ID MRGRD_HUMAN Reviewed; 321 AA. AC Q8TDS7; Q8NGK7; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 02-SEP-2026, entry version 161. DE RecName: Full=Mas-related G protein-coupled receptor member D {ECO:0000305}; DE AltName: Full=Beta-alanine receptor {ECO:0000303|PubMed:15037633}; DE AltName: Full=G protein-coupled receptor TGR7 {ECO:0000303|PubMed:15037633}; GN Name=MRGPRD {ECO:0000303|PubMed:39580805, GN ECO:0000312|HGNC:HGNC:29626}; GN Synonyms=MRGD {ECO:0000303|PubMed:12909716}; 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]. RX PubMed=12909716; DOI=10.1073/pnas.1732949100; RA Zylka M.J., Dong X., Southwell A.L., Anderson D.J.; RT "Atypical expansion in mice of the sensory neuron-specific Mrg G protein- RT coupled receptor family."; RL Proc. Natl. Acad. Sci. U.S.A. 100:10043-10048(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION. RC TISSUE=Liver; RX PubMed=15037633; DOI=10.1074/jbc.m314240200; RA Shinohara T., Harada M., Ogi K., Maruyama M., Fujii R., Tanaka H., RA Fukusumi S., Komatsu H., Hosoya M., Noguchi Y., Watanabe T., Moriya T., RA Itoh Y., Hinuma S.; RT "Identification of a G protein-coupled receptor specifically responsive to RT beta-alanine."; RL J. Biol. Chem. 279:23559-23564(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12044878; DOI=10.1016/s0014-5793(02)02775-8; RA Takeda S., Kadowaki S., Haga T., Takaesu H., Mitaku S.; RT "Identification of G protein-coupled receptor genes from the human genome RT sequence."; RL FEBS Lett. 520:97-101(2002). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.; RT "Genome-wide discovery and analysis of human seven transmembrane helix RT receptor genes."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=23091359; DOI=10.1155/2012/816159; RA Uno M., Nishimura S., Fukuchi K., Kaneta Y., Oda Y., Komori H., Takeda S., RA Haga T., Agatsuma T., Nara F.; RT "Identification of physiologically active substances as novel ligands for RT MRGPRD."; RL J. Biomed. Biotechnol. 2012:816159-816159(2012). RN [6] {ECO:0007744|PDB:7Y12, ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, ECO:0007744|PDB:7Y15} RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 5-321 IN COMPLEX WITH RP BETA-ALANINE; GNAI1, GNB1 AND GNG2, FUNCTION, DISULFIDE BOND, AND RP MUTAGENESIS OF ARG-103; TYR-106; TYR-109; ASP-179; SER-234; LEU-237; RP TRP-241; PHE-242; TYR-245 AND TRP-246. RX PubMed=35840655; DOI=10.1038/s42003-022-03668-3; RA Suzuki S., Iida M., Hiroaki Y., Tanaka K., Kawamoto A., Kato T., Oshima A.; RT "Structural insight into the activation mechanism of MrgD with RT heterotrimeric Gi-protein revealed by cryo-EM."; RL Commun. Biol. 5:707-707(2022). RN [7] {ECO:0007744|PDB:9DQH, ECO:0007744|PDB:9DQJ} RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 2-321 IN COMPLEX WITH RP GNB1 AND GNG2, FUNCTION, DISULFIDE BOND, AND MUTAGENESIS OF LYS-102; RP ARG-103; TYR-106; TYR-109; ASN-157; ASP-179; GLN-182; PHE-242 AND TYR-245. RX PubMed=39580805; DOI=10.1016/j.celrep.2024.114942; RA Wang C., Liu Y., Lanier M., Yeager A., Singh I., Gumpper R.H., Krumm B.E., RA DeLeon C., Zhang S., Boehm M., Pittner R., Baron A., Dvorak L., Bacon C., RA Shoichet B.K., Martinborough E., Fay J.F., Cao C., Roth B.L.; RT "High-affinity agonists reveal recognition motifs for the MRGPRD GPCR."; RL Cell Rep. 43:114942-114942(2024). CC -!- FUNCTION: G protein-coupled receptor that acts as a mediator of CC peripheral pain and itch sensations (PubMed:15037633, PubMed:23091359, CC PubMed:35840655, PubMed:39580805). Activated by various ligands, such CC as beta-alanine, beta-aminoisobutyrate, angiotensin 1-7, alamandine and CC allantoin, causing a conformation change that triggers signaling via CC guanine nucleotide-binding proteins (G proteins) and modulates the CC activity of downstream effectors (PubMed:15037633, PubMed:23091359, CC PubMed:35840655, PubMed:39580805). MRGPRD is both coupled to G(q) and CC G(i) G proteins: G(q) coupling activates phospholipase C-beta, CC releasing diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) CC second messengers, while G(i) coupling mediates inhibition of adenylate CC cyclase activity (PubMed:15037633, PubMed:23091359, PubMed:35840655, CC PubMed:39580805). MRGPRD is specifically expressed in neurons that CC innervate the epidermis and acts as a key mediator of skin stimuli, CC such as itch, pain and mechanical stimuli (By similarity). Required to CC maintain skin homeostasis in response to irritant dermatitis by CC initiating a signaling that promotes glutamate release, inhibiting mast CC cell hyperresponsiveness and skin inflammation (By similarity). CC Required to prevent cardiomyocyte hypertrophy following activation by CC alamandine, a decarboxylation product of angiotensin 1-7 (By CC similarity). Acts as a receptor for allantoin in dorsal root ganglion CC neurons, eliciting chronic itch (pruritus) (By similarity). CC {ECO:0000250|UniProtKB:Q91ZB8, ECO:0000269|PubMed:15037633, CC ECO:0000269|PubMed:23091359, ECO:0000269|PubMed:35840655, CC ECO:0000269|PubMed:39580805}. CC -!- ACTIVITY REGULATION: Activated by diethylstilbestrol, a synthetic CC estrogen hormone. {ECO:0000269|PubMed:23091359}. CC -!- INTERACTION: CC Q8TDS7; O60894: RAMP1; NbExp=2; IntAct=EBI-67111619, EBI-962893; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15037633}; CC Multi-pass membrane protein {ECO:0000269|PubMed:35840655, CC ECO:0000269|PubMed:39580805}. Note=Localized at the plasma membrane but CC internalized into the cytoplasm after treatment with beta-alanine. CC {ECO:0000269|PubMed:15037633}. CC -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family. Mas CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC06005.1; Type=Erroneous initiation; Evidence={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; AY427820; AAR05120.1; -; mRNA. DR EMBL; AB154410; BAD20638.1; -; mRNA. DR EMBL; AB083627; BAB89340.1; -; Genomic_DNA. DR EMBL; AB065786; BAC06005.1; ALT_INIT; Genomic_DNA. DR CCDS; CCDS31625.1; -. DR RefSeq; NP_944605.2; NM_198923.2. DR PDB; 7Y12; EM; 3.10 A; R=5-321. DR PDB; 7Y13; EM; 3.10 A; R=5-321. DR PDB; 7Y14; EM; 3.20 A; R=5-321. DR PDB; 7Y15; EM; 2.90 A; R=5-321. DR PDB; 9DQH; EM; 2.92 A; A=2-321. DR PDB; 9DQJ; EM; 2.90 A; A=2-321. DR AlphaFoldDB; Q8TDS7; -. DR EMDB; EMD-33554; -. DR EMDB; EMD-33555; -. DR EMDB; EMD-33556; -. DR EMDB; EMD-33557; -. DR EMDB; EMD-47113; -. DR EMDB; EMD-47114; -. DR SMR; Q8TDS7; -. DR FunCoup; Q8TDS7; 125. DR IntAct; Q8TDS7; 3. DR NDEx; IQUERY-CP-MRGPRD; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000310631; -. DR ChEMBL; CHEMBL4523899; -. DR GuidetoPHARMACOLOGY; 152; -. DR GlyCosmos; Q8TDS7; 4 sites, No reported glycans. DR GlyGen; Q8TDS7; 5 sites. DR iPTMnet; Q8TDS7; -. DR PhosphoSitePlus; Q8TDS7; -. DR BioMuta; MRGPRD; -. DR DMDM; 50401085; -. DR MassIVE; Q8TDS7; -. DR PaxDb; 9606-ENSP00000310631; -. DR PeptideAtlas; Q8TDS7; -. DR Antibodypedia; 16747; 100 antibodies from 23 providers. DR DNASU; 116512; -. DR Ensembl; ENST00000309106.3; ENSP00000310631.3; ENSG00000172938.3. DR GeneID; 116512; -. DR KEGG; hsa:116512; -. DR MANE-Select; ENST00000309106.3; ENSP00000310631.3; NM_198923.2; NP_944605.2. DR UCSC; uc010rqf.2; human. DR AGR; HGNC:29626; -. DR ClinPGx; PA134978563; -. DR CTD; 116512; -. DR DisGeNET; 116512; -. DR GeneCards; MRGPRD; -. DR HGNC; HGNC:29626; MRGPRD. DR HPA; ENSG00000172938; Not detected. DR MIM; 607231; gene. DR OpenTargets; ENSG00000172938; -. DR VEuPathDB; HostDB:ENSG00000172938; -. DR eggNOG; ENOG502SNJC; Eukaryota. DR GeneTree; ENSGT01030000234639; -. DR HOGENOM; CLU_009579_4_1_1; -. DR InParanoid; Q8TDS7; -. DR OMA; KCHRPRH; -. DR OrthoDB; 9631784at2759; -. DR PAN-GO; Q8TDS7; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q8TDS7; -. DR PathwayCommons; Q8TDS7; -. DR Reactome; R-HSA-375276; Peptide ligand-binding receptors. DR SignaLink; Q8TDS7; -. DR SIGNOR; Q8TDS7; -. DR BioGRID-ORCS; 116512; 16 hits in 1139 CRISPR screens. DR GeneWiki; MRGPRD; -. DR GenomeRNAi; 116512; -. DR Pharos; Q8TDS7; Tchem. DR PRO; PR:Q8TDS7; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q8TDS7; protein. DR Bgee; ENSG00000172938; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 39 other cell types or tissues. DR GO; GO:0005576; C:extracellular region; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IEA:Ensembl. DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0002033; P:angiotensin-mediated vasodilation involved in regulation of systemic arterial blood pressure; IEA:Ensembl. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISS:UniProtKB. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0160025; P:sensory perception of itch; ISS:UniProtKB. DR CDD; cd15108; 7tmA_MrgprD; 1. DR FunFam; 1.20.1070.10:FF:000193; Mas-related G-protein coupled receptor member E; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR InterPro; IPR026232; MRGPCRD. DR InterPro; IPR026234; MRGPCRFAMILY. DR PANTHER; PTHR11334; MAS-RELATED G-PROTEIN COUPLED RECEPTOR; 1. DR PANTHER; PTHR11334:SF57; MAS-RELATED G-PROTEIN COUPLED RECEPTOR MEMBER D; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR02110; MRGPCRD. DR PRINTS; PR02108; MRGPCRFAMILY. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Disulfide bond; G protein-coupled receptor; KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1..321 FT /note="Mas-related G protein-coupled receptor member D" FT /id="PRO_0000069756" FT TOPO_DOM 1..24 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT TRANSMEM 25..50 FT /note="Helical; Name=1" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT TOPO_DOM 51..61 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT TRANSMEM 62..88 FT /note="Helical; Name=2" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT TOPO_DOM 89..95 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT TRANSMEM 96..125 FT /note="Helical; Name=3" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT TOPO_DOM 126..140 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT TRANSMEM 141..165 FT /note="Helical; Name=4" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT TOPO_DOM 166..176 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT TRANSMEM 177..203 FT /note="Helical; Name=5" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT TOPO_DOM 204..219 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT TRANSMEM 220..244 FT /note="Helical; Name=6" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT TOPO_DOM 245..254 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT TRANSMEM 255..279 FT /note="Helical; Name=7" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT TOPO_DOM 280..321 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT REGION 302..321 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 103 FT /ligand="beta-alanine" FT /ligand_id="ChEBI:CHEBI:57966" FT /evidence="ECO:0000269|PubMed:35840655" FT BINDING 179 FT /ligand="beta-alanine" FT /ligand_id="ChEBI:CHEBI:57966" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0007744|PDB:7Y12, ECO:0007744|PDB:7Y14" FT BINDING 241 FT /ligand="beta-alanine" FT /ligand_id="ChEBI:CHEBI:57966" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0007744|PDB:7Y12, ECO:0007744|PDB:7Y14" FT BINDING 245 FT /ligand="beta-alanine" FT /ligand_id="ChEBI:CHEBI:57966" FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0007744|PDB:7Y14" FT CARBOHYD 2 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 6 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 16 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 92 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 164..175 FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805, ECO:0007744|PDB:7Y12, FT ECO:0007744|PDB:7Y13, ECO:0007744|PDB:7Y14, FT ECO:0007744|PDB:7Y15, ECO:0007744|PDB:9DQH, FT ECO:0007744|PDB:9DQJ" FT MUTAGEN 102 FT /note="K->A: Does not affect G protein-coupled receptor FT signaling." FT /evidence="ECO:0000269|PubMed:39580805" FT MUTAGEN 103 FT /note="R->A: Abolished G protein-coupled receptor FT signaling." FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805" FT MUTAGEN 106 FT /note="Y->A: Decreased G(i)- and G(q)-mediated signaling." FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805" FT MUTAGEN 109 FT /note="Y->A: Decreased G(i)-mediated signaling." FT /evidence="ECO:0000269|PubMed:35840655" FT MUTAGEN 157 FT /note="N->A: Slightly increased G protein-coupled receptor FT signaling." FT /evidence="ECO:0000269|PubMed:39580805" FT MUTAGEN 179 FT /note="D->A: Abolished G protein-coupled receptor FT signaling." FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805" FT MUTAGEN 182 FT /note="Q->A: Slightly increased G protein-coupled receptor FT signaling." FT /evidence="ECO:0000269|PubMed:39580805" FT MUTAGEN 234 FT /note="S->A: Decreased G(i)-mediated signaling." FT /evidence="ECO:0000269|PubMed:35840655" FT MUTAGEN 237 FT /note="L->A: Decreased G(i)-mediated signaling." FT /evidence="ECO:0000269|PubMed:35840655" FT MUTAGEN 241 FT /note="W->A: Abolished G protein-coupled receptor FT signaling. Abolished G(i)- and G(q)-mediated signaling." FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805" FT MUTAGEN 242 FT /note="F->A: Abolished G(i)- and G(q)-mediated signaling." FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805" FT MUTAGEN 245 FT /note="Y->A: Decreased G protein-coupled receptor FT signaling." FT /evidence="ECO:0000269|PubMed:35840655, FT ECO:0000269|PubMed:39580805" FT MUTAGEN 246 FT /note="W->A: Abolished G protein-coupled receptor FT signaling." FT /evidence="ECO:0000269|PubMed:35840655" FT HELIX 23..52 FT /evidence="ECO:0007829|PDB:7Y15" FT STRAND 53..56 FT /evidence="ECO:0007829|PDB:7Y15" FT HELIX 62..86 FT /evidence="ECO:0007829|PDB:7Y15" FT STRAND 91..96 FT /evidence="ECO:0007829|PDB:7Y15" FT HELIX 97..128 FT /evidence="ECO:0007829|PDB:7Y15" FT HELIX 130..135 FT /evidence="ECO:0007829|PDB:7Y15" FT HELIX 141..164 FT /evidence="ECO:0007829|PDB:7Y15" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:7Y15" FT HELIX 173..185 FT /evidence="ECO:0007829|PDB:7Y15" FT HELIX 186..190 FT /evidence="ECO:0007829|PDB:7Y15" FT HELIX 191..208 FT /evidence="ECO:0007829|PDB:7Y15" FT TURN 209..212 FT /evidence="ECO:0007829|PDB:7Y15" FT HELIX 217..229 FT /evidence="ECO:0007829|PDB:7Y15" FT HELIX 230..234 FT /evidence="ECO:0007829|PDB:7Y15" FT HELIX 235..244 FT /evidence="ECO:0007829|PDB:7Y15" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:7Y15" FT TURN 251..253 FT /evidence="ECO:0007829|PDB:7Y12" FT HELIX 254..273 FT /evidence="ECO:0007829|PDB:7Y15" FT HELIX 274..278 FT /evidence="ECO:0007829|PDB:7Y15" FT TURN 282..284 FT /evidence="ECO:0007829|PDB:7Y12" SQ SEQUENCE 321 AA; 36118 MW; B45AB7FEB2154B40 CRC64; MNQTLNSSGT VESALNYSRG STVHTAYLVL SSLAMFTCLC GMAGNSMVIW LLGFRMHRNP FCIYILNLAA ADLLFLFSMA STLSLETQPL VNTTDKVHEL MKRLMYFAYT VGLSLLTAIS TQRCLSVLFP IWFKCHRPRH LSAWVCGLLW TLCLLMNGLT SSFCSKFLKF NEDRCFRVDM VQAALIMGVL TPVMTLSSLT LFVWVRRSSQ QWRRQPTRLF VVVLASVLVF LICSLPLSIY WFVLYWLSLP PEMQVLCFSL SRLSSSVSSS ANPVIYFLVG SRRSHRLPTR SLGTVLQQAL REEPELEGGE TPTVGTNEMG A //