ID A0A099YV34_TINGU Unreviewed; 997 AA.
AC A0A099YV34;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
DE Flags: Fragment;
GN ORFNames=N309_12127 {ECO:0000313|EMBL:KGL74059.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL74059.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL74059.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL74059.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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};
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DR EMBL; KL886610; KGL74059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099YV34; -.
DR STRING; 94827.A0A099YV34; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
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; 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; 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; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
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:SF79; 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 PRINTS; PR00390; PHPHLIPASEC.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 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; SSF50729; PH domain-like; 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 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000053641};
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}; Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 314..421
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 432..521
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 556..616
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 637..697
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 719..836
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 850..974
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL74059.1"
FT NON_TER 997
FT /evidence="ECO:0000313|EMBL:KGL74059.1"
SQ SEQUENCE 997 AA; 114853 MW; BD5B981C854E53A3 CRC64;
PELCQISLYD FQKFLLHDQK ESWASDVSTV RDYMCSYLKD CSIEAADPSF QLDEFLTYLF
SKENMVMDSK YERVVPEEMN HPLSQYWISS SHNTYLTGDQ FSSESSLEAY ARCLRMGCRC
IELDCWDGPD DLPIIYHGHT LTSKIKFLDV LHTIKEHAFV TSEFPIILSI EDHCSIVQQR
NMASHFKKVF GDMLLTKPVD INADELPSPT QLKKKILIKL LSLRSFPFFV EGNLYEEVST
ASYSENDISN SIKNGILYLE DPIDHTWSPH YFVLTSNKIY YSEETSRYQF NEDEEEVEQK
EEFNNNELHF TEKWFHGKLG GGRDGRQIAE KLLHEYCTET GGKDGTFLVR ESETFVGDYT
LSFWRSNRVQ HCRIHSRQEA GTTKFYLTDN LVFDSLYSLI CHYREVPLRC NEFEMRLTDP
VPQPNAHESK EWYHANLTRL QAEHMLMRVP RDGAFLVRKR SEPNSYAISF RAEGKIKHCR
IQQEGRLFML GSSAEFESLV DLVSYYEKHP LYRKMKLRYP INEETLEKMG TTPQGSVPKP
GTPEEQAVMP MSLSSVAQCT VKALYDYKAQ REDELSFCKQ AIIHNVDKQD GGWWRGDYGG
KKQLWFPANY VEEIVNAQAQ EQDEASSENS PLGNFLKGFI DVPSCHVVIS KDGRSSKPFV
FTIHSQQMSH AAQSLDVAAD TQEELSEWVA KIREATQNAD ARMQEGKIME RRKKIALELS
ELVVYCRPVP FDEDKIGTDK ACYRDMSSFP ETKAEKYANR SKGKKFLQYN RRQLSRIYPK
GQRLDSSNYD PLPMWICGSQ LVALNFQTPD KPMQLNQALF MLGGRSGYVL QPDIMRDETF
DPFDKNSLKI VEPITVQLQA RQLGLSLLLL LLQILGARHL PKNGRSIVCP FVEVEVCGSE
YDSSKNKTDV VADNGFNPVW LFKQFVFDIN NPEFAFLRFV VYEEDMFSDP NFLAQATFPV
KGLKTGYRSV PLKNSYTEEL ELAALLIHIE IINAKVG
//
