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P59538 (T2R31_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Taste receptor type 2 member 31

Short name=T2R31
Alternative name(s):
Taste receptor type 2 member 44
Short name=T2R44
Taste receptor type 2 member 53
Short name=T2R53
Gene names
Name:TAS2R31
Synonyms:TAS2R44
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 By similarity. Activated by the sulfonyl amide sweeteners saccharin and acesulfame K.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in subsets of taste receptor cells of the tongue and exclusively in gustducin-positive cells.

Miscellaneous

Most taste cells may be activated by a limited number of bitter compounds; individual taste cells can discriminate among bitter stimuli.

Sequence similarities

Belongs to the G-protein coupled receptor T2R family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Taste receptor type 2 member 31
PRO_0000082309

Regions

Topological domain1 – 22Extracellular Potential
Transmembrane3 – 2321Helical; Name=1; Potential
Topological domain24 – 5532Cytoplasmic Potential
Transmembrane56 – 7621Helical; Name=2; Potential
Topological domain77 – 10024Extracellular Potential
Transmembrane101 – 12121Helical; Name=3; Potential
Topological domain122 – 1265Cytoplasmic Potential
Transmembrane127 – 14721Helical; Name=4; Potential
Topological domain148 – 18134Extracellular Potential
Transmembrane182 – 20221Helical; Name=5; Potential
Topological domain203 – 22927Cytoplasmic Potential
Transmembrane230 – 25021Helical; Name=6; Potential
Topological domain251 – 2599Extracellular Potential
Transmembrane260 – 28021Helical; Name=7; Potential
Topological domain281 – 30929Cytoplasmic Potential

Amino acid modifications

Glycosylation1611N-linked (GlcNAc...) Potential

Natural variations

Natural variant351R → W.
Corresponds to variant rs10845295 [ dbSNP | Ensembl ].
VAR_030684
Natural variant1621L → M. Ref.1 Ref.3
Corresponds to variant rs10743938 [ dbSNP | Ensembl ].
VAR_030685
Natural variant2171Q → E.
Corresponds to variant rs10845294 [ dbSNP | Ensembl ].
VAR_030686
Natural variant2271A → V. Ref.3
Corresponds to variant rs10845293 [ dbSNP | Ensembl ].
VAR_030687
Natural variant2401V → I. Ref.3
Corresponds to variant rs10772423 [ dbSNP | Ensembl ].
VAR_030688
Natural variant2761P → R.
Corresponds to variant rs12318612 [ dbSNP | Ensembl ].
VAR_062090

Sequences

Sequence LengthMass (Da)Tools
P59538 [UniParc].

Last modified June 28, 2011. Version 2.
Checksum: 56926C025E4C6358

FASTA30935,278
        10         20         30         40         50         60 
MTTFIPIIFS SVVVVLFVIG NFANGFIALV NSIERVKRQK ISFADQILTA LAVSRVGLLW 

        70         80         90        100        110        120 
VLLLNWYSTV FNPAFYSVEV RTTAYNVWAV TGHFSNWLAT SLSIFYLLKI ANFSNLIFLH 

       130        140        150        160        170        180 
LKRRVKSVIL VMLLGPLLFL ACQLFVINMK EIVRTKEYEG NLTWKIKLRS AVYLSDATVT 

       190        200        210        220        230        240 
TLGNLVPFTL TLLCFLLLIC SLCKHLKKMQ LHGKGSQDPS TKVHIKALQT VIFFLLLCAV 

       250        260        270        280        290        300 
YFLSIMISVW SFGSLENKPV FMFCKAIRFS YPSIHPFILI WGNKKLKQTF LSVLRQVRYW 


VKGEKPSSP 

« Hide

References

« Hide 'large scale' references
[1]"The human TAS2R16 receptor mediates bitter taste in response to beta-glucopyranosides."
Bufe B., Hofmann T., Krautwurst D., Raguse J.-D., Meyerhof W.
Nat. Genet. 32:397-401(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-162.
[2]"Identification and characterization of human taste receptor genes belonging to the TAS2R family."
Conte C., Ebeling M., Marcuz A., Nef P., Andres-Barquin P.J.
Cytogenet. Genome Res. 98:45-53(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Evolution of bitter taste receptors in humans and apes."
Fischer A., Gilad Y., Man O., Paeaebo S.
Mol. Biol. Evol. 22:432-436(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-162; VAL-227 AND ILE-240.
[4]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"Receptors for bitter and sweet taste."
Montmayeur J.-P., Matsunami H.
Curr. Opin. Neurobiol. 12:366-371(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[7]"Molecular mechanisms of bitter and sweet taste transduction."
Margolskee R.F.
J. Biol. Chem. 277:1-4(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[8]"Coding of sweet, bitter, and umami tastes: different receptor cells sharing similar signaling pathways."
Zhang Y., Hoon M.A., Chandrashekar J., Mueller K.L., Cook B., Wu D., Zuker C.S., Ryba N.J.
Cell 112:293-301(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[9]"Bitter taste receptors for saccharin and acesulfame K."
Kuhn C., Bufe B., Winnig M., Hofmann T., Frank O., Behrens M., Lewtschenko T., Slack J.P., Ward C.D., Meyerhof W.
J. Neurosci. 24:10260-10265(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVATION BY SACCHARIN AND ACESULFAME K.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF494228 Genomic DNA. Translation: AAM19319.1.
AY114090 Genomic DNA. Translation: AAM63540.1.
AY724942 Genomic DNA. Translation: AAU21144.1.
AC018630 Genomic DNA. No translation available.
BC117421 mRNA. Translation: AAI17422.1.
CCDSCCDS53747.1.
RefSeqNP_795366.2. NM_176885.2.
UniGeneHs.688197.

3D structure databases

ProteinModelPortalP59538.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL2034804.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP59538.

Polymorphism databases

DMDM338817946.

Proteomic databases

PRIDEP59538.

Protocols and materials databases

DNASU259290.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000390675; ENSP00000375093; ENSG00000256436.
ENST00000572376; ENSP00000459810; ENSG00000263097.
GeneID259290.
KEGGhsa:259290.
UCSCuc001qzo.1. human.

Organism-specific databases

CTD259290.
GeneCardsGC12M011183.
HGNCHGNC:19113. TAS2R31.
MIM612669. gene.
neXtProtNX_P59538.
GenAtlasSearch...

Phylogenomic databases

KOK08474.
OMACANGFIA.
OrthoDBEOG7P02JB.
PhylomeDBP59538.
TreeFamTF335891.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

CleanExHS_TAS2R44.
GenevestigatorP59538.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR017452. GPCR_Rhodpsn_7TM.
IPR007960. TAS2_rcpt.
[Graphical view]
PfamPF05296. TAS2R. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTAS2R31.
GenomeRNAi259290.
NextBio93119.
PROP59538.
SOURCESearch...

Entry information

Entry nameT2R31_HUMAN
AccessionPrimary (citable) accession number: P59538
Secondary accession number(s): P59547, Q17R84, Q645X5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: June 28, 2011
Last modified: July 9, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries