ID A0A3P8YB22_ESOLU Unreviewed; 1227 AA.
AC A0A3P8YB22;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 22.
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 Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000013281.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000013281.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000013281.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3P8YB22; -.
DR STRING; 8010.ENSELUP00000013281; -.
DR Ensembl; ENSELUT00000021784.2; ENSELUP00000013281.2; ENSELUG00000013508.2.
DR GeneTree; ENSGT00940000157517; -.
DR Proteomes; UP000265140; LG19.
DR Bgee; ENSELUG00000013508; Expressed in head kidney and 14 other cell types or tissues.
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; 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; cd11969; SH3_PLCgamma2; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 3.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
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; IPR035723; PLCgamma2_SH3.
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:SF25; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00388; PI-PLC-X; 2.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF000952; PLC-gamma; 2.
DR PRINTS; PR00390; PHPHLIPASEC.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
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 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
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 Reference proteome {ECO:0000313|Proteomes:UP000265140};
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 497..601
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 612..701
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 728..788
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 893..1005
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 999..1127
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 1227 AA; 143036 MW; 70D0F68D500FB80F CRC64;
MAGLGRSQRG ELTEYKKSLI KRDLEMGVVM TVFRQKAERL TVQVIMETRQ VAWTRTADKT
DGVLDLFEIR EIRPGRNSKD FERFRDGKDK HAENTCFTIF YGSQFVLNTL SVGADSVDDA
EKWLTGLELL RQETLVAPTP DIIESWLRKQ MYSVNQTKKN SISLKELKSL LLLLNFKVPC
TRYLKEKFSE IGARKDVLDF EQFHKLYNIL MFEQKDILEE FKRESCAFIL GNTDKPDASA
VLLQDFQRFL LYQQKESWAS ELNQVRELMT TFIDDTMRKT NDPEFTVSEF LSFLFSKENS
IWDEKYSEVC NLDMNNPLSH YWINSSHNTY LTGDQLRSES STEAYVRCLR LGCRCVECCW
SVGVRYPLVL SIEEHCCVEQ QRQMARIFKE VFQDKLLTDP VELMAEQLPS PAQLKGKIIL
KHKKLSVEGG ISRKDFRKGE KQGDLHIWDP VDQRWNKHYC VISDDKLYYV QNEKHFRSDP
DKPMIICSSD LHTSEPWFHG RMSEGRQTAE RLLQEFCAES GGRDGTFLVR ESDTFVTDFT
LSFWRSGRVQ HCRIRSGSDG NKTFYFLTDN LHFPSVYLLI QHYREMPLRC HDFDLRLTDA
VPRPNPHLLE GWFYSNLSRG EAEDYLLRIP RDGAFLIRQR EEGDSYAITF RGDGKVKHCR
IQKDGAMYVL GTTTEFQSLV ELVNYFRKKP LYRKIKLRYP VTLELVNHFS KVREGLDSWG
WGGAGQLEPK STIKALYDYR AMRPDELSFC KGALIHNVSK ESDGWWKGDY GGKVQQFFPA
NYVEEVFHNM TAESKEQVME DNPLGDMCKG IVDISKCNVV RSAKNGKSHV LTLQINEDHS
GMHFDFAAES LEDLFEWYQV AWDITQREIT KKHNMELEQQ EEVEKNEEVA MEMSDLVVYC
QPRSKEKERF GNYDYKEIRS FVENKVPAKN KTPQFLKYNR KALSRIYPKG QRVDSSNYDP
YPLWACGCHM VALNFQTADK YTQLNSALFS LNGRTGYVLQ PEMMRSDSYD PQIEKKKVKF
TLTVRVIAAR HLPKPGRSIA SPFVETELLG HTEENKFKTI VYRDNGLNPV WKAPPEPVMF
PIHEPELTFL RFVVNEEDMF SDPNFLAQAT FPVKGIRSGY RSVPLKNGFN ESIELASLLV
YIDMQQVEKA EEELYSSSSQ LRRRQAELSN ELFLYDTHTS LQRSALPQVR DDLMREFSTN
EKQLEKIQDT CRQKIKEKKI NNSRFYS
//
