ID F6YW30_XENTR Unreviewed; 1301 AA.
AC F6YW30;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 3.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma {ECO:0000256|PIRNR:PIRNR000952};
DE EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000952};
GN Name=LOC100496658 {ECO:0000313|Ensembl:ENSXETP00000008782,
GN ECO:0000313|RefSeq:XP_017950677.1,
GN ECO:0000313|Xenbase:XB-GENE-29083287};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000008782};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000008782};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000008782}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_017950677.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_017950677.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_017950677.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_017950677.1; XM_018095188.2.
DR Ensembl; ENSXETT00000008782; ENSXETP00000008782; ENSXETG00000004050.
DR GeneID; 100496658; -.
DR KEGG; xtr:100496658; -.
DR Xenbase; XB-GENE-29083287; LOC100496658.
DR eggNOG; KOG1264; Eukaryota.
DR HOGENOM; CLU_002738_5_0_1; -.
DR OMA; AISFRWY; -.
DR OrthoDB; 2900494at2759; -.
DR TreeFam; TF313216; -.
DR Proteomes; UP000008143; Chromosome 6.
DR Bgee; ENSXETG00000004050; Expressed in 2-cell stage embryo and 12 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; cd16216; EFh_PI-PLCgamma1_like; 1.
DR CDD; cd13362; PH_PLC_gamma; 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; 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; 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; 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 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; PS50003; PH_DOMAIN; 2.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000008143};
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 28..142
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 550..657
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 668..757
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 792..852
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 879..939
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 961..1078
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1077..1202
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT COILED 1234..1288
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1301 AA; 151017 MW; A4E344D6CACDFB8B CRC64;
MFGCRMANLN GLMEEGRGEG TDLGRTLRSL ETGTVLTLFY QKKSQRPERR TFQLRMDTRQ
VVWFRTTEKV EGDIDVREIK EIRPGKNSRD FERYPEDTRK LDATLCFIIL YGTDFRLKTV
SAAAFSEEEV NLWISGLNWV VADTLKAPGP LQIERWLGKQ FNAVDRAREG SVTVKDLKAL
LPQVNYRVPN MRFLRDKMLE IEARSELTFP HFVLFYNNLM FDAQKSIIEQ LELSFPLRNV
DRPSLCQISL YDFQRFLQFD QKEAWAGDIN KVRGYLCNYL KDSDGDVCEP ILQLDEFLTY
LFSKENMIMD SRFEQVVPEE MTYPLSQYWI SSSHNTYLTG DQFSSESSLE AYARCLRMGC
RCIELDCWDG PDDLPIIYHG HTLTSKIKFL DVLHTIKDNA FVTSEYPVIL SIEDHCSVVQ
QRNMAHYFRK VFGDMLLTKP VDINADELPS PAQLKKKILI KHKKLVEGNL YEEVSTASYS
ENDISNSIKN GILYLEDPID HTWSPHYFVL TSNKIYYSEE TSRYQSNDED EEMEPKEEFN
NNELHFSEKW FHGKLGGGRD GRQIAEKLLH EYCTETGGKD GTFLVRESET FVGDYTLSFW
RSSRVQHCRI HSRQEAGSTK FYLTDNLVFD SLYGLISHYR EVPLRCNEFE MRLTDPVPQP
NAHESKEWYH ANLTRLQAEH MLMRVPRDGA FLLRKRSETS SFAISFRAEG KIKHCRIQQE
GRLFMLGSSA EFESLVDLIS YYEKHPLYRK MRLRYPINEE ALEKMGTAEL DYDALFEGRT
PHVYVEANKM PTSRCTVKAL YDYKAQREDE LTFCKQAIIH NVDKQDGGWW RGDYGGKKQL
WFPANYVEET TSAMSPDQDE GSFYFGQSVE NSPLGNFLKG FIDVPSCHIV SSKDGRSSRP
YVFTIHSQQM SHPSQSLDVA ADTQEELNDW IGKIREATQN ADARMQEGKI MERRKKIALE
LSELVVYCRP VPFDEEKIGT EKACYRDMSS FPETKAEKYA NRSKGKKFLQ YNRRQLSRVY
PKGQRLDSSN YDPLPMWICG SQLVALNFQT PDKPMQLNQA LFMLGGQSGY VLQPDIMRDD
LFDPFDKNSL KIVEPITVQL QILGARHLPK NGRSIVCPFI EVEVCGSEFD NSKSKSDVVA
DNGLNPVWMM KQFVFDITNP EFAFLRFVVY EEDMFSDPNF LAQATFSVKG LKTGYRSVPL
RNSYSEELEL ASLLVHIEIV NAKEEDDENL YTSIQQLRDR ASELSSQVSS YERANNCDSR
YQQRLDELRA AQERLMELTE VRNRKLMEKK KRERQLANKR N
//
