TAA7B_MOUSE
ID TAA7B_MOUSE Reviewed; 358 AA.
AC Q5QD11;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Trace amine-associated receptor 7b;
DE Short=TaR-7b;
DE Short=Trace amine receptor 7b;
DE Short=mTaar7b;
GN Name=Taar7b; Synonyms=Gm698;
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=15718104; DOI=10.1016/j.ygeno.2004.11.010;
RA Lindemann L., Ebeling M., Kratochwil N.A., Bunzow J.R., Grandy D.K.,
RA Hoener M.C.;
RT "Trace amine-associated receptors form structurally and functionally
RT distinct subfamilies of novel G protein-coupled receptors.";
RL Genomics 85:372-385(2005).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=16878137; DOI=10.1038/nature05066;
RA Liberles S.D., Buck L.B.;
RT "A second class of chemosensory receptors in the olfactory epithelium.";
RL Nature 442:645-650(2006).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=23624375; DOI=10.1038/nature12114;
RA Dewan A., Pacifico R., Zhan R., Rinberg D., Bozza T.;
RT "Non-redundant coding of aversive odours in the main olfactory pathway.";
RL Nature 497:486-489(2013).
CC -!- FUNCTION: Orphan olfactory receptor specific for trace amines.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in neurons of the olfactory
CC epithelium. {ECO:0000269|PubMed:16878137}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Taar2, Taar3, Taar4, Taar5, Taar6,
CC Taar7a, Taar7b, Taar7d, Taar7e, Taar7f, Taar8a, Taar8b, Taar8c and
CC Taar9 show no visible phenotype or behavioral deficits. They however
CC show an absence of aversion to low concentrations of amines such as 2-
CC phenylethylamine, isopentylamine, N-methylpiperidine and cadaverine.
CC {ECO:0000269|PubMed:23624375}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY702332; AAV70142.1; -; Genomic_DNA.
DR CCDS; CCDS23741.1; -.
DR RefSeq; NP_001010827.1; NM_001010827.1.
DR AlphaFoldDB; Q5QD11; -.
DR SMR; Q5QD11; -.
DR STRING; 10090.ENSMUSP00000090328; -.
DR ChEMBL; CHEMBL2176792; -.
DR GlyGen; Q5QD11; 3 sites.
DR PaxDb; Q5QD11; -.
DR PRIDE; Q5QD11; -.
DR DNASU; 209517; -.
DR Ensembl; ENSMUST00000092658; ENSMUSP00000090328; ENSMUSG00000095171.
DR GeneID; 209517; -.
DR KEGG; mmu:209517; -.
DR UCSC; uc007eqk.1; mouse.
DR CTD; 209517; -.
DR MGI; MGI:3527438; Taar7b.
DR VEuPathDB; HostDB:ENSMUSG00000095171; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000160273; -.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; Q5QD11; -.
DR OMA; SQLCYEN; -.
DR OrthoDB; 973471at2759; -.
DR PhylomeDB; Q5QD11; -.
DR TreeFam; TF343107; -.
DR BioGRID-ORCS; 209517; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q5QD11; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q5QD11; protein.
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:0001594; F:trace-amine receptor activity; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR009132; TAAR_fam.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01830; TRACEAMINER.
DR SMART; SM01381; 7TM_GPCR_Srsx; 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; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..358
FT /note="Trace amine-associated receptor 7b"
FT /id="PRO_0000070164"
FT TOPO_DOM 1..47
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..143
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..309
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..333
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 358 AA; 40231 MW; 732A59E89E27B6DE CRC64;
MATDNDSFPW DQDSILSSDM FSATSTELCY ENLNRSCVRS PYSPGPRLIL YAVFGFGAAL
AVCGNLLVMT SILHFRQLHS PANFLVVSLA CADFLVGLTV MPFSTVRSVE GCWYFGESYC
KLHTCFDVSF CYCSIFHLCF ISVDRYIAVS DPLTYPTRFT AFVSGKCITF SWLLSTIYGF
SLLYTGANEA GLEDLVSALT CVGGCQLAVN QSWVFINFLL FLIPTLVMIT VYSKIFLIAK
QQAQNIEKMS KQTARASDSY KDRVAKRERK AAKTLGIAVA AFLLSWLPYF IDSIIDAFLG
FITPTYVYEI LVWIAYYNSA MNPLIYAFFY PWFRKAIKLI VSGKVLRENS STTNLFPE
