TAAR1_HUMAN
ID TAAR1_HUMAN Reviewed; 339 AA.
AC Q96RJ0; Q2M1W5; Q3MIH8; Q5VUQ1;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Trace amine-associated receptor 1;
DE Short=TaR-1;
DE Short=Trace amine receptor 1;
GN Name=TAAR1; Synonyms=TA1, TAR1, TRAR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11459929; DOI=10.1073/pnas.151105198;
RA Borowsky B., Adham N., Jones K.A., Raddatz R., Artymyshyn R.,
RA Ogozalek K.L., Durkin M.M., Lakhlani P.P., Bonini J.A., Pathirana S.,
RA Boyle N., Pu X., Kouranova E., Lichtblau H., Ochoa F.Y., Branchek T.A.,
RA Gerald C.;
RT "Trace amines: identification of a family of mammalian G protein-coupled
RT receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8966-8971(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11723224; DOI=10.1124/mol.60.6.1181;
RA Bunzow J.R., Sonders M.S., Arttamangkul S., Harrison L.M., Zhang G.,
RA Quigley D.I., Darland T., Suchland K.L., Pasumamula S., Kennedy J.L.,
RA Olson S.B., Magenis R.E., Amara S.G., Grandy D.K.;
RT "Amphetamine, 3,4-methylenedioxymethamphetamine, lysergic acid
RT diethylamide, and metabolites of the catecholamine neurotransmitters are
RT agonists of a rat trace amine receptor.";
RL Mol. Pharmacol. 60:1181-1188(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Placenta;
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 [6]
RP FUNCTION.
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).
CC -!- FUNCTION: Receptor for trace amines, including beta-phenylethylamine
CC (b-PEA), p-tyramine (p-TYR), octopamine and tryptamine, with highest
CC affinity for b-PEA and p-TYR. Unresponsive to classical biogenic
CC amines, such as epinephrine and histamine and only partially activated
CC by dopamine and serotonin. Trace amines are biogenic amines present in
CC very low levels in mammalian tissues. Although some trace amines have
CC clearly defined roles as neurotransmitters in invertebrates, the extent
CC to which they function as true neurotransmitters in vertebrates has
CC remained speculative. Trace amines are likely to be involved in a
CC variety of physiological functions that have yet to be fully
CC understood. The signal transduced by this receptor is mediated by the
CC G(s)-class of G-proteins which activate adenylate cyclase.
CC {ECO:0000269|PubMed:15718104}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Detected in low levels in discrete regions within
CC the central nervous system and in several peripheral tissues.
CC Moderately expressed in stomach. Low levels in amygdala, kidney, and
CC lung, and small intestine. Trace amounts in cerebellum, dorsal root
CC ganglia, hippocampus, hypothalamus, liver, medulla, pancreas,
CC pituitary, pontine reticular formation, prostate, skeletal muscle and
CC spleen.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF380185; AAK71236.1; -; Genomic_DNA.
DR EMBL; AF200627; AAG17112.1; -; Genomic_DNA.
DR EMBL; AY180374; AAO22154.1; -; mRNA.
DR EMBL; AL513524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101825; AAI01826.1; -; mRNA.
DR EMBL; BC112194; AAI12195.1; -; mRNA.
DR CCDS; CCDS5158.1; -.
DR RefSeq; NP_612200.1; NM_138327.2.
DR AlphaFoldDB; Q96RJ0; -.
DR SMR; Q96RJ0; -.
DR BioGRID; 126416; 6.
DR IntAct; Q96RJ0; 4.
DR MINT; Q96RJ0; -.
DR STRING; 9606.ENSP00000275216; -.
DR BindingDB; Q96RJ0; -.
DR ChEMBL; CHEMBL5857; -.
DR DrugBank; DB00182; Amphetamine.
DR DrugBank; DB01576; Dextroamphetamine.
DR DrugBank; DB01255; Lisdexamfetamine.
DR DrugBank; DB01577; Metamfetamine.
DR DrugBank; DB06714; Propylhexedrine.
DR DrugBank; DB15665; SEP-363856.
DR DrugCentral; Q96RJ0; -.
DR GuidetoPHARMACOLOGY; 364; -.
DR GlyGen; Q96RJ0; 2 sites.
DR iPTMnet; Q96RJ0; -.
DR PhosphoSitePlus; Q96RJ0; -.
DR BioMuta; TAAR1; -.
DR DMDM; 38258636; -.
DR PaxDb; Q96RJ0; -.
DR PRIDE; Q96RJ0; -.
DR ProteomicsDB; 77969; -.
DR Antibodypedia; 19712; 178 antibodies from 28 providers.
DR DNASU; 134864; -.
DR Ensembl; ENST00000275216.3; ENSP00000275216.1; ENSG00000146399.3.
DR GeneID; 134864; -.
DR KEGG; hsa:134864; -.
DR MANE-Select; ENST00000275216.3; ENSP00000275216.1; NM_138327.4; NP_612200.1.
DR UCSC; uc003qdm.1; human.
DR CTD; 134864; -.
DR DisGeNET; 134864; -.
DR GeneCards; TAAR1; -.
DR HGNC; HGNC:17734; TAAR1.
DR HPA; ENSG00000146399; Tissue enriched (stomach).
DR MIM; 609333; gene.
DR neXtProt; NX_Q96RJ0; -.
DR OpenTargets; ENSG00000146399; -.
DR PharmGKB; PA134921784; -.
DR VEuPathDB; HostDB:ENSG00000146399; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00950000182934; -.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; Q96RJ0; -.
DR OMA; YIPGFVM; -.
DR OrthoDB; 913195at2759; -.
DR PhylomeDB; Q96RJ0; -.
DR TreeFam; TF343107; -.
DR PathwayCommons; Q96RJ0; -.
DR Reactome; R-HSA-375280; Amine ligand-binding receptors.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; Q96RJ0; -.
DR BioGRID-ORCS; 134864; 34 hits in 1040 CRISPR screens.
DR GeneWiki; TAAR1; -.
DR GenomeRNAi; 134864; -.
DR Pharos; Q96RJ0; Tclin.
DR PRO; PR:Q96RJ0; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96RJ0; protein.
DR Bgee; ENSG00000146399; Expressed in islet of Langerhans and 17 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:CACAO.
DR GO; GO:0001594; F:trace-amine receptor activity; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR009133; TAAR1.
DR InterPro; IPR009132; TAAR_fam.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01831; TRACEAMINE1R.
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..339
FT /note="Trace amine-associated receptor 1"
FT /id="PRO_0000070141"
FT TOPO_DOM 1..25
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..98
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 23
FT /note="R -> C (in dbSNP:rs8192618)"
FT /id="VAR_049445"
FT VARIANT 252
FT /note="T -> A (in dbSNP:rs6926857)"
FT /id="VAR_049446"
SQ SEQUENCE 339 AA; 39092 MW; 5E72FA61CEFAC0E0 CRC64;
MMPFCHNIIN ISCVKNNWSN DVRASLYSLM VLIILTTLVG NLIVIVSISH FKQLHTPTNW
LIHSMATVDF LLGCLVMPYS MVRSAEHCWY FGEVFCKIHT STDIMLSSAS IFHLSFISID
RYYAVCDPLR YKAKMNILVI CVMIFISWSV PAVFAFGMIF LELNFKGAEE IYYKHVHCRG
GCSVFFSKIS GVLTFMTSFY IPGSIMLCVY YRIYLIAKEQ ARLISDANQK LQIGLEMKNG
ISQSKERKAV KTLGIVMGVF LICWCPFFIC TVMDPFLHYI IPPTLNDVLI WFGYLNSTFN
PMVYAFFYPW FRKALKMMLF GKIFQKDSSR CKLFLELSS
