ID TAAR5_HUMAN Reviewed; 337 AA. AC O14804; D8KZS1; Q2M1V1; Q4VBL1; Q5VUQ3; Q6NTA8; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 2. DT 12-AUG-2020, entry version 150. DE RecName: Full=Trace amine-associated receptor 5; DE Short=TaR-5; DE Short=Trace amine receptor 5; DE Short=hTaar5; DE AltName: Full=Putative neurotransmitter receptor; GN Name=TAAR5; Synonyms=PNR; 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 [MRNA], AND TISSUE SPECIFICITY. RX PubMed=9464258; DOI=10.1006/bbrc.1997.7591; RA Zeng Z., Fan P., Rand E., Kyaw H., Su K., Madike V., Carter K.C., Li Y.; RT "Cloning of a putative human neurotransmitter receptor expressed in RT skeletal muscle and brain."; RL Biochem. Biophys. Res. Commun. 242:575-578(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=20559446; DOI=10.1371/journal.pone.0011133; RA Staubert C., Boselt I., Bohnekamp J., Rompler H., Enard W., Schoneberg T.; RT "Structural and functional evolution of the trace amine-associated RT receptors TAAR3, TAAR4 and TAAR5 in primates."; RL PLoS ONE 5:E11133-E11133(2010). 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 GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] 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 [7] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=23393561; DOI=10.1371/journal.pone.0054950; RA Wallrabenstein I., Kuklan J., Weber L., Zborala S., Werner M., RA Altmuller J., Becker C., Schmidt A., Hatt H., Hummel T., Gisselmann G.; RT "Human trace amine-associated receptor TAAR5 can be activated by RT trimethylamine."; RL PLoS ONE 8:E54950-E54950(2013). CC -!- FUNCTION: Olfactory receptor specific for trimethylamine, a trace CC amine. Also activated at lower level by dimethylethylamine. CC Trimethylamine is a bacterial metabolite found in some animal odors, CC and to humans it is a repulsive odor associated with bad breath and CC spoiled food. This receptor is probably mediated by the G(s)-class of CC G-proteins which activate adenylate cyclase. CC {ECO:0000269|PubMed:23393561}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23393561}; CC Multi-pass membrane protein {ECO:0000269|PubMed:23393561}. CC -!- TISSUE SPECIFICITY: Expressed almost exclusively in skeletal muscle and CC selected areas of the brain, such amygdala, hippocampus, caudate CC nucleus, thalamus and hypothalamus. Weak expression is also find in CC substantia nigra. {ECO:0000269|PubMed:9464258}. CC -!- MISCELLANEOUS: Polymorphic variants of this gene are not associated CC with specific anosmia for trimethylamine. CC {ECO:0000305|PubMed:23393561}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF021818; AAC39581.1; -; mRNA. DR EMBL; AY702306; AAV70123.1; -; Genomic_DNA. DR EMBL; FJ372547; ACP18682.1; -; Genomic_DNA. DR EMBL; AL513524; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW48025.1; -; Genomic_DNA. DR EMBL; BC069171; AAH69171.1; -; mRNA. DR EMBL; BC095541; AAH95541.1; -; mRNA. DR EMBL; BC112209; AAI12210.1; -; mRNA. DR EMBL; BC112211; AAI12212.1; -; mRNA. DR CCDS; CCDS5156.1; -. DR PIR; JC5832; JC5832. DR RefSeq; NP_003958.2; NM_003967.2. DR SMR; O14804; -. DR STRING; 9606.ENSP00000258034; -. DR ChEMBL; CHEMBL3714046; -. DR GlyGen; O14804; 1 site. DR PhosphoSitePlus; O14804; -. DR BioMuta; TAAR5; -. DR EPD; O14804; -. DR PaxDb; O14804; -. DR PeptideAtlas; O14804; -. DR PRIDE; O14804; -. DR ProteomicsDB; 48249; -. DR Antibodypedia; 19709; 215 antibodies. DR DNASU; 9038; -. DR Ensembl; ENST00000258034; ENSP00000258034; ENSG00000135569. DR GeneID; 9038; -. DR KEGG; hsa:9038; -. DR UCSC; uc003qdk.3; human. DR CTD; 9038; -. DR DisGeNET; 9038; -. DR EuPathDB; HostDB:ENSG00000135569.4; -. DR GeneCards; TAAR5; -. DR HGNC; HGNC:30236; TAAR5. DR HPA; ENSG00000135569; Not detected. DR MIM; 607405; gene. DR neXtProt; NX_O14804; -. DR OpenTargets; ENSG00000135569; -. DR PharmGKB; PA142670843; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT00940000161258; -. DR HOGENOM; CLU_009579_11_0_1; -. DR InParanoid; O14804; -. DR KO; K05051; -. DR OMA; YQWFRKA; -. DR OrthoDB; 913195at2759; -. DR PhylomeDB; O14804; -. DR TreeFam; TF343107; -. DR PathwayCommons; O14804; -. 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 BioGRID-ORCS; 9038; 5 hits in 863 CRISPR screens. DR GeneWiki; TAAR5; -. DR GenomeRNAi; 9038; -. DR Pharos; O14804; Tchem. DR PRO; PR:O14804; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; O14804; protein. DR Bgee; ENSG00000135569; Expressed in forebrain and 7 other tissues. DR Genevisible; O14804; HS. DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB. DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:GDB. DR GO; GO:0001594; F:trace-amine receptor activity; IBA:GO_Central. DR GO; GO:1990081; F:trimethylamine receptor activity; IDA:UniProtKB. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB. DR GO; GO:0007606; P:sensory perception of chemical stimulus; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. 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; Polymorphism; Receptor; Reference proteome; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1..337 FT /note="Trace amine-associated receptor 5" FT /id="PRO_0000070154" FT TOPO_DOM 1..34 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 35..55 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 56..70 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 71..91 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 92..109 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 110..130 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 131..154 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 155..175 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 176..204 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 205..225 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 226..253 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 254..274 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 275..284 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 285..307 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 308..337 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 21 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 99..192 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT VARIANT 272 FT /note="T -> M (in dbSNP:rs34746740)" FT /id="VAR_055923" FT VARIANT 330 FT /note="R -> C (in dbSNP:rs35839363)" FT /id="VAR_055924" FT CONFLICT 16 FT /note="F -> L (in Ref. 6; AAH95541)" FT /evidence="ECO:0000305" FT CONFLICT 40 FT /note="A -> T (in Ref. 1; AAC39581)" FT /evidence="ECO:0000305" FT CONFLICT 80 FT /note="D -> N (in Ref. 6; AAH69171)" FT /evidence="ECO:0000305" FT CONFLICT 257 FT /note="A -> V (in Ref. 1; AAC39581)" FT /evidence="ECO:0000305" FT CONFLICT 332 FT /note="V -> A (in Ref. 6; AAH95541)" FT /evidence="ECO:0000305" SQ SEQUENCE 337 AA; 38242 MW; 251DB41A13A5535A CRC64; MRAVFIQGAE EHPAAFCYQV NGSCPRTVHT LGIQLVIYLA CAAGMLIIVL GNVFVAFAVS YFKALHTPTN FLLLSLALAD MFLGLLVLPL STIRSVESCW FFGDFLCRLH TYLDTLFCLT SIFHLCFISI DRHCAICDPL LYPSKFTVRV ALRYILAGWG VPAAYTSLFL YTDVVETRLS QWLEEMPCVG SCQLLLNKFW GWLNFPLFFV PCLIMISLYV KIFVVATRQA QQITTLSKSL AGAAKHERKA AKTLGIAVGI YLLCWLPFTI DTMVDSLLHF ITPPLVFDIF IWFAYFNSAC NPIIYVFSYQ WFRKALKLTL SQKVFSPQTR TVDLYQE //