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T2R40_CHICK
ID   T2R40_CHICK             Reviewed;         311 AA.
AC   Q2AB83; A0A0X9UE61;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Taste receptor type 2 member 40;
DE            Short=T2R40;
DE   AltName: Full=Taste receptor type 2 member 1;
DE            Short=T2R1;
GN   Name=TAS2R40; Synonyms=TAS2R1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16484289; DOI=10.1093/molbev/msj106;
RA   Go Y.;
RT   "Lineage-specific expansions and contractions of the bitter taste receptor
RT   gene repertoire in vertebrates.";
RL   Mol. Biol. Evol. 23:964-972(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl;
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA   Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA   Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA   Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA   McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA   Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA   Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA   Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA   Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA   Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA   Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA   Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA   Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA   Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA   Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA   Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA   Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA   Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA   Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA   Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA   Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA   Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA   Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA   Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA   Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA   Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA   Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA   Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide unique
RT   perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-297.
RA   Su Y., Zhu Q., Wu N., Chen B., Li D.;
RT   "The genetic polymorphisms of chicken bitter taste receptor genes in
RT   Sichuan domestic and Tibetan populations.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
RX   PubMed=25796330; DOI=10.1016/j.bbrc.2015.03.056;
RA   Hirose N., Kawabata Y., Kawabata F., Nishimura S., Tabata S.;
RT   "Bitter taste receptor T2R1 activities were compatible with behavioral
RT   sensitivity to bitterness in chickens.";
RL   Biochem. Biophys. Res. Commun. 460:464-468(2015).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=26049797; DOI=10.3382/ps/pev152;
RA   Cheled-Shoval S.L., Druyan S., Uni Z.;
RT   "Bitter, sweet and umami taste receptors and downstream signaling
RT   effectors: Expression in embryonic and growing chicken gastrointestinal
RT   tract.";
RL   Poult. Sci. 94:1928-1941(2015).
RN   [6]
RP   FUNCTION, AND MUTAGENESIS OF LYS-86; PHE-89; ASN-93; PHE-181; LEU-185;
RP   TYR-244; ASN-247 AND LEU-251.
RX   PubMed=28811548; DOI=10.1038/s41598-017-08344-9;
RA   Di Pizio A., Kruetzfeldt L.M., Cheled-Shoval S., Meyerhof W., Behrens M.,
RA   Niv M.Y.;
RT   "Ligand binding modes from low resolution GPCR models and mutagenesis:
RT   chicken bitter taste receptor as a test-case.";
RL   Sci. Rep. 7:8223-8223(2017).
CC   -!- FUNCTION: Bitter taste receptor (PubMed:25796330). Binds quinine,
CC       dextromethorphan, diphenhydramine, diphenidol, chlorpheniramine,
CC       diphenidol, chloramphenicol, chloroquine and coumarin, this latter
CC       being a weak agonist, as well as epiquinidine, ethylhydrocupreine and
CC       quinidine (PubMed:28811548). {ECO:0000269|PubMed:25796330,
CC       ECO:0000269|PubMed:28811548}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255|RuleBase:RU004424}.
CC   -!- TISSUE SPECIFICITY: Expressed in the oral cavity, as well as in the
CC       gastrointestinal tract, including in the upper palate, tongue,
CC       proventriculus, ventriculus, duodenum, jejunum, ileum, cecum and colon.
CC       {ECO:0000269|PubMed:25796330, ECO:0000269|PubMed:26049797}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor T2R family.
CC       {ECO:0000255|RuleBase:RU004423}.
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DR   EMBL; AB249766; BAE80384.1; -; Genomic_DNA.
DR   EMBL; AADN04000390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KT377136; AMA21693.1; -; Genomic_DNA.
DR   EMBL; KT377152; AMA21709.1; -; Genomic_DNA.
DR   EMBL; KT377138; AMA21695.1; -; Genomic_DNA.
DR   EMBL; KT377139; AMA21696.1; -; Genomic_DNA.
DR   EMBL; KT377140; AMA21697.1; -; Genomic_DNA.
DR   EMBL; KT377145; AMA21702.1; -; Genomic_DNA.
DR   EMBL; KT377147; AMA21704.1; -; Genomic_DNA.
DR   EMBL; KT377149; AMA21706.1; -; Genomic_DNA.
DR   EMBL; KT377151; AMA21708.1; -; Genomic_DNA.
DR   RefSeq; XP_004938201.1; XM_004938144.2.
DR   AlphaFoldDB; Q2AB83; -.
DR   SMR; Q2AB83; -.
DR   Ensembl; ENSGALT00000081605; ENSGALP00000051324; ENSGALG00000030506.
DR   GeneID; 101749182; -.
DR   KEGG; gga:101749182; -.
DR   CTD; 259286; -.
DR   VEuPathDB; HostDB:geneid_101749182; -.
DR   GeneTree; ENSGT00960000186638; -.
DR   OMA; FMFLNHC; -.
DR   OrthoDB; 1010573at2759; -.
DR   PhylomeDB; Q2AB83; -.
DR   Reactome; R-GGA-418594; G alpha (i) signalling events.
DR   Reactome; R-GGA-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR   Reactome; R-GGA-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR   PRO; PR:Q2AB83; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033038; F:bitter taste receptor activity; IDA:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB.
DR   GO; GO:1902656; P:calcium ion import into cytosol; IMP:AgBase.
DR   GO; GO:0072747; P:cellular response to chloramphenicol; IDA:AgBase.
DR   GO; GO:1902350; P:cellular response to chloroquine; IDA:AgBase.
DR   GO; GO:1904561; P:cellular response to diphenidol; IDA:AgBase.
DR   GO; GO:0071316; P:cellular response to nicotine; IDA:AgBase.
DR   GO; GO:0097237; P:cellular response to toxic substance; IDA:AgBase.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:AgBase.
DR   GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IBA:GO_Central.
DR   GO; GO:1904558; P:response to dextromethorphan; IDA:AgBase.
DR   GO; GO:1904560; P:response to diphenidol; IDA:AgBase.
DR   GO; GO:0080184; P:response to phenylpropanoid; IDA:AgBase.
DR   InterPro; IPR007960; TAS2R.
DR   Pfam; PF05296; TAS2R; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; G-protein coupled receptor; Membrane; Receptor;
KW   Reference proteome; Sensory transduction; Taste; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..311
FT                   /note="Taste receptor type 2 member 40"
FT                   /id="PRO_5010136905"
FT   TOPO_DOM        1..9
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..55
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..87
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..128
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        150..178
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..266
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        288..311
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         86
FT                   /note="K->A: No effect on quinine-, nor diphenhydramine-
FT                   binding, small decrease in diphenidol- and
FT                   chlorpheniramine-binding, strong decrease in
FT                   chloramphenicol- and chloroquine-binding, increase in
FT                   coumarin-binding."
FT                   /evidence="ECO:0000269|PubMed:28811548"
FT   MUTAGEN         89
FT                   /note="F->A: Strong increase in quinine-binding, loss of
FT                   diphenhydramine- and coumarin-binding, small decrease in
FT                   diphenidol-binding, strong decrease in chlorpheniramine-,
FT                   chloramphenicol- and chloroquine-binding."
FT                   /evidence="ECO:0000269|PubMed:28811548"
FT   MUTAGEN         93
FT                   /note="N->A: Loss of quinine-, diphenhydramine- and
FT                   coumarin-binding, strong decrease in diphenidol-,
FT                   chlorpheniramine-, chloramphenicol- and chloroquine-
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:28811548"
FT   MUTAGEN         181
FT                   /note="F->A: Loss of quinine-, diphenhydramine- and
FT                   coumarin-binding, strong decrease in diphenidol-,
FT                   chloramphenicol- and chloroquine-binding, decrease in
FT                   chlorpheniramine-binding."
FT                   /evidence="ECO:0000269|PubMed:28811548"
FT   MUTAGEN         185
FT                   /note="L->A: Strong decrease in quinine- and
FT                   diphenhydramine-binding, no effect on diphenidol-, nor
FT                   chlorpheniramine-binding, small decrease in
FT                   chloramphenicol- and chloroquine-binding, loss of coumarin-
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:28811548"
FT   MUTAGEN         244
FT                   /note="Y->A: Loss of quinine- and diphenhydramine-binding,
FT                   strong decrease in diphenidol-binding, small decrease in
FT                   chloramphenicol-binding, increase in coumarin-binding, no
FT                   effect on chlorpheniramine-, nor chloramphenicol-binding."
FT                   /evidence="ECO:0000269|PubMed:28811548"
FT   MUTAGEN         247
FT                   /note="N->A: Loss of quinine-, diphenhydramine- and
FT                   coumarin-binding, strong decrease in diphenidol-binding,
FT                   small decrease in chlorpheniramine- and chloramphenicol-
FT                   binding, no effect on chloramphenicol-binding."
FT                   /evidence="ECO:0000269|PubMed:28811548"
FT   MUTAGEN         251
FT                   /note="L->A: Strong decrease in quinine-binding, loss of
FT                   diphenhydramine-binding, small decrease in diphenidol- and
FT                   chloramphenicol-binding, no effect on chlorpheniramine-,
FT                   chloramphenicol-, nor coumarin-binding."
FT                   /evidence="ECO:0000269|PubMed:28811548"
FT   CONFLICT        120
FT                   /note="S -> T (in Ref. 3; AMA21693/AMA21695/AMA21696/
FT                   AMA21697/AMA21702/AMA21704/AMA21706/AMA21708/AMA21709)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   311 AA;  35281 MW;  FBFFA294F498C093 CRC64;
     MSSLFSSFCL VIAIFESVVG LLGNGTIVAV SSTSCIRSKI LSSYDVIVIF LSLSRFFLQL
     WMILDFLLIF FCQPSYYEEN LFVTFKTVFI FLNSYSFWFA AWLSVFYCVK VASFTQSFLS
     WLKQRIASLI PWMLITSSLF SFATSLPFFW DSYNAHSNFT TPLTMTNSSK RITTRKTNLI
     FLILLCNVGI ALPSIMLVFS SILLIRSLWR HTRQMQNNAT GFRDPSLEAL IGAIKTVFSF
     LLLYITNFIA LILILSDTFV PLSTEEAICV VVVAACPAGQ SMVLIWSNPR FRELLSSILH
     YVNSCVRARC S
 
 
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