ID O97034_9METZ Unreviewed; 1283 AA.
AC O97034;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma {ECO:0000256|PIRNR:PIRNR000952};
DE EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000952};
OS Ephydatia fluviatilis.
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC Spongillida; Spongillidae; Ephydatia.
OX NCBI_TaxID=31330 {ECO:0000313|EMBL:BAA76275.1};
RN [1] {ECO:0000313|EMBL:BAA76275.1}
RP NUCLEOTIDE SEQUENCE.
RA Koyanagi M., Ono K., Suga H., Iwabe N., Miyata T.;
RT "Phospholipase C cDNAs from sponge and hydra: Antiquity of genes involved
RT in the inositol phospholipid signaling pathway.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates the production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an
CC important role in the regulation of intracellular signaling cascades.
CC {ECO:0000256|PIRNR:PIRNR000952}.
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 EMBL; AB017510; BAA76275.1; -; mRNA.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16201; EFh_PI-PLCgamma; 1.
DR CDD; cd13362; PH_PLC_gamma; 1.
DR CDD; cd09932; SH2_C-SH2_PLC_gamma_like; 1.
DR CDD; cd10341; SH2_N-SH2_PLC_gamma_like; 1.
DR CDD; cd11825; SH3_PLCgamma; 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; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR016279; PLC-gamma.
DR InterPro; IPR035023; PLC-gamma_C-SH2.
DR InterPro; IPR035024; PLC-gamma_N-SH2.
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 InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10336:SF159; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA; 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 Pfam; PF00017; SH2; 2.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF000952; PLC-gamma; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR000952, ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|PIRNR:PIRNR000952,
KW ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR000952};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000952}.
FT DOMAIN 544..644
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 655..749
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 779..839
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 948..1064
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1066..1187
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 516..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 900..942
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1283 AA; 146962 MW; B8733D8831BBB915 CRC64;
MSQIPGAVSG ADIGTILGAL ERGTVMVRFP ARKRRPEKKL FCLKVDTFEV VQYPLTKGTR
TVAEESIDIR EIKEVREGVS SKDFERQPDE TKKVDQYCCF VIYHGTEFRL TTLSVAALCR
DECDAWVKAL KHVTLAGNFA SHLLTHRWLN KEFLALEPSG DNLTIGPIEL KKYVLRISSK
ALLNKARQLF IDFDYSRAGR MGVEDFFNLY HNTIHVKTIG ERFYPFCADR QSLTFSEVQM
FFREEQKDKR ADDTVYLAGL IREYARVPNR TVRDPRLPSL LLPEFVNFLF SKQNSVFAEE
YAQIYQDMDR PISHYWIASS HNTYLTGNQY SSESSCECYS RALRMGCRCI ELDCWDGPDG
NPIIYHGRTL TSKIRFIDVI KTIKDHAFVT SEYPIILSIE QHCDIQQQRI MARQFKEVFG
DALLTELVDL NATRLPSPNA LKRKIIIKHK KLDGTEETSG NNKPEEAGEE EGVTFNSDLC
NSILNGLLFM QDPIDKNWAK HYFVLTEDKL YFTDQQEKDE DEADKTETNT ETLPSTEQHL
KEKWFHGKLA GGRVAAEKLL TDYKDVNGAF LVRESTTFTG DYSLSFVRDG KYNHCRIHTK
SEGGKTRFYL IDQTLFDSIY ELIMHYKSNP LKSPTFEQVL AEPVPQQNSH LGKAWFHENL
SRSEAEEMLK KVRMDGAFLI RPSEQNTKAG QKNYAISFRA EGKVKHCRIE VDESGQYCIG
SAIFDSLTEL VQYYEANPLY RRMRLKYAIN EDLLKSLGEA ESDDVYYHPI YYTFNEEKAT
PITCKALFDY TAVRPDELSF CKDAVITNVE KHGGGWWKGD CGNKNQKWFP ANHVEEVQAD
EVTEDRQLGN LQQGAIDISG CTTEIHHLSS NNLYALKIVP MLKAESTELE KENHMGLMVA
AQSLEEILRW QKAIDEARNK ANSHALAQME KEKERKKDEQ KKRIAIEMSD IIAYCRPVPF
DENKMNDMGK YYNMCSFVET RVEKIVHNKS LAAQFLVHAH TYLNRVYPKG QRLDSSNYDP
VPMWNGGCQM VSLNYQTGDK SMQLNEGKFL QNGKCGYVLM SDCMFEPGFN PLDISTQKTS
PITLSVQIIG GRHLLRQGRG MTCPLVEVEV IGVEVDYNKY RTSTCKENGF NPVWNEGCDF
DINNPALALL RFTVLDEDAF GDANFLGQAV FPVLCLRTGY RSVPLRNAFS EELELCSLLV
HLEMRSAVEE GEELYCTIRS LREDITRMSK QFQHMVREDP ATSCDQLAEI IQEKQMQLRK
LNSARARKPG QAKPALSHIT IPR
//
