TAAR5_HUMAN
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 03-AUG-2022, entry version 157.
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}.
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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 AlphaFoldDB; O14804; -.
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 Antibodypedia; 19709; 228 antibodies from 29 providers.
DR DNASU; 9038; -.
DR Ensembl; ENST00000258034.4; ENSP00000258034.2; ENSG00000135569.5.
DR GeneID; 9038; -.
DR KEGG; hsa:9038; -.
DR MANE-Select; ENST00000258034.4; ENSP00000258034.2; NM_003967.3; NP_003958.2.
DR UCSC; uc003qdk.3; human.
DR CTD; 9038; -.
DR DisGeNET; 9038; -.
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 VEuPathDB; HostDB:ENSG00000135569; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000161258; -.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; O14804; -.
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; 6 hits in 1057 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 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; Receptor; Reference proteome; Transducer; Transmembrane;
KW 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
