AA2BR_CANLF
ID AA2BR_CANLF Reviewed; 332 AA.
AC Q6W3F4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Adenosine receptor A2b;
GN Name=ADORA2B;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Auchampach J.A., Jin X., Wang J., Moore J., Wan T.C., Keckler L., Ge Z.-D.,
RA Smits G., Whalley E., Ticho B., Gross G.J.;
RT "Reduction in infarct size by CPX and the renal modulating agent BG 9928:
RT evidence for involvement of A2B adenosine receptors.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for adenosine. The activity of this receptor is
CC mediated by G proteins which activate adenylyl cyclase (By similarity).
CC {ECO:0000250}.
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; AY313204; AAQ82905.1; -; mRNA.
DR RefSeq; NP_001002944.1; NM_001002944.1.
DR AlphaFoldDB; Q6W3F4; -.
DR SMR; Q6W3F4; -.
DR STRING; 9612.ENSCAFP00000026712; -.
DR PaxDb; Q6W3F4; -.
DR GeneID; 403410; -.
DR KEGG; cfa:403410; -.
DR CTD; 136; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q6W3F4; -.
DR OrthoDB; 550297at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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..332
FT /note="Adenosine receptor A2b"
FT /id="PRO_0000069002"
FT TOPO_DOM 1..8
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 9..33
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 34..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 44..67
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 68..78
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 79..101
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 102..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 122..144
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 145..177
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 178..202
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 203..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 235..258
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 259..266
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 267..290
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 291..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT BINDING 253
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT BINDING 278
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 LIPID 310
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 332 AA; 36387 MW; 627BCB21C14B443C CRC64;
MQLETQDALY VALELAIAAL SVAGNVLVCA AVGTSSALQT PTNYFLVSLA AADVAVGLFA
IPFAITISLG FCTDFHSCLF LACFVLVLTQ SSIFSLLAVA VDRYLAIRVP LRYKSLVTGT
RARGVIAVLW VLAFGIGLTP FLGWNSKDSA TNCTEPWDGT TNESCCLVKC LFENVVPMSY
MVYFNFFGCV LPPLLIMLVI YIKIFMVACK QLQRTELVDH SRTVIQREIH AAKSLAMIVG
IFALCWLPVH AINCVTLFQP ARAKDKPKWA MNMAILLSHA SSVVNPIVYA YRNRDFRYTF
HKIISRYVLC QTDVLKSGNG QAGTQSALDV GL
