PLCD4_HUMAN
ID PLCD4_HUMAN Reviewed; 762 AA.
AC Q9BRC7; Q53FS8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 {ECO:0000305};
DE Short=hPLCD4;
DE EC=3.1.4.11 {ECO:0000269|PubMed:15140260};
DE AltName: Full=Phosphoinositide phospholipase C-delta-4;
DE AltName: Full=Phospholipase C-delta-4;
DE Short=PLC-delta-4;
GN Name=PLCD4 {ECO:0000312|HGNC:HGNC:9062};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=15140260; DOI=10.1186/1476-4598-3-15;
RA Leung D.W., Tompkins C., Brewer J., Ball A., Coon M., Morris V.,
RA Waggoner D., Singer J.W.;
RT "Phospholipase C delta-4 overexpression upregulates ErbB1/2 expression, Erk
RT signaling pathway, and proliferation in MCF-7 cells.";
RL Mol. Cancer 3:15-15(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney proximal tubule;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION.
RX PubMed=10702683; DOI=10.1159/000015437;
RA Kim H., Suh P.-G., Ryu S.H., Park S.H.;
RT "Assignment of the human PLC delta4 gene (PLCD4) to human chromosome band
RT 2q35 by fluorescence in situ hybridization.";
RL Cytogenet. Cell Genet. 87:254-255(1999).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=15505048; DOI=10.1167/iovs.04-0084;
RA Landreville S., Coulombe S., Carrier P., Gelb M.H., Guerin S.L.,
RA Salesse C.;
RT "Expression of phospholipases A2 and C in human corneal epithelial cells.";
RL Invest. Ophthalmol. Vis. Sci. 45:3997-4003(2004).
RN [6]
RP FUNCTION (ISOFORM 2), INTERACTION WITH GNAI3, GBA MOTIF, AND MUTAGENESIS OF
RP 224-LEU--LEU-228; PHE-227 AND 227-PHE-LEU-228.
RX PubMed=30194280; DOI=10.1074/jbc.ra118.003580;
RA Maziarz M., Broselid S., DiGiacomo V., Park J.C., Luebbers A.,
RA Garcia-Navarrete L., Blanco-Canosa J.B., Baillie G.S., Garcia-Marcos M.;
RT "A biochemical and genetic discovery pipeline identifies PLCdelta4b as a
RT nonreceptor activator of heterotrimeric G-proteins.";
RL J. Biol. Chem. 293:16964-16983(2018).
CC -!- FUNCTION: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2)
CC to generate 2 second messenger molecules diacylglycerol (DAG) and
CC inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of
CC protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular
CC stores. Required for acrosome reaction in sperm during fertilization,
CC probably by acting as an important enzyme for intracellular Ca(2+)
CC mobilization in the zona pellucida-induced acrosome reaction. May play
CC a role in cell growth. Modulates the liver regeneration in cooperation
CC with nuclear PKC. Overexpression up-regulates the Erk signaling pathway
CC and proliferation. {ECO:0000269|PubMed:15140260}.
CC -!- FUNCTION: [Isoform 2]: Acts as a non-receptor guanine nucleotide
CC exchange factor which binds to and activates guanine nucleotide-binding
CC protein (G-protein) alpha subunit GNAI3. {ECO:0000269|PubMed:30194280}.
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:15140260};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000305|PubMed:15140260};
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:0000269|PubMed:15140260};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000305|PubMed:15140260};
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. {ECO:0000250};
CC -!- SUBUNIT: Interacts with GRIP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8K3R3}.
CC -!- SUBUNIT: [Isoform 2]: Interacts (via GBA motif) with guanine
CC nucleotide-binding protein G(i) alpha subunit GNAI3 (inactive GDP-bound
CC form); high-affinity interaction (PubMed:30194280).
CC {ECO:0000269|PubMed:30194280}.
CC -!- SUBUNIT: [Isoform 1]: Interacts (via GBA motif) with guanine
CC nucleotide-binding protein G(i) alpha subunit GNAI3 (inactive GDP-bound
CC form); low-affinity interaction (PubMed:30194280).
CC {ECO:0000269|PubMed:30194280}.
CC -!- INTERACTION:
CC Q9BRC7; P50221: MEOX1; NbExp=3; IntAct=EBI-748799, EBI-2864512;
CC Q9BRC7; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-748799, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:15140260}. Endoplasmic reticulum {ECO:0000250}.
CC Note=Localizes primarily to intracellular membranes mostly to the
CC endoplasmic reticulum.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BRC7-1; Sequence=Displayed;
CC Name=2; Synonyms=PLCD4b;
CC IsoId=Q9BRC7-2; Sequence=VSP_028501, VSP_028502;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and kidney
CC tissues, and at moderate level in intestinal tissue. Expressed in
CC corneal epithelial cells. {ECO:0000269|PubMed:15140260,
CC ECO:0000269|PubMed:15505048}.
CC -!- DOMAIN: The PDZ-binding motif mediates the interaction with GRIP1.
CC -!- DOMAIN: The C2 domain mediates pre-localization to the membrane prior
CC to Ca(2+) import and non-selective Ca(2+)-mediated targeting to various
CC cellular membranes.
CC -!- DOMAIN: The PH domain is not a critical determinant of the membrane
CC localization.
CC -!- DOMAIN: The GBA (G-alpha binding and activating) motif mediates binding
CC to the alpha subunits of guanine nucleotide-binding proteins (G
CC proteins). {ECO:0000269|PubMed:30194280}.
CC -!- MISCELLANEOUS: [Isoform 1]: Acceptor splice site between exons 4 and 5
CC is non-canonical but conserved through species for that particular
CC gene.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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DR EMBL; AY512961; AAS82574.1; -; mRNA.
DR EMBL; AK223203; BAD96923.1; -; mRNA.
DR EMBL; BC006355; AAH06355.1; -; mRNA.
DR CCDS; CCDS46516.1; -. [Q9BRC7-1]
DR RefSeq; NP_116115.1; NM_032726.3. [Q9BRC7-1]
DR AlphaFoldDB; Q9BRC7; -.
DR SMR; Q9BRC7; -.
DR BioGRID; 124273; 32.
DR IntAct; Q9BRC7; 4.
DR STRING; 9606.ENSP00000388631; -.
DR SwissLipids; SLP:000001758; -.
DR iPTMnet; Q9BRC7; -.
DR PhosphoSitePlus; Q9BRC7; -.
DR BioMuta; PLCD4; -.
DR DMDM; 74732863; -.
DR jPOST; Q9BRC7; -.
DR MassIVE; Q9BRC7; -.
DR PaxDb; Q9BRC7; -.
DR PeptideAtlas; Q9BRC7; -.
DR PRIDE; Q9BRC7; -.
DR ProteomicsDB; 78756; -. [Q9BRC7-1]
DR ProteomicsDB; 78757; -. [Q9BRC7-2]
DR Antibodypedia; 4087; 118 antibodies from 21 providers.
DR DNASU; 84812; -.
DR Ensembl; ENST00000417849.5; ENSP00000396942.1; ENSG00000115556.14. [Q9BRC7-1]
DR Ensembl; ENST00000450993.7; ENSP00000388631.2; ENSG00000115556.14. [Q9BRC7-1]
DR GeneID; 84812; -.
DR KEGG; hsa:84812; -.
DR MANE-Select; ENST00000450993.7; ENSP00000388631.2; NM_032726.4; NP_116115.1.
DR UCSC; uc061smf.1; human. [Q9BRC7-1]
DR CTD; 84812; -.
DR DisGeNET; 84812; -.
DR GeneCards; PLCD4; -.
DR HGNC; HGNC:9062; PLCD4.
DR HPA; ENSG00000115556; Group enriched (retina, skeletal muscle).
DR MIM; 605939; gene.
DR neXtProt; NX_Q9BRC7; -.
DR OpenTargets; ENSG00000115556; -.
DR PharmGKB; PA33390; -.
DR VEuPathDB; HostDB:ENSG00000115556; -.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000156180; -.
DR HOGENOM; CLU_002738_0_2_1; -.
DR InParanoid; Q9BRC7; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q9BRC7; -.
DR TreeFam; TF313216; -.
DR PathwayCommons; Q9BRC7; -.
DR Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR SignaLink; Q9BRC7; -.
DR SIGNOR; Q9BRC7; -.
DR BioGRID-ORCS; 84812; 6 hits in 1070 CRISPR screens.
DR ChiTaRS; PLCD4; human.
DR GeneWiki; PLCD4; -.
DR GenomeRNAi; 84812; -.
DR Pharos; Q9BRC7; Tbio.
DR PRO; PR:Q9BRC7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BRC7; protein.
DR Bgee; ENSG00000115556; Expressed in hindlimb stylopod muscle and 120 other tissues.
DR ExpressionAtlas; Q9BRC7; baseline and differential.
DR Genevisible; Q9BRC7; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0007340; P:acrosome reaction; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:UniProtKB.
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; IPR028387; PLC-delta4.
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:SF31; PTHR10336:SF31; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF00169; PH; 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; 3.
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; 3.
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 Alternative splicing; Calcium; Cytoplasm; Endoplasmic reticulum;
KW Guanine-nucleotide releasing factor; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transducer.
FT CHAIN 1..762
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase delta-4"
FT /id="PRO_0000306824"
FT DOMAIN 16..124
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 134..169
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 170..205
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 206..237
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 290..435
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 493..609
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 609..736
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 26..53
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT REGION 443..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 213..243
FT /note="GBA"
FT /evidence="ECO:0000269|PubMed:30194280"
FT MOTIF 731..734
FT /note="PDZ-binding"
FT COMPBIAS 443..463
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 433
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 522
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 549
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 650
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 652
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 676
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 705
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 706
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 707
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62711"
FT VAR_SEQ 259..272
FT /note="KLRHVLSMDGFLSY -> ASEEDPGEGEEVNT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15140260"
FT /id="VSP_028501"
FT VAR_SEQ 273..762
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15140260"
FT /id="VSP_028502"
FT MUTAGEN 224..228
FT /note="LLEFL->ALEAA: Abolishes binding to and activation of
FT GNAI3."
FT /evidence="ECO:0000269|PubMed:30194280"
FT MUTAGEN 227..228
FT /note="FL->AA: Abolishes binding to GNAI3."
FT /evidence="ECO:0000269|PubMed:30194280"
FT MUTAGEN 227
FT /note="F->A: Marked but incomplete decrease in GNAI3
FT binding and reduced activation of G-protein signaling."
FT /evidence="ECO:0000269|PubMed:30194280"
FT CONFLICT 98
FT /note="R -> H (in Ref. 2; BAD96923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 762 AA; 87585 MW; 5444BE5CE2AEA3EF CRC64;
MASLLQDQLT TDQDLLLMQE GMPMRKVRSK SWKKLRYFRL QNDGMTVWHA RQARGSAKPS
FSISDVETIR NGHDSELLRS LAEELPLEQG FTIVFHGRRS NLDLMANSVE EAQIWMRGLQ
LLVDLVTSMD HQERLDQWLS DWFQRGDKNQ DGKMSFQEVQ RLLHLMNVEM DQEYAFSLFQ
AADTSQSGTL EGEEFVQFYK ALTKRAEVQE LFESFSADGQ KLTLLEFLDF LQEEQKERDC
TSELALELID RYEPSDSGKL RHVLSMDGFL SYLCSKDGDI FNPACLPIYQ DMTQPLNHYF
ICSSHNTYLV GDQLCGQSSV EGYIRALKRG CRCVEVDVWD GPSGEPVVYH GHTLTSRILF
KDVVATVAQY AFQTSDYPVI LSLETHCSWE QQQTMARHLT EILGEQLLST TLDGVLPTQL
PSPEELRRKI LVKGKKLTLE EDLEYEEEEA EPELEESELA LESQFETEPE PQEQNLQNKD
KKKKSKPILC PALSSLVIYL KSVSFRSFTH SKEHYHFYEI SSFSETKAKR LIKEAGNEFV
QHNTWQLSRV YPSGLRTDSS NYNPQELWNA GCQMVAMNMQ TAGLEMDICD GHFRQNGGCG
YVLKPDFLRD IQSSFHPEKP ISPFKAQTLL IQVISGQQLP KVDKTKEGSI VDPLVKVQIF
GVRLDTARQE TNYVENNGFN PYWGQTLCFR VLVPELAMLR FVVMDYDWKS RNDFIGQYTL
PWTCMQQGYR HIHLLSKDGI SLRPASIFVY ICIQEGLEGD ES
