TS1R2_GORGO
ID TS1R2_GORGO Reviewed; 839 AA.
AC A3QNZ9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Taste receptor type 1 member 2;
DE AltName: Full=Sweet taste receptor T1R2;
DE Flags: Precursor;
GN Name=TAS1R2;
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 Li X., Wong E.W., Li W., Lim R., Mascioli K.J., Maehashi K.,
RA Bachmanov A.A., Tordoff M.G., Beauchamp G.K., Reed D.R.;
RT "Sweet receptor gene variation and aspartame blindness in both primates and
RT non-primates.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Putative taste receptor. TAS1R2/TAS1R3 recognizes diverse
CC natural and synthetic sweeteners (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms heterodimers with TAS1R3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family. TAS1R
CC subfamily. {ECO:0000305}.
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DR EMBL; DQ386296; ABD37676.1; -; Genomic_DNA.
DR AlphaFoldDB; A3QNZ9; -.
DR SMR; A3QNZ9; -.
DR STRING; 9593.ENSGGOP00000025238; -.
DR PRIDE; A3QNZ9; -.
DR eggNOG; KOG1056; Eukaryota.
DR InParanoid; A3QNZ9; -.
DR Proteomes; UP000001519; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IBA:GO_Central.
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 Gene3D; 2.10.50.30; -; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR000337; GPCR_3.
DR InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR InterPro; IPR038550; GPCR_3_9-Cys_sf.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR000068; GPCR_3_Ca_sens_rcpt-rel.
DR InterPro; IPR017979; GPCR_3_CS.
DR InterPro; IPR028082; Peripla_BP_I.
DR PANTHER; PTHR24061; PTHR24061; 1.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF07562; NCD3G; 1.
DR PRINTS; PR00248; GPCRMGR.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 3: Inferred from homology;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Sensory transduction; Signal; Taste;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..839
FT /note="Taste receptor type 1 member 2"
FT /id="PRO_0000285551"
FT TOPO_DOM 20..566
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..587
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 588..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..623
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 624..635
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..681
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 682..702
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 703..727
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 728..748
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 749..760
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 761..781
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 782..784
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 785..805
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 806..839
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 839 AA; 95119 MW; 9802102F3F5165D8 CRC64;
MGTRATTICS LFFLLWVLAE PAENSDFYLP GDYLLGGLFS LHANMKGIVH LNFLQVPMCK
EYEVKVIGYN LMQAMRFAVE EINNDSSLLP GVLLGYEIVD VCYISNNVQP VLYFLAHEDN
LLPIQEDYSN YISRVVAVIG PDNSESVMTV ANFLSLFLLP QITYSAISDE LQDKVRFPAL
LRTTPSADHH VEAMVQLMLH FRWNWIIVLV SSDTYGRDNG QLLGERLARR DICIAFQETL
PTLQPNQNMT SEERQRLVTI VDKLQQSTAR VVVVFSPDLS LYDFFNEVLR QNFTGAVWIA
SESWAIDPVL HNLTELRHLG TFLGITIQSV PIPGFSEFRE WSPQAGPPPL SRTSQSYTCN
QECDNCLNAT LSFNTILRLS GERVVYSVYS AVYAVAHALH SLLGCDNSTC TKRVVYPWQL
LEEIWKVNFT LLDHQIFFDP QGDVALHLEI VQWQWDRSQN PFQSVASYYP LQRQLKHIQD
ISWHTINNTI PVSMCSKRCQ SGQKKKPVGI HVCCFECIDC LPGTFLNHTE DEYECQACPN
NEWSYQSETS CFKRQLVFLE WHEAPTIAVA LLAALGFLST LAILVIFWRH FQTPIVRSAG
GPMCFLMLTL LLVAYMVVPV YVGPPKVSTC LCRQALFPLC FTICISCIAV RSFQIVCAFK
MASRFPRAYS YWVRYQGPYV SMAFITVLKM VIVVIGMLAT GLSPTTRTDP DDPKITIVSC
NPNYRNSLLF NTSLDLLLSV VGFSFAYMGK ELPTNYNEAK FITLSMTFYF TSSVSLCTFM
SAYSGVLVTI VDLLVTVLNL LAISLGYFGP KCYMILFYPE RNTPAYFNSM IQGYTMRRD
