ID A0A267GY31_9PLAT Unreviewed; 945 AA.
AC A0A267GY31;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=BOX15_Mlig021267g1 {ECO:0000313|EMBL:PAA90199.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA90199.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA90199.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA90199.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA90199.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAA90199.1}.
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DR EMBL; NIVC01000124; PAA90199.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267GY31; -.
DR STRING; 282301.A0A267GY31; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
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:SF36; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA PLC-3; 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 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; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 649..769
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 800..940
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 539..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 945 AA; 105220 MW; D5DE4C73CDC846C8 CRC64;
MEVLLALLPA PVYYAVIAGF LLTCLQLFGP DICWALSCLW ERSERLGIRH RVHTGTGLAA
LTHAFTISTE PSLVPLTLPL LFEIGEDEDD RKFAYLGKRG GWKPAWIEFE QHNKSLVLRK
LRPSAASIAK NKTRKIVALE SLQRISAEAA DNDAEYSPDS PIAVSLHRSA SEGGWPLRLL
ARSPQAACRW LQQLLVNLLS VRPDLSVPRP LVTEQALTDR LKLVCQAEAP SFSVDLLALL
LKEFGVFAKR TDLKSFLQKT MNKQKIETYR ETMDAAKEVL GQMAGLEIFQ RYATGKSNGC
LITVPDFHQN FATNSQGLRQ NLAETLNQLR SIATVDSNLL DLMLITRRLF KDILASKIYT
LPLRTDQLEL RQPLSQPMTD YFISTSHNTY LMEDQLKGRS DCLAYEIALK KNCRCVELDI
HNGPNGDPII THGGTMTSRI RFEDVIKTIK RFAFVASEYP LILSFENHCS LEQQDKMAQI
LTKHLKDYLY VDESSDHMER LPSPEELKWK IIIKNKKTQQ EPGASATFYV AATAPTASPQ
AANAAACTED DSDGDESDGE VSNSSPASSP QGGRRSISGP MASAEGDIAG GASGSESSDL
QASPPMPQNR RSSIDKSVSV GGPTVAASAA TAVGAMGKKR KKLKVSTSLS DMVSICRPVK
FKGQKYAKEN YRPVEMSSLT ESKVEKKQWL KKDGEDANRM VLHTQYQLVR VYPSGLRTNS
SNYNPINAWR LGCQLVALNY QTRCESMELN DGLFQLNGSC GYVPKPAILT EPDTKFNPFS
PSPELARSLR LEIISGVNLR QPASQQEQQL HQHAQPPQEQ QQQQQLQCQG ASERTDSSEE
KTASSPYVKV TLFGVPGDEK KDQTKKADQG FNPRWLYRCF EDNEVVRVPE LAHLRLEVKD
KSSGKVIGQF TTPLTAFNKG YRRVNLKDSR DSPTASELWI YIELR
//
