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Protein

Taste receptor type 2 member 42

Gene

TAS2R42

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Sensory transduction, Taste

Enzyme and pathway databases

ReactomeiREACT_18319. Class C/3 (Metabotropic glutamate/pheromone receptors).
REACT_19231. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Taste receptor type 2 member 42
Short name:
T2R42
Alternative name(s):
Taste receptor type 2 member 55
Short name:
T2R55
Gene namesi
Name:TAS2R42
Synonyms:TAS2R55
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:18888. TAS2R42.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77ExtracellularSequence Analysis
Transmembranei8 – 2821Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini29 – 5022CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei51 – 7121Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini72 – 10130ExtracellularSequence AnalysisAdd
BLAST
Transmembranei102 – 12221Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini123 – 1275CytoplasmicSequence Analysis
Transmembranei128 – 14821Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini149 – 18739ExtracellularSequence AnalysisAdd
BLAST
Transmembranei188 – 20821Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini209 – 23830CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei239 – 25921Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini260 – 2656ExtracellularSequence Analysis
Transmembranei266 – 28621Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini287 – 31428CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38741.

Polymorphism and mutation databases

BioMutaiTAS2R42.
DMDMi55976719.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 314314Taste receptor type 2 member 42PRO_0000082344Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ7RTR8.
PRIDEiQ7RTR8.

Expressioni

Gene expression databases

CleanExiHS_TAS2R42.
GenevestigatoriQ7RTR8.

Organism-specific databases

HPAiHPA036149.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000334050.

Structurei

3D structure databases

ProteinModelPortaliQ7RTR8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG43990.
HOGENOMiHOG000234595.
HOVERGENiHBG060698.
InParanoidiQ7RTR8.
OMAiHRRAMKM.
OrthoDBiEOG72C512.
PhylomeDBiQ7RTR8.
TreeFamiTF335891.

Family and domain databases

InterProiIPR017452. GPCR_Rhodpsn_7TM.
IPR007960. T2R.
[Graphical view]
PANTHERiPTHR11394. PTHR11394. 1 hit.
PfamiPF05296. TAS2R. 1 hit.
[Graphical view]
PROSITEiPS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7RTR8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATELDKIFL ILAIAEFIIS MLGNVFIGLV NCSEGIKNQK VFSADFILTC
60 70 80 90 100
LAISTIGQLL VILFDSFLVG LASHLYTTYR LGKTVIMLWH MTNHLTTWLA
110 120 130 140 150
TCLSIFYFFK IAHFPHSLFL WLRWRMNGMI VMLLILSLFL LIFDSLVLEI
160 170 180 190 200
FIDISLNIID KSNLTLYLDE SKTLYDKLSI LKTLLSLTSF IPFSLFLTSL
210 220 230 240 250
LFLFLSLVRH TRNLKLSSLG SRDSSTEAHR RAMKMVMSFL FLFIVHFFSL
260 270 280 290 300
QVANGIFFML WNNKYIKFVM LALNAFPSCH SFILILGNSK LRQTAVRLLW
310
HLRNYTKTPN ALPL
Length:314
Mass (Da):36,195
Last modified:December 15, 2003 - v1
Checksum:i0A49C39889F8CFA4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti175 – 1751Y → F.1 Publication
Corresponds to variant rs35969491 [ dbSNP | Ensembl ].
VAR_062086
Natural varianti196 – 1961F → S.1 Publication
Corresponds to variant rs5020531 [ dbSNP | Ensembl ].
VAR_053352
Natural varianti255 – 2551G → W.1 Publication
Corresponds to variant rs1669413 [ dbSNP | Ensembl ].
VAR_062087
Natural varianti265 – 2651Y → C.
Corresponds to variant rs1451772 [ dbSNP | Ensembl ].
VAR_053353
Natural varianti292 – 2921R → Q.
Corresponds to variant rs1669412 [ dbSNP | Ensembl ].
VAR_062088
Natural varianti311 – 3111A → P.1 Publication
Corresponds to variant rs1650017 [ dbSNP | Ensembl ].
VAR_062089

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY724953 Genomic DNA. Translation: AAU21149.1.
AC010176 Genomic DNA. No translation available.
BC131742 mRNA. Translation: AAI31743.1.
BK001099 Genomic DNA. Translation: DAA01206.1.
CCDSiCCDS31747.1.
UniGeneiHs.553716.

Genome annotation databases

EnsembliENST00000334266; ENSP00000334050; ENSG00000186136.
UCSCiuc001qzr.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY724953 Genomic DNA. Translation: AAU21149.1.
AC010176 Genomic DNA. No translation available.
BC131742 mRNA. Translation: AAI31743.1.
BK001099 Genomic DNA. Translation: DAA01206.1.
CCDSiCCDS31747.1.
UniGeneiHs.553716.

3D structure databases

ProteinModelPortaliQ7RTR8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000334050.

Protein family/group databases

GPCRDBiSearch...

Polymorphism and mutation databases

BioMutaiTAS2R42.
DMDMi55976719.

Proteomic databases

PaxDbiQ7RTR8.
PRIDEiQ7RTR8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334266; ENSP00000334050; ENSG00000186136.
UCSCiuc001qzr.1. human.

Organism-specific databases

GeneCardsiGC12M011338.
HGNCiHGNC:18888. TAS2R42.
HPAiHPA036149.
MIMi613966. gene.
neXtProtiNX_Q7RTR8.
PharmGKBiPA38741.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG43990.
HOGENOMiHOG000234595.
HOVERGENiHBG060698.
InParanoidiQ7RTR8.
OMAiHRRAMKM.
OrthoDBiEOG72C512.
PhylomeDBiQ7RTR8.
TreeFamiTF335891.

Enzyme and pathway databases

ReactomeiREACT_18319. Class C/3 (Metabotropic glutamate/pheromone receptors).
REACT_19231. G alpha (i) signalling events.

Miscellaneous databases

GenomeRNAii353164.
NextBioi99726.
PROiQ7RTR8.
SOURCEiSearch...

Gene expression databases

CleanExiHS_TAS2R42.
GenevestigatoriQ7RTR8.

Family and domain databases

InterProiIPR017452. GPCR_Rhodpsn_7TM.
IPR007960. T2R.
[Graphical view]
PANTHERiPTHR11394. PTHR11394. 1 hit.
PfamiPF05296. TAS2R. 1 hit.
[Graphical view]
PROSITEiPS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "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.
    , 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], VARIANTS PHE-175; SER-196; TRP-255 AND PRO-311.
  3. "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].
  4. "Adaptive diversification of bitter taste receptor genes in mammalian evolution."
    Shi P., Zhang J., Yang H., Zhang Y.-P.
    Mol. Biol. Evol. 20:805-814(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiT2R42_HUMAN
AccessioniPrimary (citable) accession number: Q7RTR8
Secondary accession number(s): A2RRP4, Q645X0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: December 15, 2003
Last modified: April 29, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.