATRID STNPNPLQFW LHGIQLVALN YQTDLSMQLN TALFELNGGC GYVLKPAVLW
DRTCPLYQQF CPMERDTENM SPANYSITQV VSGQNVCPGN SSGSPCIEVD VLGMPVDSHH
FRTKPIHRNT LNPMWSEQFH FAVHFEELCF LRFAVVENNS SQTTAQRTLP LTALKPYRHV
QLRTQHNEPL EVSSLFIYSR RTEEGPIGGA TPSSLQLFSS EEKHLSQQHK VSVHGAPGPE
PFTVFCVTEQ TTAKQLLDMH VLCEEKVPLL KERSEVKRCA QYRFLAPEEE VVRLVSRWDM
EEGYVGRICL KTKDELETEE ETTLASKDGG GGEEDMFLVQ VHEVSPEQPH TVIKAPRYST
AQDIIQQTLS KAKYSLSNPN PSEYVLVEEV TKDSASKKAS ATKPLQRVLL DHECVFQAQS
RWRGAGKFIL KLKDQVVRED KKKVISFASE LKKLTSRSRS MATGVSADGA GQSKEERAAC
CVALTELQE
//
