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   24-JAN-2024, entry version 148.
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   GlyCosmos; P59538; 1 site, No reported glycans.
DR   GlyGen; P59538; 1 site.
DR   iPTMnet; P59538; -.
DR   PhosphoSitePlus; P59538; -.
DR   BioMuta; TAS2R31; -.
DR   DMDM; 338817946; -.
DR   PaxDb; 9606-ENSP00000375093; -.
DR   ProteomicsDB; 57145; -.
DR   Antibodypedia; 57633; 86 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   AGR; HGNC:19113; -.
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; ENSGT01100000263477; -.
DR   HOGENOM; CLU_072337_2_0_1; -.
DR   InParanoid; P59538; -.
DR   OMA; FMICEAV; -.
DR   OrthoDB; 5306466at2759; -.
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; 10 hits in 1131 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 male germ line stem cell (sensu Vertebrata) in testis and 99 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:SF129; TASTE RECEPTOR TYPE 2 MEMBER 31; 1.
DR   Pfam; PF05296; TAS2R; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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
//