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Octopamine receptor beta-3R (DmOct-beta-3R)

 OCTB3_DROME             Reviewed;        1256 AA.
Q4LBB6; A0AVV1; Q2PDR1; Q2PDR2; Q2PDR3; Q2PDR4; Q2PDR5; Q2PDR6;
Q4LBB5; Q4LBB7; Q4LBB8; Q8INI6; Q8INI7; Q9VG56; Q9VG57;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
21-SEP-2011, sequence version 4.
23-MAY-2018, entry version 114.
RecName: Full=Octopamine receptor beta-3R;
Short=DmOct-beta-3R;
Name=Octbeta3R {ECO:0000312|FlyBase:FBgn0250910}; Synonyms=Oct-beta-3;
ORFNames=CG42244 {ECO:0000312|FlyBase:FBgn0250910};
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:0000305, ECO:0000312|EMBL:CAI56424.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C AND D).
TISSUE=Head {ECO:0000312|EMBL:CAI56424.1};
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, AND ALTERNATIVE SPLICING.
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM F).
STRAIN=Berkeley;
Stapleton M., Carlson J., Frise E., Kapadia B., Park S., Wan K.,
Yu C., Celniker S.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25605909; DOI=10.1073/pnas.1414966112;
Ohhara Y., Shimada-Niwa Y., Niwa R., Kayashima Y., Hayashi Y.,
Akagi K., Ueda H., Yamakawa-Kobayashi K., Kobayashi S.;
"Autocrine regulation of ecdysone synthesis by beta3-octopamine
receptor in the prothoracic gland is essential for Drosophila
metamorphosis.";
Proc. Natl. Acad. Sci. U.S.A. 112:1452-1457(2015).
-!- FUNCTION: Autoreceptor for octopamine, which is a
neurotransmitter, neurohormone, and neuromodulator in
invertebrates (By similarity). Probably also acts as a receptor
for tyramine during ecdysone biosynthesis (PubMed:25605909).
Required for the biosynthesis of the steroid hormone ecdysone
which is necessary for metamorphosis (PubMed:25605909). Involved
in activation of prothoracicotropic hormone and insulin-like
peptide signaling which is required for the expression of ecdysone
biosynthetic genes (PubMed:25605909).
{ECO:0000250|UniProtKB:Q9VCZ3, ECO:0000269|PubMed:25605909}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=F;
IsoId=Q4LBB6-6; Sequence=Displayed;
Name=D {ECO:0000269|PubMed:15998303}; Synonyms=variant A
{ECO:0000303|PubMed:15998303};
IsoId=Q4LBB6-4; Sequence=VSP_041777;
Name=A {ECO:0000269|PubMed:15998303}; Synonyms=variant D
{ECO:0000303|PubMed:15998303};
IsoId=Q4LBB6-2; Sequence=VSP_051835;
Name=B {ECO:0000269|PubMed:15998303}; Synonyms=variant C
{ECO:0000303|PubMed:15998303};
IsoId=Q4LBB6-1; Sequence=VSP_041779, VSP_041782;
Name=C {ECO:0000269|PubMed:15998303}; Synonyms=variant B
{ECO:0000303|PubMed:15998303};
IsoId=Q4LBB6-3; Sequence=VSP_051837;
Name=G;
IsoId=Q4LBB6-7; Sequence=VSP_041783;
Note=No experimental confirmation available.;
Name=J;
IsoId=Q4LBB6-8; Sequence=VSP_041778;
Note=No experimental confirmation available.;
Name=H;
IsoId=Q4LBB6-9; Sequence=VSP_041780, VSP_041781;
-!- TISSUE SPECIFICITY: In the adult, expressed in the inferior and
superior protocerebrum, the posterior lateral protocerebrum, the
deutocerebrum, the surface of the subesophageal ganglion, the
lateral cell body region, the cortical layer of the ventral nerve
cord and the optic lobe medulla of the central nervous system
(CNS). Also expressed in the nurse cells and follicle cells of the
egg chambers in the ovary at oogenic stages 1-10, and
spermatogonia and spermatocytes in the testis. Expressed
ubiquitously in the embryonic CNS. In larvae, expressed in the
ventral cortical layer of the ventral nerve cord, the cortical
layer of the brain lobes, salivary glands, midgut, imaginal disks
and developing reproductive organs. Expressed in the larval
prothoracic gland with weak expression in other regions of the
ring gland. {ECO:0000269|PubMed:22303848}.
-!- DEVELOPMENTAL STAGE: Levels peak during the late embryonic stages.
Slight increase in expression at the mid-larval stage that
decreases over the pupal stage and then slightly increases in the
adult. {ECO:0000269|PubMed:22303848}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the prothoracic
gland results in developmental arrest at the larval stage. This
larval-prepual arrest can be rescued by supplementing larvae diet
with 20-hydroxyecdysone (20E). {ECO:0000269|PubMed:25605909}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; AJ884591; CAI56424.1; -; mRNA.
EMBL; AJ884592; CAI56425.1; -; mRNA.
EMBL; AJ884593; CAI56426.1; -; mRNA.
EMBL; AJ884594; CAI56427.1; -; mRNA.
EMBL; AE014297; AAF54832.2; -; Genomic_DNA.
EMBL; AE014297; ABC66171.2; -; Genomic_DNA.
EMBL; AE014297; ABC66172.2; -; Genomic_DNA.
EMBL; AE014297; ABC66173.2; -; Genomic_DNA.
EMBL; BT029269; ABK30906.1; -; mRNA.
RefSeq; NP_001034043.2; NM_001038954.2. [Q4LBB6-8]
RefSeq; NP_001034046.3; NM_001038957.3. [Q4LBB6-1]
RefSeq; NP_001034048.2; NM_001038959.3. [Q4LBB6-6]
RefSeq; NP_650210.2; NM_141953.3. [Q4LBB6-7]
UniGene; Dm.26051; -.
ProteinModelPortal; Q4LBB6; -.
SMR; Q4LBB6; -.
IntAct; Q4LBB6; 3.
STRING; 7227.FBpp0288773; -.
PaxDb; Q4LBB6; -.
PRIDE; Q4LBB6; -.
EnsemblMetazoa; FBtr0290334; FBpp0288773; FBgn0250910. [Q4LBB6-6]
EnsemblMetazoa; FBtr0290335; FBpp0288774; FBgn0250910. [Q4LBB6-7]
EnsemblMetazoa; FBtr0301944; FBpp0291156; FBgn0250910. [Q4LBB6-8]
EnsemblMetazoa; FBtr0308597; FBpp0300821; FBgn0250910. [Q4LBB6-1]
GeneID; 3885573; -.
KEGG; dme:Dmel_CG42244; -.
UCSC; CG42244-RB; d. melanogaster.
CTD; 3885573; -.
FlyBase; FBgn0250910; Octbeta3R.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00890000139331; -.
InParanoid; Q4LBB6; -.
OMA; YCKIFRE; -.
OrthoDB; EOG091G0FLO; -.
PhylomeDB; Q4LBB6; -.
ChiTaRS; Octbeta3R; fly.
GenomeRNAi; 3885573; -.
PRO; PR:Q4LBB6; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0250910; -.
Genevisible; Q4LBB6; 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: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:0007186; P:G-protein coupled receptor signaling pathway; IDA:FlyBase.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 2.
2: Evidence at transcript level;
Alternative splicing; Cell membrane; Complete proteome;
G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
Reference proteome; Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 1256 Octopamine receptor beta-3R.
/FTId=PRO_0000069961.
TOPO_DOM 1 143 Extracellular. {ECO:0000255}.
TRANSMEM 144 164 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 165 171 Cytoplasmic. {ECO:0000255}.
TRANSMEM 172 192 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 193 213 Extracellular. {ECO:0000255}.
TRANSMEM 214 236 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 237 258 Cytoplasmic. {ECO:0000255}.
TRANSMEM 259 279 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 280 305 Extracellular. {ECO:0000255}.
TRANSMEM 306 326 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 327 1169 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1170 1190 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 1191 1202 Extracellular. {ECO:0000255}.
TRANSMEM 1203 1223 Helical; Name=8. {ECO:0000255}.
TOPO_DOM 1224 1256 Cytoplasmic. {ECO:0000255}.
CARBOHYD 36 36 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 262 1166 Missing (in isoform A).
{ECO:0000303|PubMed:15998303}.
/FTId=VSP_051835.
VAR_SEQ 331 1256 Missing (in isoform C).
{ECO:0000303|PubMed:15998303}.
/FTId=VSP_051837.
VAR_SEQ 351 1166 Missing (in isoform D).
{ECO:0000303|PubMed:15998303}.
/FTId=VSP_041777.
VAR_SEQ 351 1161 Missing (in isoform J). {ECO:0000305}.
/FTId=VSP_041778.
VAR_SEQ 390 456 DMLQPATDEDDDRDECDELRVPSPPPRRLSRSSIDLRDLEQ
ERYEKVTHTDSAPSMMALQQQQPSHN -> AVPCDRPKDGR
PNTRPPAPWASSWASFCSAGCPSFCGMSSHRSAVRPAHVPM
CSWWCYSGSVTSTPR (in isoform B).
{ECO:0000303|PubMed:15998303}.
/FTId=VSP_041779.
VAR_SEQ 390 395 DMLQPA -> VSLEGY (in isoform H).
{ECO:0000305}.
/FTId=VSP_041780.
VAR_SEQ 396 1256 Missing (in isoform H). {ECO:0000305}.
/FTId=VSP_041781.
VAR_SEQ 457 1256 Missing (in isoform B).
{ECO:0000303|PubMed:15998303}.
/FTId=VSP_041782.
VAR_SEQ 1013 1151 KHEFSNKSSLIRRGGICIFVDEEEAEIIEQRPRGITFAAVP
SPLPKCPLCGADISSTTGTTANATATANADSTIDTTVTTSS
KRSIHEQTPDLGQRPASSSSSTRFWHKRTAAVTACWQQSKN
RKRRFKTGCSHCGATG -> S (in isoform G).
{ECO:0000305}.
/FTId=VSP_041783.
CONFLICT 12 12 T -> A (in Ref. 1; CAI56425).
{ECO:0000305}.
CONFLICT 98 98 L -> S (in Ref. 1; CAI56426).
{ECO:0000305}.
CONFLICT 122 122 A -> T (in Ref. 1; CAI56424/CAI56425/
CAI56426/CAI56427). {ECO:0000305}.
CONFLICT 132 132 S -> G (in Ref. 1; CAI56426).
{ECO:0000305}.
CONFLICT 211 211 F -> L (in Ref. 1; CAI56426).
{ECO:0000305}.
CONFLICT 211 211 F -> P (in Ref. 1; CAI56425).
{ECO:0000305}.
CONFLICT 262 262 A -> TSSA (in Ref. 1; CAI56427).
{ECO:0000305}.
CONFLICT 320 320 V -> L (in Ref. 4; ABK30906).
{ECO:0000305}.
CONFLICT 679 679 K -> R (in Ref. 4; ABK30906).
{ECO:0000305}.
CONFLICT 852 852 Y -> C (in Ref. 4; ABK30906).
{ECO:0000305}.
CONFLICT 1186 1186 L -> M (in Ref. 1; CAI56427).
{ECO:0000305}.
SEQUENCE 1256 AA; 136370 MW; 9DA3CF6523B94A69 CRC64;
MSGVNVADLL ATTMTLPITA AAGAATSQAA ATSATNASHL QPATLTGHIS TTAAAKTTTT
PTSSLPITSQ FVDASLTSLS LTATSSDASY SSPFSSYLSS DSTFELLSTV GPNITANGSD
IAVDNQAELE ESWLDLSLLL LKGFIFSSII LAAVLGNALV IISVQRNRKL RVITNYFVVS
LAMADMLVAL CAMTFNASVE LSGGKWMFGP FMCNVYNSLD VYFSTASILH LCCISVDRYY
AIVRPLEYPL NMTHKTVCFM LANVWILPAL ISFTPIFLGW YTTEEHLREI SLHPDQCSFV
VNKAYALISS SVSFWIPGIV MLVMYWRIFK EAIRQRKALS RTSSNILLNS VHMGHTQQPT
SLSYLHPSDC DLNATSAREE THSALSNLED MLQPATDEDD DRDECDELRV PSPPPRRLSR
SSIDLRDLEQ ERYEKVTHTD SAPSMMALQQ QQPSHNQLQP PAPVFNPQIW TEGKMIPSKE
LDKEHSHPNG PQQQLSLTSG SGNSEPEPES TAYRVFGGLN SDESEGNDLY DTHLPLAEDN
KELKRLIEDN YLYFKRQTGG TIISGPGGGK YAALSETDFI RLKAGAAACG RKAFASSDSE
FLRTISESRA LPEQPVPGKE KGFNILSLLS KTKRSSTECF TLEKKRHQAN SEGSSFFRRS
RNRKLSHSYN GCGGGKERKL ERRQRQHSDT DSTPNKPDIL LDINVLSEQS GASVIQQFSD
GVQLIDFSEL KTPPERIRSD DELAQLADCF GESPQQPATP PPSLSPPELP EPSGLLIASS
SELAEIFRSL SFPLGRPAGA PQRLSTLSDQ VCANYLMSPP NTPAPPAISV PNGGAMDSSA
SSNAQSASIN VYFLSPPPHA AAPGYTPSDT STVSLDVVTS LPMPVPVPQP NPQMASQSNI
SPKPEIILDS TLSPVEGCGD EHRDVTSPLF KRKDSAGDAD VSVSGNGGAG GVGGVGGRQG
RCSILAGYDG IQTVRKRQAS VVTYDVNVIN FSQENSDSRS YIPMGRVSTS SAKHEFSNKS
SLIRRGGICI FVDEEEAEII EQRPRGITFA AVPSPLPKCP LCGADISSTT GTTANATATA
NADSTIDTTV TTSSKRSIHE QTPDLGQRPA SSSSSTRFWH KRTAAVTACW QQSKNRKRRF
KTGCSHCGAT GGSVRPAKGW KAEHKAARTL GIIMGVFLLC WLPFFLWYVI TSLCGPACPC
PDVLVVVLFW IGYFNSTLNP LIYAYFNRDF REAFRNTLEC VLPCLEKRNP YNAYYV


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EIAAB42156 Pig,Sus scrofa,TbetaR-I,TGF-beta receptor type I,TGF-beta receptor type-1,TGF-beta type I receptor,TGFBR1,TGFR-1,Transforming growth factor-beta receptor type I
EIAAB13284 ERR beta-2,ERRB2,ERR-beta,ESRL2,ESRRB,Estrogen receptor-like 2,Estrogen-related receptor beta,Homo sapiens,Human,NR3B2,Nuclear receptor subfamily 3 group B member 2,Steroid hormone receptor ERR2
U1837h CLIA kit High affinity IL-2 receptor subunit beta,Homo sapiens,Human,IL-2 receptor subunit beta,IL-2R subunit beta,IL2RB,IL-2RB,Interleukin-2 receptor subunit beta,p70-75,p75 96T
E1837h ELISA High affinity IL-2 receptor subunit beta,Homo sapiens,Human,IL-2 receptor subunit beta,IL-2R subunit beta,IL2RB,IL-2RB,Interleukin-2 receptor subunit beta,p70-75,p75 96T
U1837h CLIA High affinity IL-2 receptor subunit beta,Homo sapiens,Human,IL-2 receptor subunit beta,IL-2R subunit beta,IL2RB,IL-2RB,Interleukin-2 receptor subunit beta,p70-75,p75 96T


 

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