ID D7ELR5_TRICA Unreviewed; 1210 AA.
AC D7ELR5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 2.
DT 27-MAR-2024, entry version 94.
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=AUGUSTUS-3.0.2_04220 {ECO:0000313|EMBL:EFA12319.2};
GN ORFNames=TcasGA2_TC004220 {ECO:0000313|EMBL:EFA12319.2};
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA12319.2, ECO:0000313|Proteomes:UP000007266};
RN [1] {ECO:0000313|EMBL:EFA12319.2, ECO:0000313|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA12319.2,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=18362917; DOI=10.1038/nature06784;
RG Tribolium Genome Sequencing Consortium;
RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT "The genome of the model beetle and pest Tribolium castaneum.";
RL Nature 452:949-955(2008).
RN [2] {ECO:0000313|EMBL:EFA12319.2, ECO:0000313|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA12319.2,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=19820115; DOI=10.1093/nar/gkp807;
RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT for Tribolium castaneum.";
RL Nucleic Acids Res. 38:D437-D442(2010).
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; KQ972349; EFA12319.2; -; Genomic_DNA.
DR AlphaFoldDB; D7ELR5; -.
DR STRING; 7070.D7ELR5; -.
DR EnsemblMetazoa; TC004220_001; TC004220_001; TC004220.
DR eggNOG; KOG1264; Eukaryota.
DR HOGENOM; CLU_002738_5_0_1; -.
DR InParanoid; D7ELR5; -.
DR OMA; YMRNPLY; -.
DR Proteomes; UP000007266; Unassembled WGS sequence.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0060429; P:epithelium development; IEA:UniProt.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IBA:GO_Central.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16201; EFh_PI-PLCgamma; 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; 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); 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: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; 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|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:UP000007266};
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 23..139
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 551..652
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 663..752
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 784..846
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 943..1059
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1054..1185
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 515..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1210 AA; 140417 MW; 5196117F9B2248AC CRC64;
MFNGAFSPSP GSGYIPEMEQ IISQLERGTL VMKYSLRKKA EHKTLAIRRE TRQIVWTRPA
TNSKPVHDGA VDLRKIKEIR LGKSSKDFDK WADDSKKIEN LKCFVVYYGS EFKLRVLSIA
ALSEKECELW VKGLRYLVKD TINVPYPLQV QVWLRREFYA MENPTETINI KDLKAFLPRI
NYKIPTNKLR ELFNEVDTRK RAEIGFDDFA VLYQKIIFDE SNGAEIFDKL ALYSSNLKSV
SLQEVQSFLA KEQNDDLSND DRAVSRFICD FLKDPQREVQ EPHFTISEFL DYLFSKQNDL
WDPNKDSVHQ DMSKPLSHYW IASSHNTYLT GDQLSSESSV EAYARCLRMG CRCIELDCWD
GPDGMPFIYH GHTFTTKIKF MDVIKTIKEH AFATSEYPVI LSIEDNCSLP QQRKMATAMQ
EVFGESLLTH PVEKNEKQLP SPYQLRRRII LKHKKLPEGQ DESSSILIRH EGSEMDLRSS
FRNGIMYLED PVDKEWNPHF FVLTENKLFY TDSYKPDQES ERSEDEDDSA AAFHRSKSDV
PNEELHFSEK WFHGKLANGR EEAEQLLKAY SHLGDGTFLV RASVTFVGEY CLSFWRNGQV
NHCRIRSKPD KQHTRYYLTD AKYFDSLYSL ITHYRNCPLV TAEFSITLQE PVPQPKKHET
EEWYHKHTGK MQADEILRRV KMEGAFLVRP SENDANCYTI SFRADKKIKH CRIKLEGRLY
TIGNVEFESL VELINYYENH PLYRRVKLSY PISEEAVKRM TMEQDDNVGY NSSPSYMDPS
AFTPPKITVK ALYDYRAQQP DELSFCKHAI ITNVTKPENS PGWWRGDYGG MKQHFFPANY
VMELDRMESQ DGSDDGSGES MLQGQLDMNG AVVDLIHHPE RPGLEWVVKI VTSTACTPLE
VALQSREMAV EWMLAIKEVA QRACALENHH REMERTFRIA KEMSNLIIYC RSITFNIERA
RQQGFIFYEM SSFPETKAEK LMCQQEKKFF VKYHQHQFSR VYPKGQRVDS SNYNPINMWN
IGSQMVALNY QTGDKPMQLN QAKFRDNGNC GYLLKPDFMF RDDFDPADRN TLVGVEPWIV
TLRIIAARHL FRPKKGTASP FVEVEVIGAP FDSGTKLSTK PVTDNGFNPR WMEEVIEFPV
YNPYFALLRF VVQDEDVFGE PNFIGQATYP VTCLRTGYRS VWLKNAYSED LELASLLIHI
SIKRTSVSPS
//
