P19328 (ADA2B_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-2B adrenergic receptor

Alternative name(s):
Alpha-2B adrenoreceptor
Short name=Alpha-2B adrenoceptor
Short name=Alpha-2BAR

Gene names

Name:

Adra2b

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA2B sub-subfamily.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Lipoprotein Palmitate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MAPK cascade Inferred from electronic annotation. Source: Compara activation of MAPK activity Inferred from mutant phenotype PubMed 11891218. Source: RGD activation of MAPK activity by adrenergic receptor signaling pathway Inferred from electronic annotation. Source: Compara activation of protein kinase B activity Inferred from electronic annotation. Source: Compara angiogenesis Inferred from electronic annotation. Source: Compara epidermal growth factor-activated receptor transactivation by G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara female pregnancy Inferred from mutant phenotype PubMed 19450576. Source: RGD positive regulation of blood pressure Inferred from mutant phenotype PubMed 17070424. Source: RGD positive regulation of neuron differentiation Inferred from electronic annotation. Source: Compara positive regulation of uterine smooth muscle contraction Inferred from mutant phenotype PubMed 17664026PubMed 19634638. Source: RGD regulation of vascular smooth muscle contraction Inferred from mutant phenotype PubMed 18054907. Source: RGD
Cellular_component	integral to membrane Traceable author statement PubMed 11891218. Source: RGD plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	alpha2-adrenergic receptor activity Inferred from direct assay Ref.1. Source: RGD epinephrine binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 453	453	Alpha-2B adrenergic receptor		PRO_0000069100
Regions
	Topological domain	1 – 17	17	Extracellular By similarity
	Transmembrane	18 – 42	25	Helical; Name=1; By similarity
	Topological domain	43 – 54	12	Cytoplasmic By similarity
	Transmembrane	55 – 80	26	Helical; Name=2; By similarity
	Topological domain	81 – 90	10	Extracellular By similarity
	Transmembrane	91 – 113	23	Helical; Name=3; By similarity
	Topological domain	114 – 135	22	Cytoplasmic By similarity
	Transmembrane	136 – 158	23	Helical; Name=4; By similarity
	Topological domain	159 – 174	16	Extracellular By similarity
	Transmembrane	175 – 198	24	Helical; Name=5; By similarity
	Topological domain	199 – 375	177	Cytoplasmic By similarity
	Transmembrane	376 – 399	24	Helical; Name=6; By similarity
	Topological domain	400 – 408	9	Extracellular By similarity
	Transmembrane	409 – 432	24	Helical; Name=7; By similarity
	Topological domain	433 – 453	21	Cytoplasmic By similarity
	Compositional bias	300 – 314	15	Asp/Glu-rich (acidic)
Sites
	Site	97	1	Implicated in ligand binding By similarity
	Site	181	1	Implicated in catechol agonist binding By similarity
	Site	185	1	Implicated in catechol agonist binding By similarity
Amino acid modifications
	Lipidation	445	1	S-palmitoyl cysteine Potential
	Disulfide bond	90 ↔ 169		By similarity
Experimental info
	Sequence conflict	132	1	R → C in AAA40635. Ref.1
	Sequence conflict	162 – 163	2	EP → DA in AAA40635. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P19328 [UniParc]. Last modified October 10, 2003. Version 2. Checksum: CBA69CE23EACB511	FASTA	453	50,369
	10 20 30 40 50 60 MSGPTMDHQE PYSVQATAAI ASAITFLILF TIFGNALVIL AVLTSRSLRA PQNLFLVSLA 70 80 90 100 110 120 AADILVATLI IPFSLANELL GYWYFWRAWC EVYLALDVLF CTSSIVHLCA ISLDRYWAVS 130 140 150 160 170 180 RALEYNSKRT PRRIKCIILT VWLIAAVISL PPLIYKGDQR PEPRGLPQCE LNQEAWYILA 190 200 210 220 230 240 SSIGSFFAPC LIMILVYLRI YVIAKRSHCR GLGAKRGSGE GESKKPQPVA GGVPTSAKVP 250 260 270 280 290 300 TLVSPLSSVG EANGHPKPPR EKEEGETPED PEARALPPTW SALPRSGQGQ KKGTSGATAE 310 320 330 340 350 360 EGDEEDEEEV EECEPQTLPA SPASVCNPPL QQPQTSRVLA TLRGQVLLGK NVGVASGQWW 370 380 390 400 410 420 RRRTQLSREK RFTFVLAVVI GVFVVCWFPF FFSYSLGAIC PQHCKVPHGL FQFFFWIGYC 430 440 450 NSSLNPVIYT VFNQDFRRAF RRILCRPWTQ TGW

References

[1]	"Molecular characterization of a rat alpha 2B-adrenergic receptor." Zeng D., Harrison J.K., D'Angelo D.D., Barber C.M., Tucker A.L., Lu Z., Lynch K.R. Proc. Natl. Acad. Sci. U.S.A. 87:3102-3106(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[2]	"Cloning and functional characterization of the rat alpha2B-adrenergic receptor gene promoter region: evidence for binding sites for erythropoiesis-related transcription factors GATA1 and NF-E2." Schaak S., Cussac D., Labialle S., Mignotte V., Paris H. Biochem. Pharmacol. 70:606-617(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: Sprague-Dawley.
[3]	"Differential sodium regulation between salt-sensitive and salt-resistant Sabra rats is not due to any mutation in the renal alpha 2B-adrenoceptor gene." le Jossec M., Cloix J.F., Pecquery R., Giudicelli Y., Dausse J.P. Am. J. Hypertens. 8:177-182(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-453. Strain: Sabra. Tissue: Kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M32061 mRNA. Translation: AAA40635.1. AF366899 Genomic DNA. Translation: AAK53388.1. X74400 Genomic DNA. Translation: CAA52411.1.
IPI	IPI00194252.
PIR	A35642. I51883.
RefSeq	NP_612514.2. NM_138505.2.
UniGene	Rn.10296.
3D structure databases
ProteinModelPortal	P19328.
SMR	P19328. Positions 102-133.
ModBase	Search...
Protein family/group databases
GPCRDB	Search...
Proteomic databases
PaxDb	P19328.
PRIDE	P19328.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000018584; ENSRNOP00000018584; ENSRNOG00000013887.
GeneID	24174.
KEGG	rno:24174.
UCSC	RGD:2057. rat.
Organism-specific databases
CTD	151.
RGD	2057. Adra2b.
Phylogenomic databases
eggNOG	NOG249628.
GeneTree	ENSGT00700000104198.
HOGENOM	HOG000239242.
HOVERGEN	HBG106962.
InParanoid	P19328.
KO	K04139.
OMA	ANGHSEP.
OrthoDB	EOG4R502W.
Gene expression databases
Genevestigator	P19328.
GermOnline	ENSRNOG00000013887. Rattus norvegicus.
Family and domain databases
InterPro	IPR000207. Adren_rcpt_A2B. IPR002233. Adrnrgc_rcpt. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view]
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR01103. ADRENERGICR. PR00559. ADRENRGCA2BR. PR00237. GPCRRHODOPSN.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P19328.
ChEMBL	CHEMBL266.
NextBio	602505.

Entry information

Entry name

ADA2B_RAT

Accession

Primary (citable) accession number: P19328
Secondary accession number(s): Q63021, Q925E4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	October 10, 2003
Last modified:	April 3, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program