TS1R2_SAISC
ID TS1R2_SAISC Reviewed; 834 AA.
AC A3QP08;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Taste receptor type 1 member 2;
DE AltName: Full=Sweet taste receptor T1R2;
DE Flags: Precursor;
GN Name=TAS1R2;
OS Saimiri sciureus (Common squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=9521;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ386301; ABD37685.1; -; Genomic_DNA.
DR AlphaFoldDB; A3QP08; -.
DR SMR; A3QP08; -.
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: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; PR00592; CASENSINGR.
DR PRINTS; PR00248; GPCRMGR.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 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; Sensory transduction; Signal; Taste; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..834
FT /note="Taste receptor type 1 member 2"
FT /id="PRO_0000285556"
FT TOPO_DOM 20..561
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..597
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 598..618
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 619..630
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 631..651
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 652..676
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 677..697
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 698..722
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 723..743
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 744..755
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 756..776
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 777..779
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 780..800
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 801..834
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
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 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 834 AA; 94378 MW; 2BD57613FB423603 CRC64;
MEPRVRTVCF LFFLLRVLAE PAKNSDFYLP GDYLLGGLFT LHANMKGTVH LNFLQVPMCK
EYEVKLSGYN LMQAMRFAVE EINNDSSLLP DVRLGYEMVD VCYVSNNVQP VLYFLAQEDN
LLPIQEDYSN YVPRVVAVIG PENSESVTTV ANFLSLFLLP QITYSAISDQ LRDKQRFPAL
LRTTPSAKHH IEAMVQLMLH FRWNWISVLV SSDTYGRDNG QLLGDRLAGG DICIAFQETL
PTLQPNQDMM PEDRQRLVSI VEKLQQSTAR VVVVFSPDLT LYDFFREVLR QNFTGAVWIA
SESWAIDPVL HNLTGLHRTG TFLGITLQNV PIPGFNEFRV RGPQAGPTHQ RSTCNQECDT
CLNSTLSFNT ILRLSGERVV YSVYSAVYAV AHALHSLLGC DHSACTKRGV YPWQLLEEIW
KVNFSLLDHQ IFFDPQGDVA LHLEIVQWQW DLSQNPFQSV ASYQPLQGHL KDIQDISWHT
VNNTIPVSMC SKRCQSGQKK KPVGIHTCCF ECIDCPPGTF LNQTANEYDC QACPSNEWSH
QSETSCFKRR LSFLEWHEAA TIAVALLAAL GFLSTLAILV IFWRHFETPM VRSAGGPMCF
LMLTLLLVAY MVVPVYVGLP KVSTCLCRQA LFPVCFTICI SCIAVRSFQI VCVFKMASRF
PRAYSYWVRY QGSYVSVAFI TALKMVTVVI SLLATGLNPT TRTDTDDPKI MIISCNPNYR
NSLLFNTSLD LLLSVAGFSF AYMGKELPTN YNEAKFITFS MTFYFTSSVS LCTFMSVYDG
VLVTIVDLLV TVFNLLAISL GYFGPKCYMI LFYPERNTPA YFNSMIQGYT MRRD
