ID   T2R16_PANPA             Reviewed;         291 AA.
AC   Q646D1; Q5Y505;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Taste receptor type 2 member 16;
DE            Short=T2R16;
GN   Name=TAS2R16;
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15466715; DOI=10.1073/pnas.0404894101;
RA   Parry C.M., Erkner A., le Coutre J.;
RT   "Divergence of T2R chemosensory receptor families in humans, bonobos, and
RT   chimpanzees.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14830-14834(2004).
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   -!- SUBUNIT: Interacts with RTP3 and RTP4. {ECO:0000250|UniProtKB:Q9NYV7}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NYV7};
CC       Multi-pass membrane protein {ECO:0000255}.
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; AY724862; AAU21088.1; -; Genomic_DNA.
DR   EMBL; AY677142; AAV28570.1; -; Genomic_DNA.
DR   RefSeq; XP_003808674.1; XM_003808626.2.
DR   AlphaFoldDB; Q646D1; -.
DR   SMR; Q646D1; -.
DR   STRING; 9597.XP_003808674.1; -.
DR   Ensembl; ENSPPAT00000000668; ENSPPAP00000000163; ENSPPAG00000000642.
DR   GeneID; 100980693; -.
DR   KEGG; pps:100980693; -.
DR   CTD; 50833; -.
DR   eggNOG; ENOG502S2SI; Eukaryota.
DR   GeneTree; ENSGT00960000186648; -.
DR   OMA; CLQWTSM; -.
DR   OrthoDB; 1282504at2759; -.
DR   Proteomes; UP000240080; Chromosome 7.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR   GO; GO:0033038; F:bitter taste receptor activity; IEA:Ensembl.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR007960; TAS2R.
DR   Pfam; PF05296; TAS2R; 1.
PE   3: Inferred from homology;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Reference proteome; Sensory transduction; Taste; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..291
FT                   /note="Taste receptor type 2 member 16"
FT                   /id="PRO_0000082263"
FT   TOPO_DOM        1
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2..22
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        23..41
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        63..84
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..125
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..182
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..228
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        250..257
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..278
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        279..291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   291 AA;  33919 MW;  5C9F1C50DBC8228D CRC64;
     MIPIQLTVFF MIIYVLESLT IIVQSSLIVA VLGREWLQVR RLMPVDMILI SLGISRFCLQ
     WASMLNNFCS YFNLNYVLCN LTITWEFFNI LTFWLNSLLT VFYCIKASSF THHIFLWLRW
     RILRLFPWIL LGSLMITCVT IIPSAIGNYI QIQLLTMEHL PRNSTVTDKL EKFHQYQFQA
     HTVALVIPFI LFLASTILLM ASLTKQIQHH STGHCNPSMK AHFTALRSLA VLFIVFTSYF
     LTILITIIGT LFDKRCWLWV WEAFVYAFIL MHSTSLMLSS PTLKRILKGK C