MRGX2_PANTR
ID MRGX2_PANTR Reviewed; 329 AA.
AC Q4QXX9; H2Q3A3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 3.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Mas-related G-protein coupled receptor member X2;
GN Name=MRGPRX2; Synonyms=MRGX2;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=24583173; DOI=10.1016/j.gene.2014.02.049;
RA Premzl M.;
RT "Comparative genomic analysis of eutherian Mas-related G protein-coupled
RT receptor genes.";
RL Gene 540:16-19(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(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; AY651129; AAW70042.1; -; Genomic_DNA.
DR EMBL; HG426074; CDG86192.1; -; Genomic_DNA.
DR EMBL; AACZ03078854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_016777901.1; XM_016922412.1.
DR RefSeq; XP_521864.4; XM_521864.5.
DR AlphaFoldDB; Q4QXX9; -.
DR SMR; Q4QXX9; -.
DR STRING; 9598.ENSPTRP00000005975; -.
DR PaxDb; Q4QXX9; -.
DR GeneID; 466465; -.
DR KEGG; ptr:466465; -.
DR CTD; 117194; -.
DR eggNOG; ENOG502RTWA; Eukaryota.
DR HOGENOM; CLU_009579_4_1_1; -.
DR InParanoid; Q4QXX9; -.
DR OrthoDB; 1123658at2759; -.
DR TreeFam; TF336336; -.
DR Proteomes; UP000002277; Unplaced.
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;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..329
FT /note="Mas-related G-protein coupled receptor member X2"
FT /id="PRO_0000069778"
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..183
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..263
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 61
FT /note="K -> R (in Ref. 1; AAW70042)"
SQ SEQUENCE 329 AA; 36849 MW; F96C0BC5E876E268 CRC64;
MDPTTPAWGT ESTTMNGNDQ ALPLFCGKET LISVFLILFI ALVGLVGNGF VLWLLGFRMR
KNAFSVYVLS LAGADFLFLC FQIINCLVYL SNVFCSISIN FPSFFITVMT CAYLAGLSML
STISTERCLS VLWPIWYRCR RPRHLSAVAC VLLWALSLLL SILEGKFCGL FGDGDSGWCQ
TFDLITAAWL IFLFMVLCGS SLALLVRILC GSRGLPLTRL YLTILLTVLV FLLCGLPFGI
QWFLILWIWK NSDVLFCHIH PVSVVLSSLN SSANPIIYFF VGSFRKQWRL QQPILKLALQ
RALQDIAEVD HSEGCFRQGT PEMSRSSLV
