OAR_DROME
ID OAR_DROME Reviewed; 601 AA.
AC P22270; Q1RKQ4; Q95YF4; Q9VNW3;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Tyramine/octopamine receptor;
DE AltName: Full=Tyr/Oct-Dro;
DE Flags: Precursor;
GN Name=Oct-TyrR; Synonyms=OcR, OctyR99AB, TYR, TyrR; ORFNames=CG7485;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R;
RX PubMed=2156539; DOI=10.1016/0896-6273(90)90047-j;
RA Arakawa S., Gocayne J.D., McCombie W.R., Urquhart D.A., Hall L.M.,
RA Fraser C.M., Venter J.C.;
RT "Cloning, localization, and permanent expression of a Drosophila octopamine
RT receptor.";
RL Neuron 4:343-354(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=2170118; DOI=10.1002/j.1460-2075.1990.tb07572.x;
RA Saudou F., Amlaiky N., Plassat J.-L., Borelli E., Hen R.;
RT "Cloning and characterization of a Drosophila tyramine receptor.";
RL EMBO J. 9:3611-3617(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=10713442; DOI=10.1016/s0378-1119(99)00569-7;
RA Kutsukake M., Komatsu A., Yamamoto D., Chigusa S.I.;
RT "A tyramine receptor gene mutation causes a defective olfactory behavior in
RT Drosophila melanogaster.";
RL Gene 245:31-42(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for both octopamine and tyramine, invertebrate
CC neurotransmitters, and neuromodulators. The activity of this receptor
CC is mediated by G proteins which activate adenylyl cyclase. The rank
CC order of potency for agonists is tyramine > octopamine > dopamine >
CC epinephrine > norepinephrine > serotonin > histamine. For antagonists,
CC the rank order is yohimbine > chlorpromazine > phentolamine >
CC mianserine > cyproheptadine > dihydroergotamine > clonidine >
CC synephrine. Tyramine has a functional role in the olfactory system as a
CC neurotransmitter or a neuromodulator. {ECO:0000269|PubMed:10713442}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in Drosophila heads.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M60789; AAA28731.1; -; mRNA.
DR EMBL; X54794; CAA38565.1; -; mRNA.
DR EMBL; AB073914; BAB71788.1; -; mRNA.
DR EMBL; AE014296; AAF51802.1; -; Genomic_DNA.
DR EMBL; BT025156; ABE73326.1; -; mRNA.
DR PIR; JH0170; JH0170.
DR PIR; S12004; S12004.
DR RefSeq; NP_001163494.1; NM_001170023.2.
DR RefSeq; NP_524419.2; NM_079695.4.
DR AlphaFoldDB; P22270; -.
DR STRING; 7227.FBpp0078132; -.
DR GlyGen; P22270; 2 sites.
DR PaxDb; P22270; -.
DR PRIDE; P22270; -.
DR DNASU; 42452; -.
DR EnsemblMetazoa; FBtr0078479; FBpp0078132; FBgn0004514.
DR EnsemblMetazoa; FBtr0301930; FBpp0291142; FBgn0004514.
DR GeneID; 42452; -.
DR KEGG; dme:Dmel_CG7485; -.
DR CTD; 42452; -.
DR FlyBase; FBgn0004514; Oct-TyrR.
DR VEuPathDB; VectorBase:FBgn0004514; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000165278; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; P22270; -.
DR OMA; PMIHNDQ; -.
DR OrthoDB; 737211at2759; -.
DR PhylomeDB; P22270; -.
DR Reactome; R-DME-390696; Adrenoceptors.
DR Reactome; R-DME-392023; Adrenaline signalling through Alpha-2 adrenergic receptor.
DR Reactome; R-DME-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-DME-418594; G alpha (i) signalling events.
DR Reactome; R-DME-418597; G alpha (z) signalling events.
DR BioGRID-ORCS; 42452; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42452; -.
DR PRO; PR:P22270; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0004514; Expressed in brain and 7 other tissues.
DR ExpressionAtlas; P22270; baseline and differential.
DR Genevisible; P22270; DM.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0008227; F:G protein-coupled amine receptor activity; IDA:FlyBase.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0004989; F:octopamine receptor activity; IEA:InterPro.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007211; P:octopamine or tyramine signaling pathway; IDA:FlyBase.
DR GO; GO:1900738; P:positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0010578; P:regulation of adenylate cyclase activity involved in G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0007608; P:sensory perception of smell; IMP:FlyBase.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..601
FT /note="Tyramine/octopamine receptor"
FT /id="PRO_0000012737"
FT TOPO_DOM 27..112
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..135
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..167
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..248
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..295
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..552
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..566
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..588
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 589..601
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 361..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..415
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 182..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 34
FT /note="S -> N (in Ref. 1; AAA28731 and 3; BAB71788)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 601 AA; 64674 MW; 7E7581A11674B4C9 CRC64;
MPSADQILFV NVTTTVAAAA LTAAAAVSTT KSGSGNAARG YTDSDDDAGM GTEAVANISG
SLVEGLTTVT AALSTAQADK DSAGECEGAV EELHASILGL QLAVPEWEAL LTALVLSVII
VLTIIGNILV ILSVFTYKPL RIVQNFFIVS LAVADLTVAL LVLPFNVAYS ILGRWEFGIH
LCKLWLTCDV LCCTSSILNL CAIALDRYWA ITDPINYAQK RTVGRVLLLI SGVWLLSLLI
SSPPLIGWND WPDEFTSATP CELTSQRGYV IYSSLGSFFI PLAIMTIVYI EIFVATRRRL
RERARANKLN TIALKSTELE PMANSSPVAA SNSGSKSRLL ASWLCCGRDR AQFATPMIQN
DQESISSETH QPQDSSKAGP HGNSDPQQQH VVVLVKKSRR AKTKDSIKHG KTRGGRKSQS
SSTCEPHGEQ QLLPAGGDGG SCQPGGGHSG GGKSDAEIST ESGSDPKGCI QVCVTQADEQ
TSLKLTPPQS STGVAAVSVT PLQKKTSGVN QFIEEKQKIS LSKERRAART LGIIMGVFVI
CWLPFFLMYV ILPFCQTCCP TNKFKNFITW LGYINSGLNP VIYTIFNLDY RRAFKRLLGL
N
