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 27-MAR-2024, entry version 185. 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; Evidence={ECO:0000255|PROSITE- CC 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}. 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; 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; 33. 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; 9606-ENSP00000388631; -. DR PeptideAtlas; Q9BRC7; -. DR ProteomicsDB; 78756; -. [Q9BRC7-1] DR ProteomicsDB; 78757; -. [Q9BRC7-2] DR Antibodypedia; 4087; 129 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 AGR; HGNC:9062; -. 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; 2900494at2759; -. 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; 7 hits in 1149 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 122 other cell types or tissues. DR ExpressionAtlas; Q9BRC7; baseline and differential. 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; IEA:UniProtKB-EC. DR GO; GO:0007340; P:acrosome reaction; IEA:Ensembl. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:UniProtKB. DR CDD; cd00275; C2_PLC_like; 1. DR CDD; cd13363; PH_PLC_delta; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 1.10.238.10; EF-hand; 2. 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; 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; 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:SF31; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA-4; 1. DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 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; 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; 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. DR Genevisible; Q9BRC7; HS. 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 //