ID   OAR2_LYMST              Reviewed;         578 AA.
AC   O01670;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Octopamine receptor 2;
DE            Short=OA2;
OS   Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Lymnaeidae; Lymnaea.
OX   NCBI_TaxID=6523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   TISSUE=CNS;
RX   PubMed=9045634; DOI=10.1074/jbc.272.10.6201;
RA   Gerhardt C.C., Lodder H.C., Vincent M., Bakker R.A., Planta R.J.,
RA   Vreugdenhil E., Kits K.S., van Heerikhuizen H.;
RT   "Cloning and expression of a complementary DNA encoding a molluscan
RT   octopamine receptor that couples to chloride channels in HEK293 cells.";
RL   J. Biol. Chem. 272:6201-6207(1997).
CC   -!- FUNCTION: Receptor for octopamine. Octopamine (OA) is a
CC       neurotransmitter, neurohormone, and neuromodulator in invertebrates.
CC       This receptor induces a long lasting opening of voltage- independent
CC       chloride channels, a process which seems to involve protein
CC       phosphorylation but does not require either cAPK or PKC. The rank order
CC       of potency for agonists is p-synephrine > p-octopamine > xylometazoline
CC       > B-HT920 > norepinephrine = clonidine > epinephrine > p-tyramine >
CC       phenylephrine = oxymetazoline = mehoxamine = dopamine > serotonin >
CC       histamine. For antagonists, the rank order is rauwolscine = mianserin >
CC       phentolamine > chlorpromazine > spiperone > yohimbine > propanolol >
CC       alprenolol > prazosine > pindolol.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; U62770; AAB53033.1; -; mRNA.
DR   AlphaFoldDB; O01670; -.
DR   SMR; O01670; -.
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   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 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..578
FT                   /note="Octopamine receptor 2"
FT                   /id="PRO_0000069957"
FT   TOPO_DOM        1..84
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..107
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..117
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..139
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        140..156
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        178..197
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..220
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        221..251
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..495
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        496..517
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        518..531
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        532..553
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        554..578
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        13
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        154..239
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   578 AA;  65131 MW;  05AF2E2447B3B09C CRC64;
     MMSFPIALFA DVNQSFRANL VVSSYHHAIT FPTVRGANFS TFFPRNFSVS ADVWLCGANF
     SQEWQLMQPV CSTKYDSITI FITVAVVLTL ITLWTILGNF FVLMALYRYG TLRTMSNCLI
     GNLAISDLLL AVTVLPISTV HDLLGYWVFG EFTCTLWLCM DVLYCTASIW GLCTVAFDRY
     LATVYPVWYH DQRSVRKAVG CIVFVWIFSI VISFAPFIGW QHMIPSFFSF NASIQRYQCI
     LFTSSSYVLY SSMGSFVIPA ILMAFMYVRI FVVLHNQSRG VKFKSGLKIS SSKYNGCPVI
     NEPSREGING LGRDVTNTTL LSDAVGSSAD LTSNGKDDPR VLATAPIELT EDVPPLNGHH
     HRTVHETPYV SGLHTKRSNS FALPTELEKK CKPLTNNILH MMDFDRRNSH NAVIQRSASE
     MVNLDVSKHE LLISNVCHRS KSATALTSET GDPLGSLAGP RRSLQCNVGG LVRNKHMTLS
     MKRRFELREQ RATKRMLLIM ACFCVCWMPF LFMYILRSVC DTCHMNQHFV AAIIWLGYVN
     SSLNPVLYTL FNDDFKVAFK RLIGARSPSA YRSPGPRR