ID A0A3Q1DA38_AMPOC Unreviewed; 1133 AA.
AC A0A3Q1DA38;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
GN Name=PLCH2 {ECO:0000313|Ensembl:ENSAOCP00000027896.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000027896.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000027896.1}
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};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR AlphaFoldDB; A0A3Q1DA38; -.
DR STRING; 80972.ENSAOCP00000027896; -.
DR Ensembl; ENSAOCT00000020463.1; ENSAOCP00000027896.1; ENSAOCG00000017471.1.
DR GeneTree; ENSGT00940000158374; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00275; C2_PLC_like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF146; PHOSPHOINOSITIDE PHOSPHOLIPASE C; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF16457; PH_12; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00233; PH; 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 PROSITE; PS50004; C2; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361133};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 119..227
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 238..273
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 274..310
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 618..732
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 733..862
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 20..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..573
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..999
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 128777 MW; 41A679A2325A4D87 CRC64;
MGQESRNQMY SSGMNISPAM APMSPGLTGS PPLPSQSPKK TTFQSLGSLS SGVFSPSLGK
DSPHAARQAS FDSPIPSIMS SPKLWHKASI SRLAEEFFWI GGSVVCVSLC SPIVERCMCT
MQTGTQMTKL KGKKKGLVRF FYLDEHKSCI RWRPSRKHDK AKITIDSIHE VCEGKKSEIF
RRYADNRFDP NCCFSIYYGE RVKSLDLVST NSEEARTWIT GLKYLMAGIS DEDSLARRHR
TWLQQTFSEA DKNGDGTLSI GEVHQLLHKL NVNLPKQKVR EMFQEADTDE NQGSLAFEEF
CSFYKMISTR RDLYLIMISY SNQKEVMDLH DLARFLENEQ KMRGLTREHL VDIVAKFEPC
PVNLQRMVLG IDGLTNYMRS PAGDIFNPEH NQVNQDMTQP LCNYFISTSH NTYLTGDQLL
SQSRVEMYAY VLQAGCRCVE VDCWDGPDGE PIIHHGYTLT SKILFKDVVE TINKYAFTKS
QYPVILSIEN HCTVPQQKKM AEYLKEVLQD KLDLTNVNAH ECKKLPSPEI LKGKVLVKGK
KLPVNLDPDA EEGDVSDEDT EDEEEEDDDD DNSQFDCFRM GTMLRQLISQ KRKDDLADQS
LGASRERKRK TMRLSRALSD LVKYTKSVRV HDIETQAYTN SWQVSSLNET VMNQILQLKP
AELVRLNQRQ LLRVYPSNYR VDSSNFNPQP YWNAGCHMVA MNYQTQGRML ELNQAKFSSN
GNCGYILKPK CMCKTAFNPA LEDPLPGHRK TQLVLKIISG QQLPKPKDSM FGDRGEIIDP
FVEVEIIGLP IDCSKQQTRV VDDNGFNPMW EETLVFNIQM PQIALVRFQV WDHDPIGRDF
IGQRTVAFRS MMPGYRHVYL EGMAESSIFV HVAINDITGK VGCFKNKNCF DLETSSQHSC
PDDPAPYSQN PLIQEELEES EFPESNCEEQ QTLQKSETEQ PEPSEELPPE PEPEPEPDKD
VAPEPEQPET QSQTDSRPQP QSVPWPETKP LPLIPPPSPV RVRRTLEAPA TPRPSTPIRT
KARSRSCPRK QTTSPQTPMV NHKLDFHWQK QRVKNYGSYS NQVRRIPNGL CLSDSASSSS
DGSTDSLEFV ASCVSAEVEQ HEGTLQREMK ALFDQKMREI HCKSPLFPES EHN
//
