OCTB2_DROME
ID OCTB2_DROME Reviewed; 536 AA.
AC Q4LBB9; B7FNM5; Q9VG53; Q9VG54;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Octopamine receptor beta-2R;
DE Short=DmOct-beta-12;
DE Short=DmOct-beta-2R;
GN Name=Octbeta2R {ECO:0000312|FlyBase:FBgn0038063}; Synonyms=Octbeta2;
GN ORFNames=CG33976 {ECO:0000312|FlyBase:FBgn0038063};
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:0000312|EMBL:CAI56430.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Head {ECO:0000312|EMBL:CAI56430.1};
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 [2]
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 [3] {ECO:0000305}
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 [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21186359; DOI=10.1038/nn.2716;
RA Koon A.C., Ashley J., Barria R., DasGupta S., Brain R., Waddell S.,
RA Alkema M.J., Budnik V.;
RT "Autoregulatory and paracrine control of synaptic and behavioral plasticity
RT by octopaminergic signaling.";
RL Nat. Neurosci. 14:190-199(2011).
RN [5]
RP FUNCTION.
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 [6]
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).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25099506; DOI=10.1371/journal.pone.0104441;
RA Lim J., Sabandal P.R., Fernandez A., Sabandal J.M., Lee H.G., Evans P.,
RA Han K.A.;
RT "The octopamine receptor Octbeta2R regulates ovulation in Drosophila
RT melanogaster.";
RL PLoS ONE 9:E104441-E104441(2014).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25353988; DOI=10.1002/arch.21211;
RA Li Y., Fink C., El-Kholy S., Roeder T.;
RT "The octopamine receptor octss2R is essential for ovulation and
RT fertilization in the fruit fly Drosophila melanogaster.";
RL Arch. Insect Biochem. Physiol. 88:168-178(2015).
CC -!- FUNCTION: Autoreceptor for octopamine (OA), which is a
CC neurotransmitter, neurohormone, and neuromodulator in invertebrates
CC (PubMed:15998303, PubMed:21186359). Essential for ovulation and
CC fertilization (PubMed:25099506, PubMed:25353988). During ovulation it
CC mediates the OA-induced relaxation of the oviduct visceral muscles, by
CC increasing cAMP levels and activating effectors such as calmodulin-
CC dependent kinase II (CaMKII) and cAMP-dependent protein kinase A (PKA)
CC pathways (PubMed:25353988). Positively regulates synaptic growth; an
CC action that is antagonized by Octbeta1R (PubMed:21186359,
CC PubMed:22553037). {ECO:0000269|PubMed:21186359,
CC ECO:0000269|PubMed:22553037, ECO:0000269|PubMed:25099506,
CC ECO:0000269|PubMed:25353988}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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 the oviduct epithelium (PubMed:25099506). Also expressed
CC in the spermatheca (PubMed:25353988). Expressed in embryonic and larval
CC ventral nerve cord and brain lobe, embryonic and larval salivary glands
CC and larval imaginal disk and midgut (PubMed:22303848). Also expressed
CC in larval synaptic boutons (PubMed:21186359).
CC {ECO:0000269|PubMed:21186359, ECO:0000269|PubMed:22303848,
CC ECO:0000269|PubMed:25099506, ECO:0000269|PubMed:25353988}.
CC -!- DEVELOPMENTAL STAGE: Expressed in adult, pupae and third instar larvae.
CC Levels peak at the late embryonic and late larvae stages. Relatively
CC low expression in the pupal stage, with a slight increase in the adult.
CC {ECO:0000269|PubMed:22303848}.
CC -!- DISRUPTION PHENOTYPE: Males appear viable and fertile whereas females
CC are sterile (PubMed:25099506, PubMed:25353988). Female pre- and post-
CC mating behaviors, such as courtship and post-mating rejection, are not
CC affected and sperm storage appears normal (PubMed:25099506,
CC PubMed:25353988). However, ovulation and egg-laying is severely
CC impaired and females display a strong delay in copulation rates
CC (PubMed:25099506, PubMed:25353988). Ovaries are enlarged due to a
CC higher number of retained eggs and the small number of eggs that are
CC laid are not fertilized (PubMed:25353988). Larvae fail to respond to
CC starvation by increasing locomotor activity (PubMed:21186359). Reduced
CC growth of octopaminergic and glutamatergic (type I and type II)
CC neuromuscular junctions (PubMed:21186359). Decrease in the number of
CC terminal type I and type II boutons and in the motile filopodia-like
CC extensions (synaptopods) which form during the expansion of type II
CC terminals in developing larvae (PubMed:21186359).
CC {ECO:0000269|PubMed:21186359, ECO:0000269|PubMed:25099506,
CC ECO:0000269|PubMed:25353988}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AJ880689; CAI56430.1; -; mRNA.
DR EMBL; BT053715; ACK77633.1; -; mRNA.
DR EMBL; AE014297; AAF54835.2; -; Genomic_DNA.
DR EMBL; AE014297; AFH06394.1; -; Genomic_DNA.
DR EMBL; AE014297; AFH06395.1; -; Genomic_DNA.
DR EMBL; AE014297; AFH06396.1; -; Genomic_DNA.
DR RefSeq; NP_001034049.1; NM_001038960.3.
DR RefSeq; NP_001247076.1; NM_001260147.1.
DR RefSeq; NP_001247077.1; NM_001260148.1.
DR RefSeq; NP_001247078.1; NM_001260149.2.
DR RefSeq; NP_001303505.1; NM_001316576.1.
DR AlphaFoldDB; Q4LBB9; -.
DR SMR; Q4LBB9; -.
DR BioGRID; 66644; 3.
DR IntAct; Q4LBB9; 3.
DR STRING; 7227.FBpp0293384; -.
DR GlyGen; Q4LBB9; 4 sites.
DR PaxDb; Q4LBB9; -.
DR EnsemblMetazoa; FBtr0100019; FBpp0099980; FBgn0038063.
DR EnsemblMetazoa; FBtr0304844; FBpp0293384; FBgn0038063.
DR EnsemblMetazoa; FBtr0304845; FBpp0293385; FBgn0038063.
DR EnsemblMetazoa; FBtr0304846; FBpp0293386; FBgn0038063.
DR EnsemblMetazoa; FBtr0347149; FBpp0312480; FBgn0038063.
DR GeneID; 41549; -.
DR KEGG; dme:Dmel_CG33976; -.
DR UCSC; CG33976-RA; d. melanogaster.
DR CTD; 41549; -.
DR FlyBase; FBgn0038063; Octbeta2R.
DR VEuPathDB; VectorBase:FBgn0038063; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; Q4LBB9; -.
DR OMA; IGWYTTE; -.
DR OrthoDB; 750855at2759; -.
DR PhylomeDB; Q4LBB9; -.
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 SignaLink; Q4LBB9; -.
DR BioGRID-ORCS; 41549; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41549; -.
DR PRO; PR:Q4LBB9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038063; Expressed in brain and 9 other tissues.
DR ExpressionAtlas; Q4LBB9; baseline and differential.
DR Genevisible; Q4LBB9; 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:0003700; F:DNA-binding transcription factor 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:FlyBase.
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:FlyBase.
DR GO; GO:0009566; P:fertilization; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:FlyBase.
DR GO; GO:0030728; P:ovulation; IMP:FlyBase.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR InterPro; IPR004827; bZIP.
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; 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; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..536
FT /note="Octopamine receptor beta-2R"
FT /id="PRO_0000069960"
FT TOPO_DOM 1..157
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..233
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..256
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..320
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..444
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 121
FT /note="S -> T (in Ref. 1; CAI56430)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="N -> K (in Ref. 1; CAI56430)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="E -> V (in Ref. 1; CAI56430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 536 AA; 60379 MW; 67599A6DAC41280F CRC64;
MLLCDGLGPE PPRQRHRNRT SAARIRKRPK CCCGDGGSGN QAEQPGGIVS NPISYGQSLT
TLARVTAAAL TTAAMLHTTN ALAATGSSSA SNSSTGGIAL PLGTATPATH ELNATQPFGG
SGLNFNESGA GLSDHHHHQQ HNPDEDWLDN IVWVFKAFVM LLIIIAAICG NLLVIISVMR
VRKLRVITNY FVVSLAMADI MVAIMAMTFN FSVQVTGRWN FSPFLCDLWN SLDVYFSTAS
ILHLCCISVD RYYAIVKPLK YPISMTKRVV GIMLLNTWIS PALLSFLPIF IGWYTTPQHQ
QFVIQNPTQC SFVVNKYYAV ISSSISFWIP CTIMIFTYLA IFREANRQEK QLMMRHGNAM
LMHRPSMQPS GEALSGSGSS KTLTLHEVEQ EHTPTKDKHL IKMKREHKAA RTLGIIMGTF
ILCWLPFFLW YTLSMTCEEC QVPDIVVSIL FWIGYFNSTL NPLIYAYFNR DFREAFRNTL
LCLFCNWWKD RHLPLDIDIR RSSLRYDQRA KSVYSESYLN STTPSHRRQS QMVDNL
