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AA2BR_BOVIN
ID   AA2BR_BOVIN             Reviewed;         332 AA.
AC   Q1LZD0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Adenosine receptor A2b;
GN   Name=ADORA2B;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) 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; BC116078; AAI16079.1; -; mRNA.
DR   RefSeq; NP_001069393.1; NM_001075925.1.
DR   AlphaFoldDB; Q1LZD0; -.
DR   SMR; Q1LZD0; -.
DR   STRING; 9913.ENSBTAP00000009974; -.
DR   BindingDB; Q1LZD0; -.
DR   PaxDb; Q1LZD0; -.
DR   PRIDE; Q1LZD0; -.
DR   Ensembl; ENSBTAT00000009974; ENSBTAP00000009974; ENSBTAG00000007581.
DR   GeneID; 529760; -.
DR   KEGG; bta:529760; -.
DR   CTD; 136; -.
DR   VEuPathDB; HostDB:ENSBTAG00000007581; -.
DR   VGNC; VGNC:25688; ADORA2B.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234555; -.
DR   HOGENOM; CLU_009579_11_5_1; -.
DR   InParanoid; Q1LZD0; -.
DR   OMA; PVKCLFE; -.
DR   OrthoDB; 550297at2759; -.
DR   TreeFam; TF325296; -.
DR   Reactome; R-BTA-417973; Adenosine P1 receptors.
DR   Reactome; R-BTA-5683826; Surfactant metabolism.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000007581; Expressed in monocyte and 99 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..332
FT                   /note="Adenosine receptor A2b"
FT                   /id="PRO_0000269714"
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;  36385 MW;  DCC4B50BFB2E3B29 CRC64;
     MPLEAQDAVY VALELALAAL SVTGNVLVCA AVGTSSALQT PTNYFLVSLA AADVAVGLFA
     IPFAVTISLG FCTDFHSCLF LACFVLVLTQ SSIFSLLAVA VDRYLAVRVP LRYKSLVTGA
     RARGVIAALW VLAFGIGLTP FLGWNDRKIA TNCTEPGDAA TNVSCCLIRC LFENVVPMSY
     MVYFNFFGCV LPPLLIMLVI YVKIFLVACR QLQRTELMDH SRTVLQREIH AAKSLALIVG
     IFALCWLPVH TINCASLFQP TWAKVKPKWA INTAILLSHA NSAVNPIVYA YRNRDFRYTF
     HKIISRYILC RTHILKSGEG QVGSQPTLQL GL
 
 
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