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Octopamine receptor beta-2R (DmOct-beta-12) (DmOct-beta-2R)

 OCTB2_DROME             Reviewed;         536 AA.
Q4LBB9; B7FNM5; Q9VG53; Q9VG54;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 2.
18-JUL-2018, entry version 118.
RecName: Full=Octopamine receptor beta-2R;
Short=DmOct-beta-12;
Short=DmOct-beta-2R;
Name=Octbeta2R {ECO:0000312|FlyBase:FBgn0038063}; Synonyms=Octbeta2;
ORFNames=CG33976 {ECO:0000312|FlyBase:FBgn0038063};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000312|EMBL:CAI56430.1}
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Head {ECO:0000312|EMBL:CAI56430.1};
PubMed=15998303; DOI=10.1111/j.1471-4159.2005.03251.x;
Maqueira B., Chatwin H., Evans P.D.;
"Identification and characterization of a novel family of Drosophila
beta-adrenergic-like octopamine G-protein coupled receptors.";
J. Neurochem. 94:547-560(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3] {ECO:0000305}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=21186359; DOI=10.1038/nn.2716;
Koon A.C., Ashley J., Barria R., DasGupta S., Brain R., Waddell S.,
Alkema M.J., Budnik V.;
"Autoregulatory and paracrine control of synaptic and behavioral
plasticity by octopaminergic signaling.";
Nat. Neurosci. 14:190-199(2011).
[5]
FUNCTION.
PubMed=22553037; DOI=10.1523/JNEUROSCI.6517-11.2012;
Koon A.C., Budnik V.;
"Inhibitory control of synaptic and behavioral plasticity by
octopaminergic signaling.";
J. Neurosci. 32:6312-6322(2012).
[6]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=22303848; DOI=10.2108/zsj.29.83;
Ohhara Y., Kayashima Y., Hayashi Y., Kobayashi S.,
Yamakawa-Kobayashi K.;
"Expression of beta-adrenergic-like octopamine receptors during
Drosophila development.";
Zool. Sci. 29:83-89(2012).
[7]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=25099506; DOI=10.1371/journal.pone.0104441;
Lim J., Sabandal P.R., Fernandez A., Sabandal J.M., Lee H.G.,
Evans P., Han K.A.;
"The octopamine receptor Octbeta2R regulates ovulation in Drosophila
melanogaster.";
PLoS ONE 9:E104441-E104441(2014).
[8]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=25353988; DOI=10.1002/arch.21211;
Li Y., Fink C., El-Kholy S., Roeder T.;
"The octopamine receptor octss2R is essential for ovulation and
fertilization in the fruit fly Drosophila melanogaster.";
Arch. Insect Biochem. Physiol. 88:168-178(2015).
-!- FUNCTION: Autoreceptor for octopamine (OA), which is a
neurotransmitter, neurohormone, and neuromodulator in
invertebrates (PubMed:15998303, PubMed:21186359). Essential for
ovulation and fertilization (PubMed:25099506, PubMed:25353988).
During ovulation it mediates the OA-induced relaxation of the
oviduct visceral muscles, by increasing cAMP levels and activating
effectors such as calmodulin-dependent kinase II (CaMKII) and
cAMP-dependent protein kinase A (PKA) pathways (PubMed:25353988).
Positively regulates synaptic growth; an action that is
antagonized by Octbeta1R (PubMed:21186359, PubMed:22553037).
{ECO:0000269|PubMed:21186359, ECO:0000269|PubMed:22553037,
ECO:0000269|PubMed:25099506, ECO:0000269|PubMed:25353988}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: In the adult, expressed in the superior
protocerebrum and the optic lobe medulla of the central nervous
system, nurse cells of egg chambers in the ovary at oogenic stages
1-10, and spermatogonia and spermatocytes in the testis
(PubMed:22303848). Expressed in the oviduct epithelium
(PubMed:25099506). Also expressed in the spermatheca
(PubMed:25353988). Expressed in embryonic and larval ventral nerve
cord and brain lobe, embryonic and larval salivary glands and
larval imaginal disk and midgut (PubMed:22303848). Also expressed
in larval synaptic boutons (PubMed:21186359).
{ECO:0000269|PubMed:21186359, ECO:0000269|PubMed:22303848,
ECO:0000269|PubMed:25099506, ECO:0000269|PubMed:25353988}.
-!- DEVELOPMENTAL STAGE: Expressed in adult, pupae and third instar
larvae. Levels peak at the late embryonic and late larvae stages.
Relatively low expression in the pupal stage, with a slight
increase in the adult. {ECO:0000269|PubMed:22303848}.
-!- DISRUPTION PHENOTYPE: Males appear viable and fertile whereas
females are sterile (PubMed:25099506, PubMed:25353988). Female
pre- and post-mating behaviors, such as courtship and post-mating
rejection, are not affected and sperm storage appears normal
(PubMed:25099506, PubMed:25353988). However, ovulation and egg-
laying is severely impaired and females display a strong delay in
copulation rates (PubMed:25099506, PubMed:25353988). Ovaries are
enlarged due to a higher number of retained eggs and the small
number of eggs that are laid are not fertilized (PubMed:25353988).
Larvae fail to respond to starvation by increasing locomotor
activity (PubMed:21186359). Reduced growth of octopaminergic and
glutamatergic (type I and type II) neuromuscular junctions
(PubMed:21186359). Decrease in the number of terminal type I and
type II boutons and in the motile filopodia-like extensions
(synaptopods) which form during the expansion of type II terminals
in developing larvae (PubMed:21186359).
{ECO:0000269|PubMed:21186359, ECO:0000269|PubMed:25099506,
ECO:0000269|PubMed:25353988}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AJ880689; CAI56430.1; -; mRNA.
EMBL; BT053715; ACK77633.1; -; mRNA.
EMBL; AE014297; AAF54835.2; -; Genomic_DNA.
EMBL; AE014297; AFH06394.1; -; Genomic_DNA.
EMBL; AE014297; AFH06395.1; -; Genomic_DNA.
EMBL; AE014297; AFH06396.1; -; Genomic_DNA.
RefSeq; NP_001034049.1; NM_001038960.3.
RefSeq; NP_001247076.1; NM_001260147.1.
RefSeq; NP_001247077.1; NM_001260148.1.
RefSeq; NP_001247078.1; NM_001260149.2.
RefSeq; NP_001303505.1; NM_001316576.1.
UniGene; Dm.29778; -.
ProteinModelPortal; Q4LBB9; -.
SMR; Q4LBB9; -.
BioGrid; 66644; 2.
IntAct; Q4LBB9; 4.
STRING; 7227.FBpp0303153; -.
PaxDb; Q4LBB9; -.
PRIDE; Q4LBB9; -.
EnsemblMetazoa; FBtr0100019; FBpp0099980; FBgn0038063.
EnsemblMetazoa; FBtr0304844; FBpp0293384; FBgn0038063.
EnsemblMetazoa; FBtr0304845; FBpp0293385; FBgn0038063.
EnsemblMetazoa; FBtr0304846; FBpp0293386; FBgn0038063.
EnsemblMetazoa; FBtr0330120; FBpp0303153; FBgn0038063.
EnsemblMetazoa; FBtr0347149; FBpp0312480; FBgn0038063.
GeneID; 41549; -.
KEGG; dme:Dmel_CG33976; -.
UCSC; CG33976-RA; d. melanogaster.
CTD; 41549; -.
FlyBase; FBgn0038063; Octbeta2R.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00890000139331; -.
InParanoid; Q4LBB9; -.
OMA; HRRQDEA; -.
OrthoDB; EOG091G0FLO; -.
PhylomeDB; Q4LBB9; -.
GenomeRNAi; 41549; -.
PRO; PR:Q4LBB9; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0038063; -.
ExpressionAtlas; Q4LBB9; baseline and differential.
Genevisible; Q4LBB9; DM.
GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0003700; F:DNA binding transcription factor activity; IEA:InterPro.
GO; GO:0008227; F:G-protein coupled amine receptor activity; ISS:FlyBase.
GO; GO:0004989; F:octopamine receptor activity; IDA:FlyBase.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:FlyBase.
GO; GO:0009566; P:fertilization; IMP:FlyBase.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISS:FlyBase.
GO; GO:0030728; P:ovulation; IMP:FlyBase.
GO; GO:0045887; P:positive regulation of synaptic growth at neuromuscular junction; IMP:FlyBase.
InterPro; IPR004827; bZIP.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; G-protein coupled receptor;
Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
Transmembrane; Transmembrane helix.
CHAIN 1 536 Octopamine receptor beta-2R.
/FTId=PRO_0000069960.
TOPO_DOM 1 157 Extracellular. {ECO:0000255}.
TRANSMEM 158 178 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 179 190 Cytoplasmic. {ECO:0000255}.
TRANSMEM 191 211 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 212 233 Extracellular. {ECO:0000255}.
TRANSMEM 234 256 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 257 270 Cytoplasmic. {ECO:0000255}.
TRANSMEM 271 291 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 292 320 Extracellular. {ECO:0000255}.
TRANSMEM 321 341 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 342 412 Cytoplasmic. {ECO:0000255}.
TRANSMEM 413 433 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 434 444 Extracellular. {ECO:0000255}.
TRANSMEM 445 465 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 466 536 Cytoplasmic. {ECO:0000255}.
CARBOHYD 18 18 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 121 121 S -> T (in Ref. 1; CAI56430).
{ECO:0000305}.
CONFLICT 124 124 N -> K (in Ref. 1; CAI56430).
{ECO:0000305}.
CONFLICT 439 439 E -> V (in Ref. 1; CAI56430).
{ECO:0000305}.
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


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