OCTB1_DROME
ID OCTB1_DROME Reviewed; 508 AA.
AC Q9VCZ3; A0A0B4KHN2; Q2PDQ3; Q4LBC0;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Octopamine receptor beta-1R;
DE Short=DmOA2;
DE Short=DmOct-beta-1R;
GN Name=Octbeta1R {ECO:0000312|FlyBase:FBgn0038980};
GN Synonyms=oa2 {ECO:0000312|FlyBase:FBgn0038980}, Oct-beta-1;
GN ORFNames=CG6919 {ECO:0000312|FlyBase:FBgn0038980};
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] {ECO:0000305, ECO:0000312|EMBL:CAE84925.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15816867; DOI=10.1111/j.1471-4159.2005.03034.x;
RA Balfanz S., Struenker T., Frings S., Baumann A.;
RT "A family of octopamine receptors that specifically induce cyclic AMP
RT production or Ca2+ release in Drosophila melanogaster.";
RL J. Neurochem. 93:440-451(2005).
RN [2]
RP ERRATUM OF PUBMED:15816867.
RA Balfanz S., Struenker T., Frings S., Baumann A.;
RL J. Neurochem. 94:1168-1168(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAI56428.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC TISSUE=Head {ECO:0000312|EMBL:CAI56428.1};
RX PubMed=15998303; DOI=10.1111/j.1471-4159.2005.03251.x;
RA Maqueira B., Chatwin H., Evans P.D.;
RT "Identification and characterization of a novel family of Drosophila beta-
RT adrenergic-like octopamine G-protein coupled receptors.";
RL J. Neurochem. 94:547-560(2005).
RN [4] {ECO:0000312|EMBL:AAF56012.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305, ECO:0000312|EMBL:AAF56012.1}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22553037; DOI=10.1523/jneurosci.6517-11.2012;
RA Koon A.C., Budnik V.;
RT "Inhibitory control of synaptic and behavioral plasticity by octopaminergic
RT signaling.";
RL J. Neurosci. 32:6312-6322(2012).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=22303848; DOI=10.2108/zsj.29.83;
RA Ohhara Y., Kayashima Y., Hayashi Y., Kobayashi S., Yamakawa-Kobayashi K.;
RT "Expression of beta-adrenergic-like octopamine receptors during Drosophila
RT development.";
RL Zool. Sci. 29:83-89(2012).
CC -!- FUNCTION: Autoreceptor for octopamine, which is a neurotransmitter,
CC neurohormone, and neuromodulator in invertebrates (PubMed:15816867,
CC PubMed:22553037). Negatively regulates synaptic growth by activating
CC the inhibitory G protein Galphao and limiting cAMP production
CC (PubMed:22553037). Antagonizes the action of Octbeta2R which stimulates
CC synaptic growth (PubMed:22553037). {ECO:0000269|PubMed:15816867,
CC ECO:0000269|PubMed:22553037}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000269|PubMed:15998303};
CC IsoId=Q9VCZ3-1; Sequence=Displayed;
CC Name=B {ECO:0000269|PubMed:15998303};
CC IsoId=Q9VCZ3-2; Sequence=VSP_051833, VSP_051834;
CC -!- TISSUE SPECIFICITY: In the adult, expressed in the superior
CC protocerebrum and the optic lobe medulla of the central nervous system,
CC nurse cells of egg chambers in the ovary at oogenic stages 1-10, and
CC spermatogonia and spermatocytes in the testis (PubMed:22303848).
CC Expressed in embryonic and larval ventral nerve cord and brain lobe,
CC and the larval imaginal disk and larval salivary gland
CC (PubMed:22303848). Also expressed in larval synaptic boutons and
CC retinal cells in the optic disk (PubMed:22553037).
CC {ECO:0000269|PubMed:22303848, ECO:0000269|PubMed:22553037}.
CC -!- DEVELOPMENTAL STAGE: Expressed in adult, pupae, third instar larvae,
CC and 0-4 hour and 0-18 hour old embryos (PubMed:15816867,
CC PubMed:22303848). Levels increase significantly at the late embryonic
CC stage, gradually decrease during postembryonic development and increase
CC slightly in the adult (PubMed:22303848). {ECO:0000269|PubMed:15816867,
CC ECO:0000269|PubMed:22303848}.
CC -!- DISRUPTION PHENOTYPE: Fails to respond to starvation by increasing
CC locomotor activity. Decreased basal levels of locomotion. Overgrowth of
CC octopaminergic and glutamatergic (type I and type II) neuromuscular
CC junctions. Increase in the number of terminal type I and type II
CC boutons and in the motile filopodia-like extensions (synaptopods) which
CC form during the expansion of type II terminals in developing larvae.
CC {ECO:0000269|PubMed:22553037}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AJ617526; CAE84925.1; -; mRNA.
DR EMBL; AJ880687; CAI56428.1; -; mRNA.
DR EMBL; AJ880688; CAI56429.1; -; mRNA.
DR EMBL; AE014297; AAF56012.1; -; Genomic_DNA.
DR EMBL; AE014297; ABC66185.1; -; Genomic_DNA.
DR EMBL; AE014297; AGB96223.1; -; Genomic_DNA.
DR RefSeq; NP_001034064.1; NM_001038975.3. [Q9VCZ3-2]
DR RefSeq; NP_001262843.1; NM_001275914.1. [Q9VCZ3-1]
DR RefSeq; NP_651057.1; NM_142800.3. [Q9VCZ3-1]
DR AlphaFoldDB; Q9VCZ3; -.
DR SMR; Q9VCZ3; -.
DR BioGRID; 67607; 1.
DR STRING; 7227.FBpp0304263; -.
DR GlyGen; Q9VCZ3; 1 site.
DR PaxDb; Q9VCZ3; -.
DR DNASU; 42652; -.
DR EnsemblMetazoa; FBtr0084260; FBpp0083653; FBgn0038980. [Q9VCZ3-1]
DR EnsemblMetazoa; FBtr0100322; FBpp0099727; FBgn0038980. [Q9VCZ3-2]
DR EnsemblMetazoa; FBtr0331930; FBpp0304263; FBgn0038980. [Q9VCZ3-1]
DR GeneID; 42652; -.
DR KEGG; dme:Dmel_CG6919; -.
DR CTD; 42652; -.
DR FlyBase; FBgn0038980; Octbeta1R.
DR VEuPathDB; VectorBase:FBgn0038980; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000171582; -.
DR InParanoid; Q9VCZ3; -.
DR PhylomeDB; Q9VCZ3; -.
DR Reactome; R-DME-390651; Dopamine receptors.
DR Reactome; R-DME-390696; Adrenoceptors.
DR Reactome; R-DME-418555; G alpha (s) signalling events.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 42652; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42652; -.
DR PRO; PR:Q9VCZ3; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038980; Expressed in brain and 17 other tissues.
DR ExpressionAtlas; Q9VCZ3; baseline and differential.
DR Genevisible; Q9VCZ3; 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:0004935; F:adrenergic receptor activity; IEA:InterPro.
DR GO; GO:0008227; F:G protein-coupled amine receptor activity; ISS:FlyBase.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0004989; F:octopamine receptor activity; IDA:UniProtKB.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:FlyBase.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR InterPro; IPR002233; ADR_fam.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
DR PRINTS; PR00237; GPCRRHODOPSN.
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 Alternative splicing; Cell membrane; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..508
FT /note="Octopamine receptor beta-1R"
FT /id="PRO_0000069959"
FT TOPO_DOM 1..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..209
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..383
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 440..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 421
FT /note="S -> T (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15998303"
FT /id="VSP_051833"
FT VAR_SEQ 422..508
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15998303"
FT /id="VSP_051834"
SQ SEQUENCE 508 AA; 56855 MW; 02C7C335676EAEF0 CRC64;
MTLLQRLQAM SATTTRTILE GSISSFGGGT NEPLASKIPV LEESASHARY LKFIADGLID
EGLGSAVGSG SSIAVSVEDV VAGQAQDIQA SEGSTDDADG SSHLALVFVK CFIIGFIILA
AILGNMLVIV SVMRHRKLRI ITNYFVVSLA VADMLVALCA MTFNASVMIS GKWMFGSVMC
DMWNSFDVYF STASIMHLCC ISVDRYYAIV QPLDYPLIMT QRRVFIMLLM VWLSPALLSF
LPICSGWYTT TENYKYLKSN PHICEFKVNK AYAIVSSSMS FWIPGIVMLS MYYRIYQEAD
RQERLVYRSK VAALLLEKHL QISQIPKPRP SIQVEQSTIS TMRRERKAAR TLGIIMSAFL
ICWLPFFLWY IVSSLCDSCI TPRLLVGILF WIGYFNSALN PIIYAYFNRD FRAAFKKTLK
SLFPYAFYFC RRGRGRDDDR DLEFGGPSRR GTNGAQRTGS GSAEMANCVN STASSEIHMS
VMRARQYAVN VTPTTDAQMQ QLHPLYTN
