OCTB2_CHISP
ID OCTB2_CHISP Reviewed; 395 AA.
AC G3M4F8;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Octopamine receptor beta-2R {ECO:0000305};
DE Short=CsOA2B2 {ECO:0000303|PubMed:22786641};
GN Name=OA2B2 {ECO:0000303|PubMed:22786641, ECO:0000312|EMBL:AEO89318.1};
OS Chilo suppressalis (Asiatic rice borer moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC Crambidae; Crambinae; Chilo.
OX NCBI_TaxID=168631 {ECO:0000312|EMBL:AEO89318.1};
RN [1] {ECO:0000312|EMBL:AEO89318.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND PHYLOGENETIC ANALYSIS.
RC TISSUE=Nerve cord {ECO:0000303|PubMed:22786641};
RX PubMed=22786641; DOI=10.1242/jeb.068932;
RA Wu S.F., Yao Y., Huang J., Ye G.Y.;
RT "Characterization of a beta-adrenergic-like octopamine receptor from the
RT rice stem borer (Chilo suppressalis).";
RL J. Exp. Biol. 215:2646-2652(2012).
CC -!- FUNCTION: Autoreceptor for octopamine, which is a neurotransmitter,
CC neurohormone, and neuromodulator in invertebrates. Also acts as a
CC receptor for tyramine, but with much less potency. The activity of this
CC receptor is mediated by G proteins which activate adenylyl cyclase.
CC {ECO:0000269|PubMed:22786641}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22786641};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed in egg, larva, pupa and adult. In fifth-
CC instar larvae stage, highly expressed in the nerve cord, and by a
CC lesser extent in the epidermis, hemocytes, Malpighian tubules, midgut
CC and fat body. {ECO:0000269|PubMed:22786641}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521, ECO:0000255|RuleBase:RU000688,
CC ECO:0000305}.
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DR EMBL; JN620367; AEO89318.1; -; mRNA.
DR AlphaFoldDB; G3M4F8; -.
DR SMR; G3M4F8; -.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004989; F:octopamine receptor activity; IDA:UniProtKB.
DR GO; GO:0008226; F:tyramine receptor activity; IDA:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0071418; P:cellular response to amine stimulus; IDA:UniProtKB.
DR GO; GO:0071927; P:octopamine signaling pathway; IDA:UniProtKB.
DR GO; GO:0071928; P:tyramine signaling pathway; IDA:UniProtKB.
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; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..395
FT /note="Octopamine receptor beta-2R"
FT /id="PRO_0000441026"
FT TOPO_DOM 1..42
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 43..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..117
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 118..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..202
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 203..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 283..303
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..315
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 316..336
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 395 AA; 44798 MW; 72D6E375F40C2142 CRC64;
MDPINGSHSG ANATISDITN GAYNATDAGE WTSSVMFKLR TCVLLLIVIM AVLGNMLVIV
SVMRHRKLRV ITNYFVVSLA FADILVAMVV MPFNFSVQFN QGWVFGETIC DLWNSSDVYF
TSTSILHLCC ISVDRYYAIV KPLKYPIKMT KKMAFVMLAA TWLSPITISY VPIFMGWYTT
TDFLESRRDD QCEFKVNKPY AVISSSISFW IPCTIMIFTY LAIFKEANRQ EKALHARAGN
AMLMHRHSRE VSDKNGALHI NATTPTKDRN LLKMKREHKA ARTLGIIMGA FILCWLPFFL
YYVSTSLCDS CNCPEVVTVI MFWTGYFNSA LNPIIYAYFN RDFRNAFKNT LACAFCSFCK
RSASDLDAME RLDRRGSAQL RVPIPSRRAS DLASL
