T2R13_PAPHA
ID T2R13_PAPHA Reviewed; 303 AA.
AC Q646F7;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Taste receptor type 2 member 13;
DE Short=T2R13;
GN Name=TAS2R13;
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; AY724825; AAU21062.1; -; 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..303
FT /note="Taste receptor type 2 member 13"
FT /id="PRO_0000082250"
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..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..85
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..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..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 303 AA; 34841 MW; CB8F3D805F070934 CRC64;
MESALLSILT LVIIAEFVIG NLSNGFXVLI NCIDWVSKRQ LSSVDKILTF LAISRIGLIW
ELLVSWFLGL HYLAIFVSGT GLRIMIFSWV VSNHFSLWLA TILSIFYLLK IASFSSPAFL
YLKWRVNQVI LMILLGTLVF LFLNLIQINI HIKDWLDRCE RNTIWNFSMS GLPTFSVPVK
FTMTMFSLAP FTVALISFLL LIFSLRKHLQ KMQLNYKGHR EPRTKAHINA LKIVISFLLL
YASFFLCILI SWISELYQNT LIHMFCQTIG VFYPSSHSFL LILGNPKLRQ ASLLVAAKVW
AKR
