PLCD1_RAT
ID PLCD1_RAT Reviewed; 756 AA.
AC P10688; Q80WI4; Q9QVD3; Q9QVD4; Q9QVD5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000269|PubMed:16000311};
DE AltName: Full=Phosphoinositide phospholipase C-delta-1;
DE AltName: Full=Phospholipase C-III;
DE Short=PLC-III;
DE AltName: Full=Phospholipase C-delta-1;
DE Short=PLC-delta-1;
GN Name=Plcd1 {ECO:0000312|RGD:3346};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3390863; DOI=10.1016/0092-8674(88)90548-x;
RA Suh P.-G., Ryu S.H., Moon K.H., Suh H.W., Rhee S.G.;
RT "Cloning and sequence of multiple forms of phospholipase C.";
RL Cell 54:161-169(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SHR MET-412; SER-423; ASP-463 AND
RP ALA-668.
RC TISSUE=Aorta;
RX PubMed=1684614; DOI=10.1097/00004872-199111000-00004;
RA Yagisawa H., Tanase H., Nojima H.;
RT "Phospholipase C-delta gene of the spontaneously hypertensive rat harbors
RT point mutations causing amino acid substitutions in a catalytic domain.";
RL J. Hypertens. 9:997-1004(1991).
RN [3]
RP PROTEIN SEQUENCE OF 50-57; 128-140 AND 728-738.
RC TISSUE=Brain;
RX PubMed=1313009; DOI=10.1016/s0021-9258(19)50458-6;
RA Kanematsu T., Takeya H., Watanabe Y., Ozaki S., Yoshida M., Koga T.,
RA Iwanaga S., Hirata M.;
RT "Putative inositol 1,4,5-trisphosphate binding proteins in rat brain
RT cytosol.";
RL J. Biol. Chem. 267:6518-6525(1992).
RN [4]
RP PROTEIN SEQUENCE OF 61-76, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP MUTAGENESIS OF HIS-311; ASN-312; LEU-320; GLU-341; ASP-343; HIS-356;
RP PHE-360; GLU-390; LYS-438; LYS-440; SER-522; ARG-549; TYR-551 AND TRP-555.
RX PubMed=9565585; DOI=10.1074/jbc.273.19.11650;
RA Ellis M.V., James S.R., Perisic O., Downes C.P., Williams R.L., Katan M.;
RT "Catalytic domain of phosphoinositide-specific phospholipase C (PLC).
RT Mutational analysis of residues within the active site and hydrophobic
RT ridge of plcdelta1.";
RL J. Biol. Chem. 273:11650-11659(1998).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16000311; DOI=10.1074/jbc.m500629200;
RA Nomikos M., Blayney L.M., Larman M.G., Campbell K., Rossbach A.,
RA Saunders C.M., Swann K., Lai F.A.;
RT "Role of phospholipase C-zeta domains in Ca2+-dependent
RT phosphatidylinositol 4,5-bisphosphate hydrolysis and cytoplasmic Ca2+
RT oscillations.";
RL J. Biol. Chem. 280:31011-31018(2005).
RN [7]
RP INTERACTION WITH TGM2.
RX PubMed=12054611; DOI=10.1016/s0006-291x(02)00197-3;
RA Kang S.K., Kim D.K., Damron D.S., Baek K.J., Im M.J.;
RT "Modulation of intracellular Ca(2+) via alpha(1B)-adrenoreceptor signaling
RT molecules, G alpha(h) (transglutaminase II) and phospholipase C-delta 1.";
RL Biochem. Biophys. Res. Commun. 293:383-390(2002).
RN [8]
RP GLYCOSYLATION AT SER-191 AND THR-193.
RX PubMed=24098488; DOI=10.1371/journal.pone.0076399;
RA Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.;
RT "Discovery and confirmation of O-GlcNAcylated proteins in rat liver
RT mitochondria by combination of mass spectrometry and immunological
RT methods.";
RL PLoS ONE 8:E76399-E76399(2013).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-130.
RX PubMed=8521504; DOI=10.1016/0092-8674(95)90219-8;
RA Ferguson K.M., Lemmon M.A., Schlessinger J., Sigler P.B.;
RT "Structure of the high affinity complex of inositol trisphosphate with a
RT phospholipase C pleckstrin homology domain.";
RL Cell 83:1037-1046(1995).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 205-756.
RX PubMed=8784353; DOI=10.1038/nsb0996-788;
RA Grobler J.A., Essen L.-O., Williams R.L., Hurley J.H.;
RT "C2 domain conformational changes in phospholipase C-delta 1.";
RL Nat. Struct. Biol. 3:788-795(1996).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 133-756.
RX PubMed=8602259; DOI=10.1038/380595a0;
RA Essen L.-O., Perisic O., Cheung R., Katan M., Williams R.L.;
RT "Crystal structure of a mammalian phosphoinositide-specific phospholipase C
RT delta.";
RL Nature 380:595-602(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 133-756, AND CALCIUM-BINDING.
RX PubMed=9062102; DOI=10.1021/bi962466t;
RA Essen L.-O., Perisic O., Lynch D.E., Katan M., Williams R.L.;
RT "A ternary metal binding site in the C2 domain of phosphoinositide-specific
RT phospholipase C-delta1.";
RL Biochemistry 36:2753-2762(1997).
CC -!- FUNCTION: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC by activated phosphatidylinositol-specific phospholipase C enzymes
CC (PubMed:16000311). Essential for trophoblast and placental development
CC (By similarity). Binds phosphatidylinositol 4,5-bisphosphate (By
CC similarity). {ECO:0000250|UniProtKB:P51178,
CC ECO:0000250|UniProtKB:Q8R3B1, ECO:0000269|PubMed:16000311}.
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:0000269|PubMed:16000311};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000269|PubMed:16000311};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O =
CC 1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433;
CC Evidence={ECO:0000250|UniProtKB:P51178};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000250|UniProtKB:P51178};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 5 Ca(2+) ions per subunit. Two of the Ca(2+) ions are bound
CC to the C2 domain.;
CC -!- SUBUNIT: Interacts with TGM2. {ECO:0000269|PubMed:12054611}.
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DR EMBL; M20637; AAA41886.1; -; mRNA.
DR EMBL; S74591; AAP31521.1; -; mRNA.
DR PIR; B28821; B28821.
DR RefSeq; NP_058731.1; NM_017035.1.
DR PDB; 1DJG; X-ray; 2.60 A; A/B=133-756.
DR PDB; 1DJH; X-ray; 2.50 A; A/B=133-756.
DR PDB; 1DJI; X-ray; 2.50 A; A/B=133-756.
DR PDB; 1DJW; X-ray; 2.45 A; A/B=133-756.
DR PDB; 1DJX; X-ray; 2.30 A; A/B=133-756.
DR PDB; 1DJY; X-ray; 2.80 A; A/B=133-756.
DR PDB; 1DJZ; X-ray; 2.95 A; A/B=133-756.
DR PDB; 1MAI; X-ray; 1.90 A; A=11-140.
DR PDB; 1QAS; X-ray; 2.40 A; A/B=135-756.
DR PDB; 1QAT; X-ray; 3.00 A; A/B=135-756.
DR PDB; 2ISD; X-ray; 2.50 A; A/B=133-756.
DR PDBsum; 1DJG; -.
DR PDBsum; 1DJH; -.
DR PDBsum; 1DJI; -.
DR PDBsum; 1DJW; -.
DR PDBsum; 1DJX; -.
DR PDBsum; 1DJY; -.
DR PDBsum; 1DJZ; -.
DR PDBsum; 1MAI; -.
DR PDBsum; 1QAS; -.
DR PDBsum; 1QAT; -.
DR PDBsum; 2ISD; -.
DR AlphaFoldDB; P10688; -.
DR SMR; P10688; -.
DR BioGRID; 246790; 1.
DR STRING; 10116.ENSRNOP00000042824; -.
DR BindingDB; P10688; -.
DR ChEMBL; CHEMBL1914273; -.
DR SwissLipids; SLP:000001066; -.
DR GlyGen; P10688; 2 sites.
DR iPTMnet; P10688; -.
DR PhosphoSitePlus; P10688; -.
DR jPOST; P10688; -.
DR PaxDb; P10688; -.
DR PRIDE; P10688; -.
DR GeneID; 24655; -.
DR KEGG; rno:24655; -.
DR UCSC; RGD:3346; rat.
DR CTD; 5333; -.
DR RGD; 3346; Plcd1.
DR eggNOG; KOG0169; Eukaryota.
DR InParanoid; P10688; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; P10688; -.
DR BRENDA; 3.1.4.11; 5301.
DR Reactome; R-RNO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR SABIO-RK; P10688; -.
DR EvolutionaryTrace; P10688; -.
DR PRO; PR:P10688; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IMP:CAFA.
DR GO; GO:0032794; F:GTPase activating protein binding; ISO:RGD.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IMP:CAFA.
DR GO; GO:0070300; F:phosphatidic acid binding; ISO:RGD.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; ISO:RGD.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:RGD.
DR GO; GO:0004629; F:phospholipase C activity; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; IDA:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; ISO:RGD.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IMP:RGD.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; IMP:RGD.
DR GO; GO:0010701; P:positive regulation of norepinephrine secretion; IMP:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:1900274; P:regulation of phospholipase C activity; IMP:RGD.
DR GO; GO:0010044; P:response to aluminum ion; IEP:RGD.
DR GO; GO:0051592; P:response to calcium ion; IMP:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IMP:RGD.
DR GO; GO:0034696; P:response to prostaglandin F; IEP:RGD.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR028391; PLC-delta1.
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; PTHR10336; 1.
DR PANTHER; PTHR10336:SF80; PTHR10336:SF80; 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; SM00054; EFh; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transducer.
FT CHAIN 1..756
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase delta-1"
FT /id="PRO_0000088506"
FT DOMAIN 21..130
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 140..175
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 176..211
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 296..440
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 492..609
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 609..737
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 30..57
FT /note="Substrate binding"
FT ACT_SITE 311
FT ACT_SITE 356
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 312
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT BINDING 438
FT /ligand="substrate"
FT BINDING 440
FT /ligand="substrate"
FT BINDING 522
FT /ligand="substrate"
FT BINDING 549
FT /ligand="substrate"
FT BINDING 651
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 653
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 677
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 706
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 707
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 708
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT MOD_RES 457
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R3B1"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51178"
FT CARBOHYD 191
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:24098488"
FT CARBOHYD 193
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:24098488"
FT VARIANT 412
FT /note="I -> M (in SHR)"
FT /evidence="ECO:0000269|PubMed:1684614"
FT VARIANT 423
FT /note="T -> S (in SHR)"
FT /evidence="ECO:0000269|PubMed:1684614"
FT VARIANT 463
FT /note="V -> D (in SHR)"
FT /evidence="ECO:0000269|PubMed:1684614"
FT VARIANT 668
FT /note="G -> A (in SHR)"
FT /evidence="ECO:0000269|PubMed:1684614"
FT MUTAGEN 311
FT /note="H->A: Lowers activity 10000-fold."
FT /evidence="ECO:0000269|PubMed:9565585"
FT MUTAGEN 312
FT /note="N->A: Lowers activity 10000-fold."
FT /evidence="ECO:0000269|PubMed:9565585"
FT MUTAGEN 320
FT /note="L->A: Lowers activity 3-fold."
FT /evidence="ECO:0000269|PubMed:9565585"
FT MUTAGEN 341
FT /note="E->A,H,Q: Lowers activity 200000-fold."
FT /evidence="ECO:0000269|PubMed:9565585"
FT MUTAGEN 343
FT /note="D->A: Lowers activity 1000-fold."
FT /evidence="ECO:0000269|PubMed:9565585"
FT MUTAGEN 343
FT /note="D->R: Lowers activity 100000-fold."
FT /evidence="ECO:0000269|PubMed:9565585"
FT MUTAGEN 356
FT /note="H->A: Lowers activity 1000-fold."
FT /evidence="ECO:0000269|PubMed:9565585"
FT MUTAGEN 360
FT /note="F->A: Lowers activity 4-fold."
FT /evidence="ECO:0000269|PubMed:9565585"
FT MUTAGEN 390
FT /note="E->A,H,K: Lowers activity 1000-fold."
FT /evidence="ECO:0000269|PubMed:9565585"
FT MUTAGEN 390
FT /note="E->Q: Lowers activity 200-fold."
FT /evidence="ECO:0000269|PubMed:9565585"
FT MUTAGEN 438
FT /note="K->A: Lowers activity very slightly."
FT /evidence="ECO:0000269|PubMed:9565585"
FT MUTAGEN 440
FT /note="K->A: No effect on activity towards
FT phosphatidylinositol 4-monophosphate. Lowers activity 5-
FT fold towards phosphatidylinositol 4,5-bisphosphate."
FT /evidence="ECO:0000269|PubMed:9565585"
FT MUTAGEN 522
FT /note="S->A: Lowers activity 10000-fold."
FT /evidence="ECO:0000269|PubMed:9565585"
FT MUTAGEN 549
FT /note="R->A: Lowers activity 600-fold."
FT /evidence="ECO:0000269|PubMed:9565585"
FT MUTAGEN 551
FT /note="Y->A: Lowers activity 600-fold."
FT /evidence="ECO:0000269|PubMed:9565585"
FT MUTAGEN 555
FT /note="W->A: Lowers activity very slightly."
FT /evidence="ECO:0000269|PubMed:9565585"
FT CONFLICT 627..629
FT /note="RPE -> APK (in Ref. 2; AAP31521)"
FT /evidence="ECO:0000305"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:1MAI"
FT STRAND 26..35
FT /evidence="ECO:0007829|PDB:1MAI"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:1MAI"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1MAI"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:1MAI"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1MAI"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1MAI"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:1MAI"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:1MAI"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1MAI"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:1MAI"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:1MAI"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:1MAI"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:1DJX"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 230..239
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 262..266
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:1DJX"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 326..334
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:1QAS"
FT TURN 357..360
FT /evidence="ECO:0007829|PDB:1DJY"
FT HELIX 366..376
FT /evidence="ECO:0007829|PDB:1DJX"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 385..392
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 395..409
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:1DJX"
FT TURN 428..433
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 490..493
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 496..502
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 509..514
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 519..524
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 525..545
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 565..568
FT /evidence="ECO:0007829|PDB:1DJX"
FT TURN 569..571
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 574..577
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 584..594
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 596..598
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 600..603
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 606..609
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 629..640
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 644..646
FT /evidence="ECO:0007829|PDB:1QAT"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 654..663
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 664..666
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 668..671
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 683..693
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 695..697
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 699..706
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 709..711
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 714..722
FT /evidence="ECO:0007829|PDB:1DJX"
FT HELIX 723..725
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 729..736
FT /evidence="ECO:0007829|PDB:1DJX"
FT STRAND 742..755
FT /evidence="ECO:0007829|PDB:1DJX"
SQ SEQUENCE 756 AA; 85962 MW; E33F2313AC81E9F9 CRC64;
MDSGRDFLTL HGLQDDPDLQ ALLKGSQLLK VKSSSWRRER FYKLQEDCKT IWQESRKVMR
SPESQLFSIE DIQEVRMGHR TEGLEKFARD IPEDRCFSIV FKDQRNTLDL IAPSPADAQH
WVQGLRKIIH HSGSMDQRQK LQHWIHSCLR KADKNKDNKM NFKELKDFLK ELNIQVDDGY
ARKIFRECDH SQTDSLEDEE IETFYKMLTQ RAEIDRAFEE AAGSAETLSV ERLVTFLQHQ
QREEEAGPAL ALSLIERYEP SETAKAQRQM TKDGFLMYLL SADGNAFSLA HRRVYQDMDQ
PLSHYLVSSS HNTYLLEDQL TGPSSTEAYI RALCKGCRCL ELDCWDGPNQ EPIIYHGYTF
TSKILFCDVL RAIRDYAFKA SPYPVILSLE NHCSLEQQRV MARHLRAILG PILLDQPLDG
VTTSLPSPEQ LKGKILLKGK KLGGLLPAGG ENGSEATDVS DEVEAAEMED EAVRSQVQHK
PKEDKLKLVP ELSDMIIYCK SVHFGGFSSP GTSGQAFYEM ASFSESRALR LLQESGNGFV
RHNVSCLSRI YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ TPGPEMDVYL GCFQDNGGCG
YVLKPAFLRD PNTTFNSRAL TQGPWWRPER LRVRIISGQQ LPKVNKNKNS IVDPKVIVEI
HGVGRDTGSR QTAVITNNGF NPRWDMEFEF EVTVPDLALV RFMVEDYDSS SKNDFIGQST
IPWNSLKQGY RHVHLLSKNG DQHPSATLFV KISIQD
