ID F2E8Y0_HORVV Unreviewed; 577 AA.
AC F2E8Y0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
OS Hordeum vulgare subsp. vulgare (Domesticated barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=112509 {ECO:0000313|EMBL:BAK03802.1};
RN [1] {ECO:0000313|EMBL:BAK03802.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seed {ECO:0000313|EMBL:BAK03802.1};
RX PubMed=21415278; DOI=10.1104/pp.110.171579;
RA Matsumoto T., Tanaka T., Sakai H., Amano N., Kanamori H., Kurita K.,
RA Kikuta A., Kamiya K., Yamamoto M., Ikawa H., Fujii N., Hori K., Itoh T.,
RA Sato K.;
RT "Comprehensive sequence analysis of 24,783 barley full-length cDNAs derived
RT from 12 clone libraries.";
RL Plant Physiol. 156:20-28(2011).
RN [2] {ECO:0000313|Proteomes:UP000011116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Morex {ECO:0000313|Proteomes:UP000011116};
RX PubMed=23075845; DOI=10.1038/nature11543;
RG The International Barley Genome Sequencing Consortium;
RA Mayer K.F., Waugh R., Brown J.W., Schulman A., Langridge P., Platzer M.,
RA Fincher G.B., Muehlbauer G.J., Sato K., Close T.J., Wise R.P., Stein N.;
RT "A physical, genetic and functional sequence assembly of the barley
RT genome.";
RL Nature 491:711-716(2012).
RN [3] {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.1HG0015110.1}
RP IDENTIFICATION.
RC STRAIN=subsp. vulgare
RC {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.1HG0015110.1};
RG EnsemblPlants;
RL Submitted (JAN-2022) 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|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}.
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DR EMBL; AK372605; BAK03802.1; -; mRNA.
DR AlphaFoldDB; F2E8Y0; -.
DR EnsemblPlants; HORVU.MOREX.r3.1HG0015110.1; HORVU.MOREX.r3.1HG0015110.1; HORVU.MOREX.r3.1HG0015110.
DR Gramene; HORVU.MOREX.r2.1HG0011560.1; HORVU.MOREX.r2.1HG0011560.1; HORVU.MOREX.r2.1HG0011560.
DR Gramene; HORVU.MOREX.r2.1HG0011560.1.mrna1; HORVU.MOREX.r2.1HG0011560.1.mrna1; HORVU.MOREX.r2.1HG0011560.1.
DR Gramene; HORVU.MOREX.r3.1HG0015110.1; HORVU.MOREX.r3.1HG0015110.1; HORVU.MOREX.r3.1HG0015110.
DR OrthoDB; 882863at2759; -.
DR Proteomes; UP000011116; Chromosome 1H.
DR ExpressionAtlas; F2E8Y0; baseline and differential.
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; 1.
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:SF36; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA PLC-3; 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; 1.
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; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 2: Evidence at transcript level;
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:UP000011116};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 345..431
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 428..559
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 256..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 65508 MW; F781DF5355ECA7CE CRC64;
MTTYRVCCFL RRFRPASNEP TEAICDVFQA YAGADGALRE EALRRFLREV QREAGDDDVE
AVAREAMAFA AEHRLLKKGG GLTVKGFHRW LCSDANAALH PRRGVHDDMG LPLSHYFIYT
GHNSYLTGNQ LSSGCSEVPI AKALRDGVRV IELDLWPNAA KDDVEVVHGR TWTSPVNLMK
CLEAIKEHAF VSSPYPVILT LEDHLTPHLQ AKVAKMIKET FGDLLHLSDS EAMPVFPSPE
DLRGKILIST KPPKEYLETK TSKEEAQNGS TEEESVWGDE IPDSKAQVSE KDTEQYVEED
EEMEMQGQLG VNEEYKSLIS IPLTRRKHDM DQDLKVDPEK VSRMSLGEAA YEKATITHGS
EIIKFTQRNL LRIFPKTTRI TSSNYNPLMG WTYGAQMVAA NMQGHGRKLW LTQGMFRANG
GCGYVKKPDF LMKTDKMFDP RSELPVKTRL KVTVYMGDGW RFDFRKTHFD KCSPPDFYAR
VGIAGVVADT TMKETKVIKD NWIPTWDQEF EFPLAVPELA LLRVEVHESD NHQKDDFAGQ
TCLPVWELRS GIRSVRLYAR DGEVLRSVKL LMRFEFS
//
