MRGX2_TRAFR
ID MRGX2_TRAFR Reviewed; 330 AA.
AC Q4QXU4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Mas-related G-protein coupled receptor member X2;
GN Name=MRGPRX2; Synonyms=MRGX2;
OS Trachypithecus francoisi (Francois' leaf monkey) (Presbytis francoisi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Trachypithecus.
OX NCBI_TaxID=54180;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15862286; DOI=10.1016/j.gene.2005.03.001;
RA Yang S., Liu Y., Lin A.A., Cavalli-Sforza L.L., Zhao Z., Su B.;
RT "Adaptive evolution of MRGX2, a human sensory neuron specific gene involved
RT in nociception.";
RL Gene 352:30-35(2005).
CC -!- FUNCTION: Mast cell-specific receptor for basic secretagogues, i.e.
CC cationic amphiphilic drugs, as well as endo- or exogenous peptides,
CC consisting of a basic head group and a hydrophobic core. Recognizes and
CC binds small molecules containing a cyclized tetrahydroisoquinoline
CC (THIQ), such as non-steroidal neuromuscular blocking drugs (NMBDs),
CC including tubocurarine and atracurium. In response to these compounds,
CC mediates pseudo-allergic reactions characterized by histamine release,
CC inflammation and airway contraction. {ECO:0000250|UniProtKB:Q3KNA1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Mas
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY651164; AAW70077.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4QXU4; -.
DR SMR; Q4QXU4; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:1990595; F:mast cell secretagogue receptor activity; ISS:UniProtKB.
DR GO; GO:0045576; P:mast cell activation; ISS:UniProtKB.
DR GO; GO:0043303; P:mast cell degranulation; ISS:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR026234; MRGPCRFAMILY.
DR PANTHER; PTHR11334; PTHR11334; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR02108; MRGPCRFAMILY.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; G-protein coupled receptor; Membrane; Receptor; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..330
FT /note="Mas-related G-protein coupled receptor member X2"
FT /id="PRO_0000069781"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 330 AA; 37043 MW; 4EE8ADD391CE443A CRC64;
MDPTTLVWGT ESTTMNGNDQ ALPLLCGKET LILVVLILFI ALVGLVGNAF VLWLLGFRMR
RNAFSVYVLS LAGADFLFLC FPMINCLAYL INFFHSISIN FPSFFTTVMT CAYLAGLSML
SAISTERCLS VLWPIWYRSR RPRHLSAVMC VLLWALSLLL SILEGKFCGF LFSDGDSGWC
QTFDFITAAW LMFLFVVLCG SSLALLVRIL CGSRGLPLTR LYLTILLTVL IFLLCGLPFG
IQWFLILWIW KNSDVLFCHI HPVSVVLSSF NSSANPIIYF FVGSFRKQWR LRQPVLKLAL
QRALQDTAEV DHSEGCFSQG TLEMSGSSLV