ID T2R50_HUMAN Reviewed; 299 AA. AC P59544; P59545; Q2M255; Q645Y0; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 24-JAN-2024, entry version 153. DE RecName: Full=Taste receptor type 2 member 50; DE Short=T2R50; DE AltName: Full=Taste receptor type 2 member 51; DE Short=T2R51; GN Name=TAS2R50; 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], AND VARIANT TYR-203. RX PubMed=12379855; DOI=10.1038/ng1014; RA Bufe B., Hofmann T., Krautwurst D., Raguse J.-D., Meyerhof W.; RT "The human TAS2R16 receptor mediates bitter taste in response to beta- RT glucopyranosides."; RL Nat. Genet. 32:397-401(2002). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=12584440; DOI=10.1159/000068546; RA Conte C., Ebeling M., Marcuz A., Nef P., Andres-Barquin P.J.; RT "Identification and characterization of human taste receptor genes RT belonging to the TAS2R family."; RL Cytogenet. Genome Res. 98:45-53(2002). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=15496549; DOI=10.1093/molbev/msi027; RA Fischer A., Gilad Y., Man O., Paeaebo S.; RT "Evolution of bitter taste receptors in humans and apes."; RL Mol. Biol. Evol. 22:432-436(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 REVIEW. RX PubMed=12139982; DOI=10.1016/s0959-4388(02)00345-8; RA Montmayeur J.-P., Matsunami H.; RT "Receptors for bitter and sweet taste."; RL Curr. Opin. Neurobiol. 12:366-371(2002). RN [7] RP REVIEW. RX PubMed=11696554; DOI=10.1074/jbc.r100054200; RA Margolskee R.F.; RT "Molecular mechanisms of bitter and sweet taste transduction."; RL J. Biol. Chem. 277:1-4(2002). RN [8] RP REVIEW. RX PubMed=12581520; DOI=10.1016/s0092-8674(03)00071-0; RA Zhang Y., Hoon M.A., Chandrashekar J., Mueller K.L., Cook B., Wu D., RA Zuker C.S., Ryba N.J.; RT "Coding of sweet, bitter, and umami tastes: different receptor cells RT sharing similar signaling pathways."; RL Cell 112:293-301(2003). CC -!- FUNCTION: Receptor that may play a role in the perception of bitterness CC and is gustducin-linked. May play a role in sensing the chemical CC composition of the gastrointestinal content. The activity of this CC receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation CC and lead to the gating of TRPM5 (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the CC tongue and exclusively in gustducin-positive cells. CC -!- MISCELLANEOUS: Most taste cells may be activated by a limited number of CC bitter compounds; individual taste cells can discriminate among bitter CC stimuli. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor T2R family. CC {ECO:0000305}. 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; AF494235; AAM19326.1; -; Genomic_DNA. DR EMBL; AY114088; AAM63538.1; -; Genomic_DNA. DR EMBL; AY724937; AAU21139.1; -; Genomic_DNA. DR EMBL; AC018630; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC112100; AAI12101.1; -; mRNA. DR CCDS; CCDS8638.1; -. DR RefSeq; NP_795371.2; NM_176890.2. DR AlphaFoldDB; P59544; -. DR SMR; P59544; -. DR BioGRID; 129251; 26. DR STRING; 9606.ENSP00000424040; -. DR ChEMBL; CHEMBL3559706; -. DR GuidetoPHARMACOLOGY; 677; -. DR GlyCosmos; P59544; 1 site, No reported glycans. DR GlyGen; P59544; 1 site. DR BioMuta; TAS2R50; -. DR DMDM; 296452919; -. DR PaxDb; 9606-ENSP00000424040; -. DR Antibodypedia; 23416; 51 antibodies from 15 providers. DR DNASU; 259296; -. DR Ensembl; ENST00000506868.1; ENSP00000424040.1; ENSG00000212126.3. DR Ensembl; ENST00000575654.1; ENSP00000458551.1; ENSG00000273431.1. DR Ensembl; ENST00000613831.1; ENSP00000479785.1; ENSG00000276167.1. DR GeneID; 259296; -. DR KEGG; hsa:259296; -. DR MANE-Select; ENST00000506868.1; ENSP00000424040.1; NM_176890.2; NP_795371.2. DR UCSC; uc001qzl.2; human. DR AGR; HGNC:18882; -. DR CTD; 259296; -. DR DisGeNET; 259296; -. DR GeneCards; TAS2R50; -. DR HGNC; HGNC:18882; TAS2R50. DR HPA; ENSG00000212126; Not detected. DR MIM; 609627; gene. DR neXtProt; NX_P59544; -. DR OpenTargets; ENSG00000212126; -. DR PharmGKB; PA38736; -. DR VEuPathDB; HostDB:ENSG00000212126; -. DR eggNOG; ENOG502TE6U; Eukaryota. DR GeneTree; ENSGT01100000263477; -. DR HOGENOM; CLU_072337_2_0_1; -. DR InParanoid; P59544; -. DR OMA; ILCQIRC; -. DR OrthoDB; 5306466at2759; -. DR PhylomeDB; P59544; -. DR TreeFam; TF335891; -. DR PathwayCommons; P59544; -. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-420499; Class C/3 (Metabotropic glutamate/pheromone receptors). DR Reactome; R-HSA-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste. DR BioGRID-ORCS; 259296; 12 hits in 1101 CRISPR screens. DR GeneWiki; TAS2R50; -. DR GenomeRNAi; 259296; -. DR Pharos; P59544; Tchem. DR PRO; PR:P59544; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P59544; Protein. DR Bgee; ENSG00000212126; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 34 other cell types or tissues. DR GO; GO:0016020; C:membrane; IC:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0033038; F:bitter taste receptor activity; IDA:UniProtKB. DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW. DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IDA:UniProtKB. DR CDD; cd15027; 7tm_TAS2R43-like; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR007960; TAS2R. DR PANTHER; PTHR11394; TASTE RECEPTOR TYPE 2; 1. DR PANTHER; PTHR11394:SF43; TASTE RECEPTOR TYPE 2 MEMBER 50; 1. DR Pfam; PF05296; TAS2R; 1. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR Genevisible; P59544; HS. PE 2: Evidence at transcript level; KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Reference proteome; Sensory transduction; Taste; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1..299 FT /note="Taste receptor type 2 member 50" FT /id="PRO_0000082337" FT TOPO_DOM 1 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 2..22 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 23..55 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 56..76 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 77..87 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 88..108 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 109..126 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 127..147 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 148..181 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 182..202 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 203..229 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 230..250 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 251..259 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 260..280 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 281..299 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 161 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 203 FT /note="C -> Y (in dbSNP:rs1376251)" FT /evidence="ECO:0000269|PubMed:12379855" FT /id="VAR_024187" SQ SEQUENCE 299 AA; 34558 MW; D5C3E41E1B370E6A CRC64; MITFLYIFFS ILIMVLFVLG NFANGFIALV NFIDWVKRKK ISSADQILTA LAVSRIGLLW ALLLNWYLTV LNPAFYSVEL RITSYNAWVV TNHFSMWLAA NLSIFYLLKI ANFSNLLFLH LKRRVRSVIL VILLGTLIFL VCHLLVANMD ESMWAEEYEG NMTGKMKLRN TVHLSYLTVT TLWSFIPFTL SLISFLMLIC SLCKHLKKMQ LHGEGSQDLS TKVHIKALQT LISFLLLCAI FFLFLIVSVW SPRRLRNDPV VMVSKAVGNI YLAFDSFILI WRTKKLKHTF LLILCQIRC //