ID D7MQG5_ARALL Unreviewed; 548 AA.
AC D7MQG5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN ORFNames=ARALYDRAFT_685532 {ECO:0000313|EMBL:EFH42544.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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:ARBA00001195,
CC ECO:0000256|RuleBase:RU361133};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL348720; EFH42544.1; -; Genomic_DNA.
DR RefSeq; XP_002866285.1; XM_002866239.1.
DR AlphaFoldDB; D7MQG5; -.
DR STRING; 81972.D7MQG5; -.
DR EnsemblPlants; Al_scaffold_0008_2352; Al_scaffold_0008_2352; Al_scaffold_0008_2352.
DR Gramene; Al_scaffold_0008_2352; Al_scaffold_0008_2352; Al_scaffold_0008_2352.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_002738_3_2_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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 InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
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:SF162; PHOSPHOINOSITIDE PHOSPHOLIPASE C 5; 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; PF00388; PI-PLC-X; 2.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 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; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 2.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 313..399
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 400..530
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 225..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 62838 MW; D0C05F727D301E2B CRC64;
MKREMGRYKM GLCFSDKLRM NRGAPPPDVV TAFVEYTEGR NHMTAEQLCR FLVEAQDETE
VLVSDAEKII ERITCERHHI TKFLRHTLNL DDFFSFLFSD DLNHSIDSKV HQDMASPLSH
YFIYTSHNSY LTGNQINSEC SDVPLIKALK RRVRALELDL WPKSTKDASA TLLGGWLPPD
LQAKAAEMMK EIFMDMVYFP EAGGLKEFPS PEDLKYKIVI STKPPKGNLK RDKDSESDVS
GKASSDFSDD QVDDGKTEEE TSEAKNEEEG FDQESSNLDF LTYSRLITIP SGNAKNGLKE
ALTIDNGGIR RLSLREQKFK KATEMYGTEV MKFTQKNLLR IYPKATRVNS SNYRPYNGWM
YGAQMVAFNM QGYGRALWMM HGMFRGNGGC GYVKKPDFMM KNGLGGEVFD PKAKLPIKTT
LKVKVYMGKG WDSGFQRTCF NTWSSPNFYT RVGITGVRAD KVMKKTKKEE KTWEPFWDEE
FEFQLTVPEL ALLRIEVHDY NMPEKDDFSG QTCLPVSELR QGIRSVPLYD RKGERLVSVT
LLMRFHFV
//
