ID A0A3B3QUK7_9TELE Unreviewed; 1674 AA.
AC A0A3B3QUK7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=PLCH1 {ECO:0000313|Ensembl:ENSPKIP00000009808.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000009808.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000009808.1}
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|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 Ensembl; ENSPKIT00000033920.1; ENSPKIP00000009808.1; ENSPKIG00000024765.1.
DR GeneTree; ENSGT00940000157185; -.
DR Proteomes; UP000261540; 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 CDD; cd16205; EFh_PI-PLCeta; 1.
DR CDD; cd13364; PH_PLC_eta; 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; 2.
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; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF51; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE ETA-1; 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; PF09279; EF-hand_like; 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 Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 32..140
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 154..189
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 190..226
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 610..722
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 724..852
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 537..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1464..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1540..1596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1542..1570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1674 AA; 186537 MW; 9C5C6E78EDFB6724 CRC64;
MSSRRINRQG SMQYCRHFLA DNSAFHVERC MSVMQSGTQM VKLKSGSKGL VRLFYLDEHR
SCIRWRPSRK SEKAKITIDS LYKVTEGRQS DIFHRYAEGN FDPGCCFTIY HGNHMESLDV
VTSNPEEART WVTGLRYLMA GISDEDSLAR RQRTHDQWMK QTFEEADRNG DGLLNIEEIY
QLLHKINVNL PRRKVKQMFQ EADTDDQQGT LTYEEFNVFY KMMSLRRDLY LLMMAYSDKK
EYLTAEELGN FLQVEQKMTN ITLEYCLDII DKFEVSDDNK QKFFLGIEGF TNFMRSPTCD
IFNPLHHQVN QDMDQPLCNY YVASSHNTYL TGDQLLSHSK ADMYAWVLQN GCRCVEVDCW
DGPDGDPMVQ HGYTLTSKIT FKSVIETINK YAFINNEYPV ILSLENHCSI QQQKKMARYL
QEILGDKLDL GPVNIKEMKQ LPSPNLLKGK ILIKGKRLPP NLSADAEEGE VSDDDSADEI
EDGFKLKSSS NGHNRHQVES FIRKKLDSLM KESQIGDKED TDSFSIRALL QATHKGLDSN
FKQKANQKEG GKRSQSRSFI SNLKQKRHSK SRLKCQSVDT DEDGQQDGPN KDTGQFHRRR
RKTMKLTRDL STLVVFTNSI IAQESLEEST PSDVLSFSET QAQHLVHQQA ERFVRFNQQQ
LSRIYPSAYR IDSSNFNPQT YWNMGCHLVA LNYQTEGRMM QLNRAKFQVN GDSGYVLKPP
PMCKGSFNPF SSDPLPAYPK KQLVLKIISG QQLPKPPDSM LGDRGEIIDP FVEVEIIGLP
IDCCKEQTRV VDDNGFNPVW EETLSFTLHM AELTLVRFLV WDHDPIGRDF VGQRTVAFSS
LMPGYRHVYL EGLTEASIFI HVAIHDIFGK WSPLILNPSY TILHFLGANK GRQLRGIKGL
FSRSSRSCVD TPLVGPPLCK RSISQQLLRR TASAPAKGRR KTKRPPAPPT EGEDGEGGAP
PPSCPLLPRP ASMPLDKLLQ DTLTLSSPRQ DAHEAGSNPP AETTSVLRPR SSSLNLLLET
PSSYMARPKS PPHVGGEVNP AVRGPHMDRL YDLSLGGEQD RLTDTAEPTQ HRIGQNQPNT
GQTVEEDHLR GETVCGQEGV TTETLESSAG PVNRVNLLSD SSLQDSTLSR LIDAVSLGND
TCGSISALIG QFDVTAELSS VALRSSDHDA SQTPCRTSAC DSCQSSGPSN AVLFSSPETT
DLTIYTILNE EVLSPISEFS PGENTVRSLQ MGSEESTPVA SPAPSPVKPL LTHKPLFSRK
QAPYSRAPEV PCGQNPCFRP IAVREEVTWG SHGGSFHSAA SDRFLLCQDS AGSSLMEIEI
NVDEDPLDVT LTPSSLTHQL AGPRPPSTCG PLNHSPLHHI PGNFPLSSTR TDPHRSPSSW
IHGPTPWRPS HQSRCGHQMG DKHLPAQGTI GHHSGHASSG SRPFPLRINS TMDQAASRSS
SDWPPGSRME NGHFLQQGHP AIGTVVTSLS PSPGPCKSKS LGDLTSEDIS CNFESKYKFI
NRSFMAARAQ SGRQASGPAR CPAPADPLTE QLRRLVSLDQ DEHSQNPDLL TASPLHPLSR
KLSSRSQSRV RHIASRARER QQEALKPRPT SASYSTTGVV LRSKPANHNP PACRHSTGSY
IAGYLEHSEG RGLPEGSCTK SFYANGDQRC HGDASIPVDW CQPSEPEVYF LLRL
//
