OAR1_LOCMI
ID OAR1_LOCMI Reviewed; 484 AA.
AC Q25321;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Tyramine receptor 1;
DE AltName: Full=Tyr-Loc1;
GN Name=GCR1;
OS Locusta migratoria (Migratory locust).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC Acridoidea; Acrididae; Oedipodinae; Locusta.
OX NCBI_TaxID=7004;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Neuron;
RX PubMed=7760020; DOI=10.1046/j.1471-4159.1995.64062387.x;
RA Vanden Broeck J.J.M., Vulsteke V., Huybrechts R., de Loof A.;
RT "Characterization of a cloned locust tyramine receptor cDNA by functional
RT expression in permanently transformed Drosophila S2 cells.";
RL J. Neurochem. 64:2387-2395(1995).
CC -!- FUNCTION: G-protein coupled receptor for tyramine, a known
CC neurotransmitter and neuromodulator and direct precursor of octopamine.
CC The rank order of potency for agonists of this receptor is tyramine >
CC naphazoline > tolazoline > DL-octopamine > dopamine > epinephrine > 5-
CC hydroxytryptamine. For antagonists, the rank order is yohimbine >
CC chlorpromazine > mianserin > phentolamine > metoclopramide.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Present mainly in the central nervous system,
CC especially in the supra- and subesophageal, thoracic and abdominal
CC ganglia. Not found in the distal part of optic lobes.
CC -!- DEVELOPMENTAL STAGE: Expressed in the nervous system by the first
CC larval stage.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X69520; CAA49268.1; -; mRNA.
DR PIR; S58868; S58868.
DR AlphaFoldDB; Q25321; -.
DR SMR; Q25321; -.
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:0004989; F:octopamine receptor activity; IEA:InterPro.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002002; Octopmn_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00664; OCTOPAMINER.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..484
FT /note="Tyramine receptor 1"
FT /id="PRO_0000069954"
FT TOPO_DOM 1..54
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..77
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..109
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..190
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..237
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..433
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..448
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..470
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 253..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 124..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 484 AA; 53531 MW; 4484FBC85A810619 CRC64;
MVRVELQAAS LMNGSSAAEE PQDALVGGDA CGGRRPPSVL GVRLAVPEWE VAVTAVSLSL
IILITIVGNV LVVLSVFTYK PLRIVQNFFI VSLAVADLTV AVLVMPFNVA YSLIQRWVFG
IVVCKMWLTC DVLCCTASIL NLCAIALDRY WAITDPINYA QKRTLRRVLA MIAGVWLLSG
VISSPPLIGW NDWPMEFNDT TPCQLTEEQG YVIYSSLGSF FIPLFIMTIV YVEIFIATKR
RLRERAKASK LNSAMKQQMA AQAVPSSVPS HDQESVSSET NHNELPPPPA PPSKEKRRKT
KKKSKKKEQA AEEGRFLAPA MVAEDSVTDN SVSVGPVARN HLAEDGYTCT TTTTTTTTTT
AVTDSPRSRT ASQKGSTAPP TPVQPKSIPV YQFIEEKQRI SLSKERRAAR TLGIIMGVFV
VCWLPFFLMY VIVPFCNPSC KPSPKLVNFI TWLGYINSAL NPIIYTIFNL DFRRAFKKLL
HFKT