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Database: UniProt
Entry: T2R38_GORGO
LinkDB: T2R38_GORGO
Original site: T2R38_GORGO 
ID   T2R38_GORGO             Reviewed;         333 AA.
AC   Q697L4; Q645Y6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-MAY-2023, entry version 84.
DE   RecName: Full=Taste receptor type 2 member 38;
DE            Short=T2R38;
GN   Name=TAS2R38;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Davidson A.C., Pakstis A.J., Speed W.C., Odunsi A., Okonafua F.,
RA   Kajuna S.L.J., Kungulilo S.V., Friedlaender J., Lu R.-B., Grigorenko E.L.,
RA   Zhukova O.V., Schultz L.O., Bonne-Tamir B., Duffy V., Bartoshuk L.,
RA   Kidd K.K., Kidd J.R.;
RT   "A global survey of haplotype frequencies for the TAS2R38 (PTC) gene.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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; AY566403; AAS67623.1; -; Genomic_DNA.
DR   EMBL; AY724927; AAU21133.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q697L4; -.
DR   SMR; Q697L4; -.
DR   STRING; 9593.ENSGGOP00000000265; -.
DR   GlyCosmos; Q697L4; 1 site, No reported glycans.
DR   eggNOG; ENOG502T15G; Eukaryota.
DR   HOGENOM; CLU_072337_3_0_1; -.
DR   InParanoid; Q697L4; -.
DR   Proteomes; UP000001519; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0033038; F:bitter taste receptor activity; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IBA:GO_Central.
DR   CDD; cd15025; 7tm_TAS2R38; 1.
DR   InterPro; IPR007960; TAS2R.
DR   InterPro; IPR030050; TAS2R38.
DR   PANTHER; PTHR11394; TASTE RECEPTOR TYPE 2; 1.
DR   PANTHER; PTHR11394:SF52; TASTE RECEPTOR TYPE 2 MEMBER 38; 1.
DR   Pfam; PF05296; TAS2R; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
PE   3: Inferred from homology;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Sensory transduction; Taste; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..333
FT                   /note="Taste receptor type 2 member 38"
FT                   /id="PRO_0000082272"
FT   TOPO_DOM        1..17
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        18..38
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        39..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..94
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..142
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        164..190
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..211
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        212..251
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..276
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        298..333
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        147
FT                   /note="I -> T (in Ref. 2; AAU21133)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   333 AA;  37871 MW;  376B89003067CAC2 CRC64;
     MLTLTRIRTV SYEVRSTFLF ISVLEFAVGF LTNAFVFLVN FWDVVKRQPL SNSDCVLLCL
     SISRLFLHGL LFLSAIQLTH FQKLSEPLNH SYQAIIMLWM IANQANLWLA ACLSLLYCSK
     LIRFSHTFLI CLASWVSRKI SQMLLGIILC SCICTVLCVW CFFSRPHFTV TTVLFMNNNT
     RLNWQIKDLN LFYSFLFCYL WSVPPFLLFL VSSGMLTVSL GRHMRTMKVY IRDSRDPSLE
     AHIKALKSLV SFFCFFVISS CAAFISVPLL ILWRDKIGVM VCVGIMAACP SGHAAVLISG
     NAKLRRAVTT ILLWAQSSLK VRADHKADSR TPC
//
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