AA2BR_CHICK
ID AA2BR_CHICK Reviewed; 340 AA.
AC O13076; Q540H7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Adenosine receptor A2b;
DE AltName: Full=Adenosine receptor 2b;
GN Name=ADORA2B;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SPAFAS;
RX PubMed=9244356; DOI=10.1038/sj.onc.1201179;
RA Worpenberg S., Burk O., Klempnauer K.H.;
RT "The chicken adenosine receptor 2B gene is regulated by v-myb.";
RL Oncogene 15:213-221(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12559577; DOI=10.1016/s0378-1119(02)01155-1;
RA Braas D., Kattmann D., Miethe J., Klempnauer K.H.;
RT "Analysis of DNase I-hypersensitive sites in the chromatin of the chicken
RT adenosine receptor 2B gene reveals multiple cell-type-specific cis-
RT regulatory elements.";
RL Gene 303:157-164(2003).
CC -!- FUNCTION: Receptor for adenosine. The activity of this receptor is
CC mediated by G proteins which activate adenylyl cyclase.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; Y12601; CAA73173.1; -; mRNA.
DR EMBL; AY169692; AAN87848.1; -; Genomic_DNA.
DR RefSeq; NP_990418.1; NM_205087.1.
DR AlphaFoldDB; O13076; -.
DR SMR; O13076; -.
DR STRING; 9031.ENSGALP00000027991; -.
DR PaxDb; O13076; -.
DR Ensembl; ENSGALT00000028044; ENSGALP00000027991; ENSGALG00000014182.
DR GeneID; 395971; -.
DR KEGG; gga:395971; -.
DR CTD; 136; -.
DR VEuPathDB; HostDB:geneid_395971; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234555; -.
DR HOGENOM; CLU_009579_11_5_1; -.
DR InParanoid; O13076; -.
DR OMA; PVKCLFE; -.
DR OrthoDB; 550297at2759; -.
DR PhylomeDB; O13076; -.
DR Reactome; R-GGA-417973; Adenosine P1 receptors.
DR Reactome; R-GGA-418555; G alpha (s) signalling events.
DR Reactome; R-GGA-5683826; Surfactant metabolism.
DR PRO; PR:O13076; -.
DR Proteomes; UP000000539; Chromosome 19.
DR Bgee; ENSGALG00000014182; Expressed in cerebellum and 11 other tissues.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0001609; F:G protein-coupled adenosine receptor activity; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
DR GO; GO:0019934; P:cGMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0043303; P:mast cell degranulation; IEA:Ensembl.
DR GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
DR GO; GO:0002882; P:positive regulation of chronic inflammatory response to non-antigenic stimulus; IEA:Ensembl.
DR GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IEA:Ensembl.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IEA:Ensembl.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IEA:Ensembl.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; IEA:Ensembl.
DR GO; GO:0042311; P:vasodilation; IBA:GO_Central.
DR InterPro; IPR001435; Adeno_A2B_rcpt.
DR InterPro; IPR001634; Adenosn_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00554; ADENOSINA2BR.
DR PRINTS; PR00424; ADENOSINER.
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; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..340
FT /note="Adenosine receptor A2b"
FT /id="PRO_0000069006"
FT TOPO_DOM 1..6
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 7..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 32..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 42..65
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 66..76
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 77..99
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 100..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 120..142
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 143..178
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 179..203
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 204..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 236..259
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 260..267
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 268..291
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 292..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT BINDING 254
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT BINDING 279
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT BINDING 280
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT LIPID 310
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 76..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 340 AA; 37772 MW; 2DAC18E6DC6A950F CRC64;
MNTMKTTYIV LELIIAVLSI AGNVLVCWAV AINSTLKNAT NYFLVSLAVA DIAVGLLAIP
FAITISIGFQ VDFHSCLFFA CFVLVLTQSS IFSLLAVAID RYLAIKIPLR YNSLVTGKRA
RGLIAVLWLL SFVIGLTPLM GWNKAMSGCP NSTNETGADH GAGHHGCFIS CLFENVVTMS
YMVYFNFFGC VLLPLIIMLG IYIKIFMVAC KQLHQIELMG NSRTTLQKEV HAAKSLAIIV
GLFAFCWLPL HILNCITHFH EEFSKSKPEW VMYVAIILSH ANSVINPIIY AYRIRDFRYT
FHKIISKILC KTDDFPKCTT DNNQHLTVTN VNAPAASVTI
