ID T2MH83_HYDVU Unreviewed; 1086 AA.
AC T2MH83;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
DE Flags: Fragment;
GN Name=PLCG1 {ECO:0000313|EMBL:CDG71287.1};
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087 {ECO:0000313|EMBL:CDG71287.1};
RN [1] {ECO:0000313|EMBL:CDG71287.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole animals {ECO:0000313|EMBL:CDG71287.1};
RX PubMed=24065732; DOI=10.1093/gbe/evt142;
RA Wenger Y., Galliot B.;
RT "Punctuated emergences of genetic and phenotypic innovations in eumetazoan,
RT bilaterian, euteleostome, and hominidae ancestors.";
RL Genome Biol. Evol. 5:1949-1968(2013).
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 EMBL; HAAD01005055; CDG71287.1; -; mRNA.
DR AlphaFoldDB; T2MH83; -.
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; cd08592; PI-PLCc_gamma; 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; 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; 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 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; PF09279; EF-hand_like; 1.
DR Pfam; PF00169; PH; 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 PRINTS; PR00390; PHPHLIPASEC.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00239; C2; 1.
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; SSF51695; PLC-like phosphodiesterases; 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 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|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361133};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 300..733
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 366..465
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 476..567
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 598..658
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 755..871
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 869..994
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 335..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 728..755
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CDG71287.1"
SQ SEQUENCE 1086 AA; 125556 MW; A7A9EA870EEF3307 CRC64;
LQRANIKLPN NKVKDIYQCH SGKANVFNAT ALCEAYESLI FQSSIADRYE EYLHRSDEGL
FMTAYDFQRF LVDEQKDYKA AKDMSYVHSL MSPCVPDESM KNEIFFTQQQ FLTYLFSPAN
SVFNEEQNKV CQDMTKPLSC YWIASSHNTY LTGDQLQSES SFESYIRCLR MGCRCIELDC
WDGPSEPIIY HGLTLCTKIN FVDVVKAIAT YAFAESEYPL ILSLENHCSI PQQIMMADIF
KKYLGKYLVT QFLDPNETQL PSPESLKRKI ILKNKRLIDD DLGSSIGSRD SLLDEDFLAS
SLKTGLIYME DEDKKWNKHF FVLTSRVLYY SDSKEAAEDD DDNDDENSDA DKKAGGDEDL
HFSEKWFHRN ISRQEAESLL QEYQRGDGSF LVRPSNMFVG DFSLSFWRKN RVQHCHIKSR
PTNDGTAKYF LVGPKGFDNL YSLINHYQTN PLKSDKFELM LTEPVPQPNA HLGKDWYHEN
LTRLQAEEML RRMRKDSYFL VRKRNDGDQN ESYAISFRTG GTIKHCVIKK EGRLFMIGTA
PFESLTELIA HYEKNPLYRK TKLKYPCNQD VVQEFGMNPD GTFNDPEQYV YSQPNLTMPK
QACKAKYDYT AQKEDELSFT KGALIVNIMK YDGGWWRGDY NGHIQKWFPV NFTEEITIPS
KAEEEQAKPV DVLLESQEIG TINLTGCHLQ ILTSRPQRPY VFSLKTSSGE FVCSVDTEQE
MVEWLTCIQR ASTDAENAVN KIRALSEQKN IAKELSDLIV YCVTVPFRET NYENGKHFEM
SSFSEQKLEK YVNKKTSDNR LIKYHQRQLS RVYPRGTRVD SSNYDPVPYW NIGSQMVALN
YQTGDRPMQI NNGLFMNNGR CGYVLKPEYF RDPNFNPHDN NTFKNVEPWN IRLTILGARH
LPKLGRGISS PFVEVEVIDL RSEKDTFRTK TKSDNGFCPT WFDTFDFDVV CPPSAMIRFV
VQDEDMFGDP NFIAQSCLLL TSMKVGHRSI PLLNAYSEEI PLASLLVELK IQNAQDDEEY
SSIAELRDKM QMLIDRNEGT TQSVIDSETE NQLQNYQAQL SMLNTTRRTR HLEEDASKSH
STIHRN
//
