T2R31_HUMAN
ID T2R31_HUMAN Reviewed; 309 AA.
AC P59538; P59547; Q17R84; Q645X5;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Taste receptor type 2 member 31;
DE Short=T2R31;
DE AltName: Full=Taste receptor type 2 member 44;
DE Short=T2R44;
DE AltName: Full=Taste receptor type 2 member 53;
DE Short=T2R53;
GN Name=TAS2R31; Synonyms=TAS2R44;
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 MET-162.
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], AND VARIANTS MET-162; VAL-227 AND
RP ILE-240.
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).
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). Activated by the
CC sulfonyl amide sweeteners saccharin and acesulfame K. {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}.
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DR EMBL; AF494228; AAM19319.1; -; Genomic_DNA.
DR EMBL; AY114090; AAM63540.1; -; Genomic_DNA.
DR EMBL; AY724942; AAU21144.1; -; Genomic_DNA.
DR EMBL; AC018630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117421; AAI17422.1; -; mRNA.
DR CCDS; CCDS53747.1; -.
DR RefSeq; NP_795366.2; NM_176885.2.
DR AlphaFoldDB; P59538; -.
DR SMR; P59538; -.
DR BioGRID; 129245; 6.
DR STRING; 9606.ENSP00000375093; -.
DR BindingDB; P59538; -.
DR ChEMBL; CHEMBL2034804; -.
DR GuidetoPHARMACOLOGY; 674; -.
DR GlyGen; P59538; 1 site.
DR iPTMnet; P59538; -.
DR PhosphoSitePlus; P59538; -.
DR BioMuta; TAS2R31; -.
DR DMDM; 338817946; -.
DR PaxDb; P59538; -.
DR PRIDE; P59538; -.
DR ProteomicsDB; 57145; -.
DR Antibodypedia; 57633; 79 antibodies from 20 providers.
DR DNASU; 259290; -.
DR Ensembl; ENST00000390675.2; ENSP00000375093.2; ENSG00000256436.1.
DR Ensembl; ENST00000572376.1; ENSP00000459810.1; ENSG00000263097.3.
DR GeneID; 259290; -.
DR KEGG; hsa:259290; -.
DR MANE-Select; ENST00000390675.2; ENSP00000375093.2; NM_176885.2; NP_795366.2.
DR UCSC; uc001qzo.1; human.
DR CTD; 259290; -.
DR DisGeNET; 259290; -.
DR GeneCards; TAS2R31; -.
DR HGNC; HGNC:19113; TAS2R31.
DR HPA; ENSG00000256436; Not detected.
DR MIM; 612669; gene.
DR neXtProt; NX_P59538; -.
DR OpenTargets; ENSG00000256436; -.
DR VEuPathDB; HostDB:ENSG00000256436; -.
DR eggNOG; ENOG502TE6U; Eukaryota.
DR GeneTree; ENSGT00960000186648; -.
DR HOGENOM; CLU_072337_2_0_1; -.
DR InParanoid; P59538; -.
DR OMA; FMICEAV; -.
DR OrthoDB; 1339037at2759; -.
DR PhylomeDB; P59538; -.
DR TreeFam; TF335891; -.
DR PathwayCommons; P59538; -.
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; 259290; 9 hits in 1059 CRISPR screens.
DR GeneWiki; TAS2R31; -.
DR GenomeRNAi; 259290; -.
DR Pharos; P59538; Tchem.
DR PRO; PR:P59538; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P59538; protein.
DR Bgee; ENSG00000256436; Expressed in adrenal tissue and 98 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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 InterPro; IPR007960; TAS2R.
DR Pfam; PF05296; TAS2R; 1.
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..309
FT /note="Taste receptor type 2 member 31"
FT /id="PRO_0000082309"
FT TOPO_DOM 1..2
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..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..100
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..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..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 35
FT /note="R -> W (in dbSNP:rs10845295)"
FT /id="VAR_030684"
FT VARIANT 162
FT /note="L -> M (in dbSNP:rs10743938)"
FT /evidence="ECO:0000269|PubMed:12379855,
FT ECO:0000269|PubMed:15496549"
FT /id="VAR_030685"
FT VARIANT 217
FT /note="Q -> E (in dbSNP:rs10845294)"
FT /id="VAR_030686"
FT VARIANT 227
FT /note="A -> V (in dbSNP:rs10845293)"
FT /evidence="ECO:0000269|PubMed:15496549"
FT /id="VAR_030687"
FT VARIANT 240
FT /note="V -> I (in dbSNP:rs10772423)"
FT /evidence="ECO:0000269|PubMed:15496549"
FT /id="VAR_030688"
FT VARIANT 276
FT /note="P -> R (in dbSNP:rs12318612)"
FT /id="VAR_062090"
SQ SEQUENCE 309 AA; 35278 MW; 56926C025E4C6358 CRC64;
MTTFIPIIFS SVVVVLFVIG NFANGFIALV NSIERVKRQK ISFADQILTA LAVSRVGLLW
VLLLNWYSTV FNPAFYSVEV RTTAYNVWAV TGHFSNWLAT SLSIFYLLKI ANFSNLIFLH
LKRRVKSVIL VMLLGPLLFL ACQLFVINMK EIVRTKEYEG NLTWKIKLRS AVYLSDATVT
TLGNLVPFTL TLLCFLLLIC SLCKHLKKMQ LHGKGSQDPS TKVHIKALQT VIFFLLLCAV
YFLSIMISVW SFGSLENKPV FMFCKAIRFS YPSIHPFILI WGNKKLKQTF LSVLRQVRYW
VKGEKPSSP
