MRGB2_MOUSE
ID MRGB2_MOUSE Reviewed; 338 AA.
AC Q3KNA1; Q8CDY4; Q91ZC2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Mas-related G-protein coupled receptor member B2;
GN Name=Mrgprb2; Synonyms=Mrgb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=11551509; DOI=10.1016/s0092-8674(01)00483-4;
RA Dong X., Han S.-K., Zylka M.J., Simon M.I., Anderson D.J.;
RT "A diverse family of GPCRs expressed in specific subsets of nociceptive
RT sensory neurons.";
RL Cell 106:619-632(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25517090; DOI=10.1038/nature14022;
RA McNeil B.D., Pundir P., Meeker S., Han L., Undem B.J., Kulka M., Dong X.;
RT "Identification of a mast-cell-specific receptor crucial for pseudo-
RT allergic drug reactions.";
RL Nature 519:237-241(2015).
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 (PubMed:25517090).
CC {ECO:0000269|PubMed:25517090}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Mast cell-specific. {ECO:0000269|PubMed:25517090}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in normal conditions.
CC Absence of pseudo-allergic reactions in response to small-molecule
CC therapeutic drugs: secretagogue-induced histamine release, inflammation
CC and airway contraction are abolished. {ECO:0000269|PubMed:25517090}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Mas
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: In spite of its official gene name, this protein may be the
CC functional ortholog of human MRGPRX2, in terms of expression pattern
CC and pharmacology. {ECO:0000269|PubMed:25517090}.
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DR EMBL; AY042200; AAK91796.1; -; Genomic_DNA.
DR EMBL; AK029369; BAC26422.1; -; mRNA.
DR EMBL; BC107390; AAI07391.1; -; mRNA.
DR EMBL; BC107391; AAI07392.1; -; mRNA.
DR CCDS; CCDS21303.1; -.
DR RefSeq; NP_780740.2; NM_175531.4.
DR AlphaFoldDB; Q3KNA1; -.
DR SMR; Q3KNA1; -.
DR STRING; 10090.ENSMUSP00000061878; -.
DR GlyGen; Q3KNA1; 3 sites.
DR iPTMnet; Q3KNA1; -.
DR PhosphoSitePlus; Q3KNA1; -.
DR PaxDb; Q3KNA1; -.
DR PRIDE; Q3KNA1; -.
DR DNASU; 243979; -.
DR Ensembl; ENSMUST00000052730; ENSMUSP00000061878; ENSMUSG00000050425.
DR GeneID; 243979; -.
DR KEGG; mmu:243979; -.
DR UCSC; uc009hat.2; mouse.
DR CTD; 243979; -.
DR MGI; MGI:2441674; Mrgprb2.
DR VEuPathDB; HostDB:ENSMUSG00000050425; -.
DR eggNOG; ENOG502RTWA; Eukaryota.
DR GeneTree; ENSGT01030000234639; -.
DR HOGENOM; CLU_009579_4_1_1; -.
DR InParanoid; Q3KNA1; -.
DR OMA; LEWRFCD; -.
DR OrthoDB; 1123658at2759; -.
DR PhylomeDB; Q3KNA1; -.
DR TreeFam; TF336336; -.
DR BioGRID-ORCS; 243979; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q3KNA1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3KNA1; protein.
DR Bgee; ENSMUSG00000050425; Expressed in zone of skin and 6 other tissues.
DR ExpressionAtlas; Q3KNA1; baseline and differential.
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; ISO:MGI.
DR GO; GO:0042923; F:neuropeptide binding; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0045576; P:mast cell activation; ISO:MGI.
DR GO; GO:0043303; P:mast cell degranulation; ISO:MGI.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISO:MGI.
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 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..338
FT /note="Mas-related G-protein coupled receptor member B2"
FT /id="PRO_0000304878"
FT TOPO_DOM 1..40
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 310..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 28
FT /note="I -> F (in Ref. 2; BAC26422)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="E -> K (in Ref. 3; AAI07391/AAI07392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 38832 MW; 1B0A091D67C868B9 CRC64;
MSGDFLIKNL STSAWKTNIT VLNGSYYIDT SVCVTRNQAM ILLSIIISLV GMGLNAIVLW
FLGIRMHTNA FTVYILNLAM ADFLYLCSQF VICLLIAFYI FYSIDINIPL VLYVVPIFAY
LSGLSILSTI SIERCLSVIW PIWYRCKRPR HTSAITCFVL WVMSLLLGLL EGKACGLLFN
SFDSYWCETF DVITNIWSVV FFGVLCGSSL TLLVRIFCGS QRIPMTRLYV TITLTVLVFL
IFGLPFGIYW ILYQWISNFY YVEICNFYLE ILFLSCVNSC MNPIIYFLVG SIRHRRFRRK
TLKLLLQRAM QDTPEEEQSG NKSSSEHPEE LETVQSCS
