ADA2B_RAT
ID ADA2B_RAT Reviewed; 453 AA.
AC P19328; Q63021; Q925E4;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Alpha-2B adrenergic receptor;
DE AltName: Full=Alpha-2B adrenoreceptor;
DE Short=Alpha-2B adrenoceptor;
DE Short=Alpha-2BAR;
GN Name=Adra2b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=2158103; DOI=10.1073/pnas.87.8.3102;
RA Zeng D., Harrison J.K., D'Angelo D.D., Barber C.M., Tucker A.L., Lu Z.,
RA Lynch K.R.;
RT "Molecular characterization of a rat alpha 2B-adrenergic receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3102-3106(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=15993847; DOI=10.1016/j.bcp.2005.05.024;
RA Schaak S., Cussac D., Labialle S., Mignotte V., Paris H.;
RT "Cloning and functional characterization of the rat alpha2B-adrenergic
RT receptor gene promoter region: evidence for binding sites for
RT erythropoiesis-related transcription factors GATA1 and NF-E2.";
RL Biochem. Pharmacol. 70:606-617(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-453.
RC STRAIN=Sabra; TISSUE=Kidney;
RX PubMed=7755946; DOI=10.1016/0895-7061(94)00177-d;
RA le Jossec M., Cloix J.F., Pecquery R., Giudicelli Y., Dausse J.P.;
RT "Differential sodium regulation between salt-sensitive and salt-resistant
RT Sabra rats is not due to any mutation in the renal alpha 2B-adrenoceptor
RT gene.";
RL Am. J. Hypertens. 8:177-182(1995).
CC -!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-
CC induced inhibition of adenylate cyclase through the action of G
CC proteins.
CC -!- SUBUNIT: Interacts with RAB26. Interacts with PPP1R9B. Interacts with
CC GGA1, GGA2 and GGA3. {ECO:0000250|UniProtKB:P18089}.
CC -!- INTERACTION:
CC P19328; Q9UJY5: GGA1; Xeno; NbExp=3; IntAct=EBI-21453893, EBI-447141;
CC P19328; Q9UJY4: GGA2; Xeno; NbExp=3; IntAct=EBI-21453893, EBI-447646;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18089};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P18089}.
CC Note=Interaction with RAB26, GGA1, GGA2 and GGA3 mediates transport
CC from the Golgi to the cell membrane. {ECO:0000250|UniProtKB:P18089}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Adrenergic receptor subfamily. ADRA2B sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M32061; AAA40635.1; -; mRNA.
DR EMBL; AF366899; AAK53388.1; -; Genomic_DNA.
DR EMBL; X74400; CAA52411.1; -; Genomic_DNA.
DR PIR; A35642; A35642.
DR PIR; I51883; I51883.
DR RefSeq; NP_612514.2; NM_138505.2.
DR AlphaFoldDB; P19328; -.
DR SMR; P19328; -.
DR IntAct; P19328; 2.
DR STRING; 10116.ENSRNOP00000018584; -.
DR BindingDB; P19328; -.
DR ChEMBL; CHEMBL266; -.
DR DrugCentral; P19328; -.
DR GuidetoPHARMACOLOGY; 26; -.
DR PhosphoSitePlus; P19328; -.
DR PaxDb; P19328; -.
DR Ensembl; ENSRNOT00000018584; ENSRNOP00000018584; ENSRNOG00000013887.
DR GeneID; 24174; -.
DR KEGG; rno:24174; -.
DR UCSC; RGD:2057; rat.
DR CTD; 151; -.
DR RGD; 2057; Adra2b.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000161915; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; P19328; -.
DR OMA; CEPQAVP; -.
DR OrthoDB; 737211at2759; -.
DR PhylomeDB; P19328; -.
DR TreeFam; TF316350; -.
DR Reactome; R-RNO-390696; Adrenoceptors.
DR Reactome; R-RNO-392023; Adrenaline signalling through Alpha-2 adrenergic receptor.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-418597; G alpha (z) signalling events.
DR PRO; PR:P19328; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000013887; Expressed in adult mammalian kidney and 7 other tissues.
DR Genevisible; P19328; RN.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR GO; GO:0004935; F:adrenergic receptor activity; ISO:RGD.
DR GO; GO:0004938; F:alpha2-adrenergic receptor activity; IDA:RGD.
DR GO; GO:0051379; F:epinephrine binding; ISO:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISO:RGD.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0071875; P:adrenergic receptor signaling pathway; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IMP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0000165; P:MAPK cascade; ISO:RGD.
DR GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR GO; GO:0045777; P:positive regulation of blood pressure; IMP:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0070474; P:positive regulation of uterine smooth muscle contraction; IMP:RGD.
DR GO; GO:0035624; P:receptor transactivation; ISO:RGD.
DR GO; GO:0003056; P:regulation of vascular associated smooth muscle contraction; IMP:RGD.
DR InterPro; IPR002233; ADR_fam.
DR InterPro; IPR000207; ADRA2B_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
DR PRINTS; PR00559; ADRENRGCA2BR.
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 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..453
FT /note="Alpha-2B adrenergic receptor"
FT /id="PRO_0000069100"
FT TOPO_DOM 1..17
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 18..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 43..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 55..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 81..90
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 91..113
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 114..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 136..158
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 159..174
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 175..198
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 199..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 376..399
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 400..408
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 409..432
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 433..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 213..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..314
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 97
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250"
FT SITE 181
FT /note="Implicated in catechol agonist binding"
FT /evidence="ECO:0000250"
FT SITE 185
FT /note="Implicated in catechol agonist binding"
FT /evidence="ECO:0000250"
FT LIPID 445
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT DISULFID 90..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 132
FT /note="R -> C (in Ref. 1; AAA40635)"
FT /evidence="ECO:0000305"
FT CONFLICT 162..163
FT /note="EP -> DA (in Ref. 1; AAA40635)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 50369 MW; CBA69CE23EACB511 CRC64;
MSGPTMDHQE PYSVQATAAI ASAITFLILF TIFGNALVIL AVLTSRSLRA PQNLFLVSLA
AADILVATLI IPFSLANELL GYWYFWRAWC EVYLALDVLF CTSSIVHLCA ISLDRYWAVS
RALEYNSKRT PRRIKCIILT VWLIAAVISL PPLIYKGDQR PEPRGLPQCE LNQEAWYILA
SSIGSFFAPC LIMILVYLRI YVIAKRSHCR GLGAKRGSGE GESKKPQPVA GGVPTSAKVP
TLVSPLSSVG EANGHPKPPR EKEEGETPED PEARALPPTW SALPRSGQGQ KKGTSGATAE
EGDEEDEEEV EECEPQTLPA SPASVCNPPL QQPQTSRVLA TLRGQVLLGK NVGVASGQWW
RRRTQLSREK RFTFVLAVVI GVFVVCWFPF FFSYSLGAIC PQHCKVPHGL FQFFFWIGYC
NSSLNPVIYT VFNQDFRRAF RRILCRPWTQ TGW
