TA2R8_PAPHA
ID TA2R8_PAPHA Reviewed; 309 AA.
AC Q646G4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Taste receptor type 2 member 8;
DE Short=T2R8;
GN Name=TAS2R8;
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; AY724817; AAU21055.1; -; 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..309
FT /note="Taste receptor type 2 member 8"
FT /id="PRO_0000082230"
FT TOPO_DOM 1..7
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..82
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 309 AA; 35558 MW; C648624F2025C7FA CRC64;
MFSPADNIFI ILITGEFIIG ILGNGYIGLV NWIDWIKKKK ISTIDCILTN LVISRICLIS
VMVVNGIVIV LYPDVYTKTK LQIVICTFWT FANYLNMWFT ACLNVFYSLK VANSSHPLFL
WLKRKIDMVV RWILLGCFAI SLLVSLIIAT VLSHDYRFHA IAKHKRNVTE MFHVSKMPYF
EPLTLFNLLA IVPFIVSLMS FFLLVRSLWR HTKQIKLYAT GGRDPSTEAH VRAIKTMTLL
IFFFFLYYIT SLLVXFSYLI TNYKLAMAFG EIVAILYPSG HSLILIILNN KLRQASVRML
TCRKIACVT