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   27-MAR-2024, entry version 118.
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   ChEMBL; CHEMBL5169153; -.
DR   GlyCosmos; Q3KNA1; 3 sites, No reported glycans.
DR   GlyGen; Q3KNA1; 3 sites.
DR   iPTMnet; Q3KNA1; -.
DR   PhosphoSitePlus; Q3KNA1; -.
DR   PaxDb; 10090-ENSMUSP00000061878; -.
DR   DNASU; 243979; -.
DR   Ensembl; ENSMUST00000052730.3; ENSMUSP00000061878.2; ENSMUSG00000050425.3.
DR   GeneID; 243979; -.
DR   KEGG; mmu:243979; -.
DR   UCSC; uc009hat.2; mouse.
DR   AGR; MGI:2441674; -.
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; NAIVLWF; -.
DR   OrthoDB; 4338913at2759; -.
DR   PhylomeDB; Q3KNA1; -.
DR   TreeFam; TF336336; -.
DR   BioGRID-ORCS; 243979; 2 hits in 76 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 cell types or tissues.
DR   ExpressionAtlas; Q3KNA1; baseline and differential.
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:0004888; F:transmembrane signaling receptor activity; 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   CDD; cd15107; 7tmA_MrgprB; 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; IPR026234; MRGPCRFAMILY.
DR   PANTHER; PTHR11334; MAS-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR11334:SF65; MAS-RELATED G-PROTEIN COUPLED RECEPTOR MRG-RELATED; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR02108; MRGPCRFAMILY.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
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
//