Mrgprx1
entrez
404242
canonical
uniprot
Q8CIP3
canonical
ensembl
ENSMUSG00000070552
resolver
ensp
ENSMUSP00000091954
resolver
enst
ENSMUST00000094390
resolver
genesymbol
Mrgprx1
resolver
genesymbol_syn
Mrgc11
resolver
genesymbol_syn
Mrgprc11
resolver
uniprot_entry
MRGX1_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Activated by the positive allosteric modulator ML382 (2-(cyclopropanesulfonamido)-N-(2-ethoxyphenyl)benzamide). {ECO:0000250|UniProtKB:Q96LB2}.
uniprot
proteins
amino_acid_sequence
MDPTISSHDTESTPLNETGHPNCTPILTLSFLVLITTLVGLAGNTIVLWLLGFRMRRKAISVYILNLALADSFFLCCHFIDSLLRIIDFYGLYAHKLSKDILGNAAIIPYISGLSILSAISTERCLCVLWPIWYHCHRPRNMSAIICALIWVLSFLMGILDWFSGFLGETHHHLWKNVDFIITAFLIFLFMLLSGSSLALLLRILCGPRRKPLSRLYVTIALTVMVYLICGLPLGLYLFLLYWFGVHLHYPFCHIYQVTAVLSCVNSSANPIIYFLVGSFRQHRKHRSLKRVLKRALEDTPEEDEYTDSHLHKTTEISESRY
uniprot
proteins
function
FUNCTION: G protein-coupled receptor specifically expressed in sensory neurons of dorsal root ganglion, and which is involved in itch perception and pain transmission (PubMed:12397184, PubMed:20004959, PubMed:31350433, PubMed:33358893, PubMed:33876765, PubMed:39243765). Specifically activated by a variety of enkephalin (PENK) neuropeptides, such as BAM22 and BAM8-22, which induce itch in a histamine-independent manner (PubMed:31350433, PubMed:39243765). Activated by some tick defensins, such as I.persulcatus Def1 and I.ricinus Def2, evoking itch (PubMed:33358893). Also activated following cleavage by cathepsin S (CTSS) and dust mite cysteine protease Der p1 (PubMed:26216096, PubMed:28768771). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (PubMed:12397184). MRGPRX1 is both coupled to G(q) and G(i) G proteins: G(q) coupling activates phospholipase C-beta, releasing diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) second messengers, leading to sensitize TRPV1 in pruriceptors, while G(i) coupling mediates inhibition of adenylate cyclase activity (PubMed:12397184). Activation of MRGPRX1 in the peripheral nervous system elicits itch, evoking scratching (PubMed:31350433, PubMed:33876765). MRGPRX1 activation in sensory neurons of the nasal mucosa mediates sneezing responses to irritants or influenza-virus (PubMed:39243765). Activation in the central nervous system dampens chronic pain: BAM8-22-binding at the central terminals prevents pain signals passing to spinal cord neurons, attenuating spinal nociceptive transmission (By similarity). Activation by CXCL17 induces chemotactic movement (By similarity). {ECO:0000250|UniProtKB:Q96LB2, ECO:0000269|PubMed:12397184, ECO:0000269|PubMed:20004959, ECO:0000269|PubMed:26216096, ECO:0000269|PubMed:28768771, ECO:0000269|PubMed:31350433, ECO:0000269|PubMed:33358893, ECO:0000269|PubMed:33876765, ECO:0000269|PubMed:39243765}.
uniprot
proteins
mass_dalton
36810
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="D->H: Does not affect activation by the dust mite cysteine protease Der p1."; /evidence="ECO:0000269|PubMed:28768771"; MUTAGEN 11; /note="E->H: Abolished activation by the dust mite cysteine protease Der p1."; /evidence="ECO:0000269|PubMed:28768771"; MUTAGEN 17; /note="E->H: Abolished activation by the dust mite cysteine protease Der p1."; /evidence="ECO:0000269|PubMed:28768771
uniprot
proteins
post_translational_modification
PTM: Cleavage by D.pteronyssinus cysteine protease Der p1 leads to activation (PubMed:28768771). Cleavage by cathepsin S (CTSS) activates MRGPRX1, inducing itch (PubMed:26216096). {ECO:0000269|PubMed:26216096, ECO:0000269|PubMed:28768771}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
protein_family
Mas subfamily
uniprot
proteins
pubmed
12397184
uniprot
proteins
pubmed
20004959
uniprot
proteins
pubmed
26216096
uniprot
proteins
pubmed
28768771
uniprot
proteins
pubmed
31350433
uniprot
proteins
pubmed
33358893
uniprot
proteins
pubmed
33876765
uniprot
proteins
pubmed
39243765
uniprot
proteins
sequence_length
322
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96LB2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96LB2}.
uniprot
proteins
transmembrane_region
TRANSMEM 25..52; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:Q96LB2"; TRANSMEM 60..86; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:Q96LB2"; TRANSMEM 97..126; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:Q96LB2"; TRANSMEM 142..168; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:Q96LB2"; TRANSMEM 175..202; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:Q96LB2"; TRANSMEM 216..242; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:Q96LB2"; TRANSMEM 253..277; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:Q96LB2
uniprot
proteins