ID H0YWG6_TAEGU Unreviewed; 1023 AA.
AC H0YWG6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN Name=LOC100228479 {ECO:0000313|Ensembl:ENSTGUP00000002639.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000002639.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000002639.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000002639.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; H0YWG6; -.
DR STRING; 59729.ENSTGUP00000029127; -.
DR Ensembl; ENSTGUT00000002667.2; ENSTGUP00000002639.2; ENSTGUG00000002570.2.
DR GeneTree; ENSGT00940000164828; -.
DR HOGENOM; CLU_002738_0_1_1; -.
DR TreeFam; TF313216; -.
DR Proteomes; UP000007754; Chromosome 27.
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; cd16206; EFh_PRIP; 1.
DR CDD; cd13364; PH_PLC_eta; 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; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; 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 PANTHER; PTHR10336:SF85; PHOSPHOINOSITIDE PHOSPHOLIPASE C; 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; PF16457; PH_12; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 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 PROSITE; PS50004; C2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
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:UP000007754};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 35..145
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 512..628
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 628..757
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1023 AA; 113659 MW; 90886ACEBA2931A8 CRC64;
MKDGSRQRPP HKKKTVSFSS MPNDRKINST AACISLMLEG CELKKVRSNS RMYSRFFVLD
ADMRSVRWEP SKKDSEKAKI EIKSVKEVRV GKKTPVLRSN GLSDQFPDEC AFSIIYGDNY
ESLDLVASSA DVVSAWVMGL RYLVSYGKHS PEAPGTGHPS LRTSWISSVF DLADLEKSGR
IPVSRAVQLI KALNPGMKTS TIELKFKELQ KASERPGTEV ACDLFVEAYC ELCTRPEIFF
LLVQFSSNKE YLGVKDLLMF LEVEQGMEGV TEEKCLEIVS KYEPSKEGRE KGYLAIDGFT
RYLLSADCSI FDPQHRKVCQ DMAQPLSHYY ISSAHSACLL EDNFWGRSDI SGYISALGLG
CRSIELVLWD GPEGEPVVYT SPSAASCVPF RAVVGLIDQH AFTASAYPLI LCLVVRCSAP
QQRLAAQCLR KTLGEKLYLE PPNPVASYLP SPEELKGRIL IKGKKLPPSC EDSEGEVSDE
EEGWELARRL GQEEREAPEG GGLRRVRLSR ELSELVSLCQ AVPFQDFESS RRGQRYWEMC
SFSEVEAGRF ANECPAELVS YNKRFLSRIY PSPMRIDASN MNPQDFWKCG CQMVAMNYQT
PGLMMDLNAG WFRQNGACGY VLRPAIMREE VSYFSANAKD SLPGVPAQLL HLKVISGQNL
PKPKGSGAKG EVVEPYVCAE IHGIPADCAE HRTKTALQSG DNPIFDESLE FQINLPELAV
LRFVVLDDDY IGDEFIAQYT IPFECLQPGY RHVPLQSLAG EPLPHATLFV HVAITDRRGG
GKGHRRGLAG RRGRRVREYT STKATGIKAI DEVFRTATQP LREATDLREN VQNALVSFKE
LCGLTPAANM KQCILTVSTW LLHSDSAPSV TLNLAEQYPP MEARGPIPDL LRKVLTAYET
MIQTSRTLIE SADAVYGKLI QAQQAGMDFH KELHRIETKE GLRGRKLQKA LESFAWNITV
LKGQADLLKH AKAEALDNLW QIHNAGQSCG IGRNGSASPE PSRLQTPLEP IPETEGGGDT
ASC
//
