T2R43_HUMAN
ID T2R43_HUMAN Reviewed; 309 AA.
AC P59537; P59546; Q645X4;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Taste receptor type 2 member 43;
DE Short=T2R43;
DE AltName: Full=Taste receptor type 2 member 52;
DE Short=T2R52;
GN Name=TAS2R43;
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=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).
RN [9]
RP ACTIVATION BY SACCHARIN AND ACESULFAME K.
RX PubMed=15537898; DOI=10.1523/jneurosci.1225-04.2004;
RA Kuhn C., Bufe B., Winnig M., Hofmann T., Frank O., Behrens M.,
RA Lewtschenko T., Slack J.P., Ward C.D., Meyerhof W.;
RT "Bitter taste receptors for saccharin and acesulfame K.";
RL J. Neurosci. 24:10260-10265(2004).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19628819; DOI=10.1126/science.1173869;
RA Shah A.S., Ben-Shahar Y., Moninger T.O., Kline J.N., Welsh M.J.;
RT "Motile cilia of human airway epithelia are chemosensory.";
RL Science 325:1131-1134(2009).
CC -!- FUNCTION: Gustducin-coupled receptor immplicated in the perception of
CC bitter compounds in the oral cavity and the gastrointestinal tract.
CC Signals through PLCB2 and the calcium-regulated cation channel TRPM5.
CC Activated by the sulfonyl amide sweeteners saccharin and acesulfame K.
CC In airway epithelial cells, binding of bitter compounds increases the
CC intracellular calcium ion concentration and stimulates ciliary beat
CC frequency. May act as chemosensory receptors in airway epithelial cells
CC to detect and eliminate potential noxious agents from the airways (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19628819}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:19628819}. Cell projection,
CC cilium membrane {ECO:0000269|PubMed:19628819}. Note=In airway
CC epithelial cells, localizes to motile cilia.
CC -!- TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the
CC tongue and exclusively in gustducin-positive cells. Expressed in airway
CC epithelia. {ECO:0000269|PubMed:19628819}.
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 -!- WEB RESOURCE: Name=Protein Spotlight; Note=A tail of protection - Issue
CC 119 of July 2010;
CC URL="https://web.expasy.org/spotlight/back_issues/119";
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DR EMBL; AF494237; AAM19328.1; -; Genomic_DNA.
DR EMBL; AY114089; AAM63539.1; -; Genomic_DNA.
DR EMBL; AY724943; AAU21145.1; -; Genomic_DNA.
DR EMBL; AC018630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117423; AAI17424.1; -; mRNA.
DR CCDS; CCDS53749.1; -.
DR RefSeq; NP_795365.2; NM_176884.2.
DR AlphaFoldDB; P59537; -.
DR SMR; P59537; -.
DR BioGRID; 129244; 2.
DR STRING; 9606.ENSP00000431719; -.
DR ChEMBL; CHEMBL4523251; -.
DR GlyGen; P59537; 2 sites.
DR BioMuta; TAS2R43; -.
DR DMDM; 374095447; -.
DR PaxDb; P59537; -.
DR PeptideAtlas; P59537; -.
DR PRIDE; P59537; -.
DR Antibodypedia; 57634; 77 antibodies from 17 providers.
DR DNASU; 259289; -.
DR Ensembl; ENST00000531678.1; ENSP00000431719.1; ENSG00000255374.3.
DR Ensembl; ENST00000571879.1; ENSP00000458723.1; ENSG00000262612.3.
DR GeneID; 259289; -.
DR KEGG; hsa:259289; -.
DR MANE-Select; ENST00000531678.1; ENSP00000431719.1; NM_176884.2; NP_795365.2.
DR UCSC; uc001qzq.1; human.
DR CTD; 259289; -.
DR DisGeNET; 259289; -.
DR GeneCards; TAS2R43; -.
DR HGNC; HGNC:18875; TAS2R43.
DR HPA; ENSG00000255374; Not detected.
DR MIM; 612668; gene.
DR neXtProt; NX_P59537; -.
DR PharmGKB; PA38729; -.
DR VEuPathDB; HostDB:ENSG00000255374; -.
DR eggNOG; ENOG502TE6U; Eukaryota.
DR GeneTree; ENSGT00960000186648; -.
DR InParanoid; P59537; -.
DR OMA; IRIMYPS; -.
DR OrthoDB; 1339037at2759; -.
DR PhylomeDB; P59537; -.
DR TreeFam; TF335891; -.
DR PathwayCommons; P59537; -.
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; 259289; 15 hits in 990 CRISPR screens.
DR GeneWiki; TAS2R43; -.
DR GenomeRNAi; 259289; -.
DR Pharos; P59537; Tchem.
DR PRO; PR:P59537; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P59537; protein.
DR Bgee; ENSG00000255374; Expressed in adrenal tissue and 72 other tissues.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031514; C:motile cilium; IDA: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:0008527; F:taste receptor activity; IDA:HGNC-UCL.
DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IC:HGNC-UCL.
DR InterPro; IPR007960; TAS2R.
DR Pfam; PF05296; TAS2R; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cilium; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Sensory transduction;
KW Taste; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..309
FT /note="Taste receptor type 2 member 43"
FT /id="PRO_0000082302"
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..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..86
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..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..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..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..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 35
FT /note="W -> S (in Ref. 1; AAM19328, 3; AAU21145 and 5;
FT AAI17424)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="H -> R (in Ref. 1; AAM19328, 3; AAU21145 and 5;
FT AAI17424)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 35599 MW; 3B4FCD1089EB6857 CRC64;
MITFLPIIFS SLVVVTFVIG NFANGFIALV NSIEWFKRQK ISFADQILTA LAVSRVGLLW
VLLLNWYSTV LNPAFNSVEV RTTAYNIWAV INHFSNWLAT TLSIFYLLKI ANFSNFIFLH
LKRRVKSVIL VMLLGPLLFL ACHLFVINMN EIVRTKEFEG NMTWKIKLKS AMYFSNMTVT
MVANLVPFTL TLLSFMLLIC SLCKHLKKMQ LHGKGSQDPS TKVHIKALQT VISFLLLCAI
YFLSIMISVW SFGSLENKPV FMFCKAIRFS YPSIHPFILI WGNKKLKQTF LSVFWQMRYW
VKGEKTSSP
