T2R39_PAPHA
ID T2R39_PAPHA Reviewed; 338 AA.
AC Q646F0;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Taste receptor type 2 member 39;
DE Short=T2R39;
GN Name=TAS2R39;
OS Papio hamadryas (Hamadryas baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9557;
RN [1]
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).
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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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; AY724834; AAU21069.1; -; Genomic_DNA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0050909; P:sensory perception of taste; IEA:UniProtKB-KW.
DR InterPro; IPR007960; TAS2R.
DR Pfam; PF05296; TAS2R; 1.
PE 3: Inferred from homology;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Sensory transduction; Taste; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..338
FT /note="Taste receptor type 2 member 39"
FT /id="PRO_0000082285"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 338 AA; 38570 MW; DB211486D21017D8 CRC64;
MLGRCFPPNT KEKQQLRMIK LCDPAESELS PFLITLTLAV LLAEYLTGII ANGFITAIHA
AECVQNKSVS TSGRILVFLS VSRIALQSLM MLEITISSTS LSFYSEDTVY YAFKISFIFL
NFCSLWFAAW LSFFYFVKIA NFSYPLFLKL RWRISGLIPW LLWLSVFISF SHSMFCINIC
TGYCDNSFPI HSSNSTEKTY FSEISVVSLA FFFNLGIVIP LIMFILAAIL LILSLKRHTL
YMXSNATGSK DPSMEAHIGA IKATSYFLIL YIFNAVALFI YLSNMFDINS LWNTLCQIIM
AAYPASHSIL LIKDNPGLRR AWKQLQHRLH LYPKEWTL