ADRA1B
entrez
147
canonical
uniprot
P35368
canonical
ensembl
ENSG00000170214
resolver
ensp
ENSP00000306662
resolver
ensp
ENSP00000535073
resolver
enst
ENST00000306675
resolver
enst
ENST00000865014
resolver
genesymbol
ADRA1B
resolver
hgnc
HGNC:278
resolver
uniprot
B0LPE1
resolver
uniprot_entry
ADA1B_HUMAN
resolver
uniprot_sec
B0LPE1
resolver
amino_acid_sequence
MNPDLDTGHNTSAPAHWGELKNANFTGPNQTSSNSTLPQLDITRAISVGLVLGAFILFAIVGNILVILSVACNRHLRTPTNYFIVNLAMADLLLSFTVLPFSAALEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRRKAILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAGVMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLFSTLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFVRILGCQCRGRGRRRRRRRRRLGGCAYTYRPWTRGGSLERSQSRKDSLDDSGSCLSGSQRTLPSASPSPGYLGRGAPPPVELCAFPEWKAPGALLSLPAPEPPGRRGRHDSGPLFTFKLLTEPESPGTDGGASNGGCEAAADVANGQPGFKSNMPLAPGQF
uniprot
proteins
function
FUNCTION: Alpha-1 adrenergic receptors are G protein-coupled receptors for catecholamines that signal through the G(q) family of G proteins, including G(q) and G(11). Upon activation, they stimulate the phosphatidylinositol-calcium second messenger pathway, leading to calcium release from intracellular stores and activation of protein kinase C (By similarity). ADRA1B binds the catecholamine ligands norepinephrine and epinephrine (PubMed:7815325, PubMed:8183249). Can also couple to G(14) and G(16) proteins (By similarity). Nuclear ADRA1B forms heterooligomers with ADRA1A to regulate phenylephrine(PE)-stimulated ERK signaling in cardiac myocytes (PubMed:18802028, PubMed:22120526). At the plasma membrane, ADRA1B interacts with CAVIN4/MURC to regulates ERK activation in cardiomyocytes, contributing to the regulation of cardiac hypertrophy (PubMed:24567387). {ECO:0000250|UniProtKB:P18841, ECO:0000269|PubMed:18802028, ECO:0000269|PubMed:22120526, ECO:0000269|PubMed:24567387, ECO:0000269|PubMed:7815325, ECO:0000269|PubMed:8183249}.
uniprot
proteins
mass_dalton
56836
uniprot
proteins
mutagenesis
MUTAGEN 368..380; /note="RGRGRRRRRRRRR->AGAGAAAAAAAAA: Abolishes targeting to the nuclear membrane of cardiac myocytes."; /evidence="ECO:0000269|PubMed:22120526
uniprot
proteins
protein_family
ADRA1B sub-subfamily
uniprot
proteins
protein_family
Adrenergic receptor subfamily
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
1328250
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18802028
uniprot
proteins
pubmed
22120526
uniprot
proteins
pubmed
24567387
uniprot
proteins
pubmed
7815325
uniprot
proteins
pubmed
8183249
uniprot
proteins
sequence_length
520
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:18802028, ECO:0000269|PubMed:22120526}; Multi-pass membrane protein. Cell membrane {ECO:0000269|PubMed:24567387}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:24567387}. Membrane, caveola {ECO:0000269|PubMed:24567387}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (PubMed:18802028, PubMed:22120526). Colocalizes with CAVIN4 and CAV3 at the plasma membrane and partly within the cytoplasm in cardiomyocytes (PubMed:24567387). {ECO:0000269|PubMed:18802028, ECO:0000269|PubMed:22120526, ECO:0000269|PubMed:24567387}.
uniprot
proteins
transmembrane_region
TRANSMEM 46..70; /note="Helical; Name=1"; /evidence="ECO:0000250"; TRANSMEM 84..105; /note="Helical; Name=2"; /evidence="ECO:0000250"; TRANSMEM 116..141; /note="Helical; Name=3"; /evidence="ECO:0000250"; TRANSMEM 162..184; /note="Helical; Name=4"; /evidence="ECO:0000250"; TRANSMEM 202..224; /note="Helical; Name=5"; /evidence="ECO:0000250"; TRANSMEM 296..319; /note="Helical; Name=6"; /evidence="ECO:0000250"; TRANSMEM 327..351; /note="Helical; Name=7"; /evidence="ECO:0000250
uniprot
proteins