MRGB1_MOUSE
ID MRGB1_MOUSE Reviewed; 350 AA.
AC Q3UG61; A4FUT5; A4QMY7; Q3UFN5; Q3UFT1; Q3UFW7; Q3UFX0; Q3UFX7; Q3UFY5;
AC Q3UG23; Q3UG95; Q91ZC3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Mas-related G-protein coupled receptor member B1;
GN Name=Mrgprb1; Synonyms=Mrgb1;
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;
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] OF 14-350.
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).
CC -!- FUNCTION: Orphan receptor. Probably involved in the function of
CC nociceptive neurons. May regulate nociceptor function and/or
CC development, including the sensation or modulation of pain (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; AY042199; AAK91795.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK148044; BAE28310.1; -; mRNA.
DR EMBL; AK148052; BAE28314.1; -; mRNA.
DR EMBL; AK148074; BAE28326.1; -; mRNA.
DR EMBL; AK148108; BAE28348.1; -; mRNA.
DR EMBL; AK148114; BAE28352.1; -; mRNA.
DR EMBL; AK148166; BAE28386.1; -; mRNA.
DR EMBL; AK148226; BAE28424.1; -; mRNA.
DR EMBL; AK148241; BAE28432.1; -; mRNA.
DR EMBL; AK148253; BAE28439.1; -; mRNA.
DR EMBL; AK148256; BAE28442.1; -; mRNA.
DR EMBL; AK148273; BAE28451.1; -; mRNA.
DR EMBL; AK148279; BAE28455.1; -; mRNA.
DR EMBL; AK148322; BAE28479.1; -; mRNA.
DR EMBL; AK148388; BAE28525.1; -; mRNA.
DR EMBL; BC116396; AAI16397.1; -; mRNA.
DR EMBL; BC116395; AAI16396.1; -; mRNA.
DR CCDS; CCDS52257.1; -.
DR RefSeq; NP_991379.3; NM_205810.4.
DR AlphaFoldDB; Q3UG61; -.
DR SMR; Q3UG61; -.
DR STRING; 10090.ENSMUSP00000091946; -.
DR GlyGen; Q3UG61; 2 sites.
DR PaxDb; Q3UG61; -.
DR PRIDE; Q3UG61; -.
DR DNASU; 233231; -.
DR Ensembl; ENSMUST00000094384; ENSMUSP00000091946; ENSMUSG00000070547.
DR GeneID; 233231; -.
DR KEGG; mmu:233231; -.
DR UCSC; uc009hap.1; mouse.
DR CTD; 233231; -.
DR MGI; MGI:3033115; Mrgprb1.
DR VEuPathDB; HostDB:ENSMUSG00000070547; -.
DR eggNOG; ENOG502RTWA; Eukaryota.
DR GeneTree; ENSGT01030000234639; -.
DR HOGENOM; CLU_009579_4_1_1; -.
DR InParanoid; Q3UG61; -.
DR OMA; WVNSSAN; -.
DR OrthoDB; 1123658at2759; -.
DR PhylomeDB; Q3UG61; -.
DR TreeFam; TF336336; -.
DR BioGRID-ORCS; 233231; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Mrgprb1; mouse.
DR PRO; PR:Q3UG61; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3UG61; protein.
DR Bgee; ENSMUSG00000070547; Expressed in lip and 15 other tissues.
DR ExpressionAtlas; Q3UG61; baseline and differential.
DR Genevisible; Q3UG61; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..350
FT /note="Mas-related G-protein coupled receptor member B1"
FT /id="PRO_0000305585"
FT TOPO_DOM 1..46
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 51
FT /note="I -> V (in Ref. 2; BAE28439)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="E -> G (in Ref. 2; BAE28479)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="T -> A (in Ref. 2; BAE28525)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="P -> H (in Ref. 2; BAE28326/BAE28455/BAE28442)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="L -> P (in Ref. 2; BAE28314)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="A -> V (in Ref. 2; BAE28432)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 40161 MW; 4B00E727A9DBE992 CRC64;
MEQRTEIAPL LKMDLVIQDW TINITALKES NDNGISFCEV VSRTMTFLSL IIALVGLVGN
ATVLWFLGFQ MSRNAFSVYI LNLAGADFVF MCFQIVHCFY IILDIYFIPT NFFSSYTMVL
NIAYLSGLSI LTVISTERFL SVMWPIWYRC QRPRHTSAVI CTVLWVLSLV LSLLEGKECG
FLYYTSGPGL CKTFDLITTA WLIVLFVVLL GSSLALVLTI FCGLHKVPVT RLYVTIVFTV
LVFLIFGLPY GIYWFLLEWI REFHDNKPCG FRNVTIFLSC INSCANPIIY FLVGSIRHHR
FQRKTLKLLL QRAMQDSPEE EECGEMGSSR RPREIKTVWK GLRAALIRHK
