ADRA1A
entrez
148
canonical
uniprot
P35348
canonical
ensembl
ENSG00000120907
resolver
ensp
ENSP00000346557
resolver
ensp
ENSP00000369946
resolver
ensp
ENSP00000369947
resolver
ensp
ENSP00000369956
resolver
ensp
ENSP00000369960
resolver
ensp
ENSP00000776634
resolver
ensp
ENSP00000776636
resolver
ensp
ENSP00000776637
resolver
ensp
ENSP00000787635
resolver
genesymbol
ADRA1A
resolver
genesymbol_syn
ADRA1C
resolver
hgnc
HGNC:277
resolver
uniprot
A8K0I3
resolver
uniprot
B0ZBD1
resolver
uniprot
B0ZBD2
resolver
uniprot
B0ZBD4
resolver
uniprot
B0ZBD5
resolver
uniprot
B0ZBD6
resolver
uniprot
B0ZBD8
resolver
uniprot
B0ZBD9
resolver
uniprot
O60451
resolver
uniprot
Q13675
resolver
uniprot
Q13729
resolver
uniprot
Q4VBM7
resolver
uniprot
Q6RUJ4
resolver
uniprot
Q6RUJ5
resolver
uniprot
Q6RUJ7
resolver
uniprot
Q6RUJ8
resolver
uniprot
Q6RUJ9
resolver
uniprot
Q96RE8
resolver
uniprot
Q9UD63
resolver
uniprot
Q9UD67
resolver
uniprot_entry
ADA1A_HUMAN
resolver
uniprot_sec
A8K0I3
resolver
uniprot_sec
B0ZBD1
resolver
uniprot_sec
B0ZBD2
resolver
uniprot_sec
B0ZBD4
resolver
uniprot_sec
B0ZBD5
resolver
uniprot_sec
B0ZBD6
resolver
uniprot_sec
B0ZBD8
resolver
uniprot_sec
B0ZBD9
resolver
uniprot_sec
O60451
resolver
uniprot_sec
Q13675
resolver
uniprot_sec
Q13729
resolver
uniprot_sec
Q4VBM7
resolver
uniprot_sec
Q6RUJ4
resolver
uniprot_sec
Q6RUJ5
resolver
uniprot_sec
Q6RUJ7
resolver
uniprot_sec
Q6RUJ8
resolver
uniprot_sec
Q6RUJ9
resolver
uniprot_sec
Q96RE8
resolver
uniprot_sec
Q9UD63
resolver
uniprot_sec
Q9UD67
resolver
amino_acid_sequence
MVFLSGNASDSSNCTQPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEVLGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGLMALLCVWALSLVISIGPLFGWRQPAPEDETICQINEEPGYVLFSALGSFYLPLAIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGMASAKTKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV
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 (PubMed:37563160). ADRA1A binds the catecholamine ligands norepinephrine and epinephrine (PubMed:18802028, PubMed:37563160, PubMed:7815325, PubMed:8024574, PubMed:8183249, PubMed:8832064). Can also couple to G(14) protein (By similarity). Nuclear ADRA1A forms heterooligomers with ADRA1B to regulate phenylephrine(PE)-stimulated ERK signaling in cardiac myocytes (PubMed:18802028, PubMed:22120526). At the plasma membrane, ADRA1A interacts with CAVIN4/MURC to regulates ERK activation in cardiomyocytes, contributing to the regulation of cardiac hypertrophy (PubMed:24567387). Additionally, functions as a vasopressor in resistance arteries and plays a role in maintaining normal arterial blood pressure (By similarity). {ECO:0000250|UniProtKB:P18130, ECO:0000250|UniProtKB:P97718, ECO:0000269|PubMed:18802028, ECO:0000269|PubMed:22120526, ECO:0000269|PubMed:24567387, ECO:0000269|PubMed:37563160, ECO:0000269|PubMed:7815325, ECO:0000269|PubMed:8024574, ECO:0000269|PubMed:8183249, ECO:0000269|PubMed:8832064}.
uniprot
proteins
mass_dalton
51487
uniprot
proteins
mutagenesis
MUTAGEN 334; /note="K->A: Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-335; A-342; A-348 and A-349."; /evidence="ECO:0000269|PubMed:22120526"; MUTAGEN 335; /note="K->A: Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-342; A-348 and A-349."; /evidence="ECO:0000269|PubMed:22120526"; MUTAGEN 342; /note="R->A: Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-335; A-348 and A-349."; /evidence="ECO:0000269|PubMed:22120526"; MUTAGEN 348; /note="R->A: Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-335; A-342 and A-349."; /evidence="ECO:0000269|PubMed:22120526"; MUTAGEN 349; /note="K->A: Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-335; A-342 and A-348."; /evidence="ECO:0000269|PubMed:22120526
uniprot
proteins
post_translational_modification
PTM: C-terminal Ser or Thr residues may be phosphorylated. {ECO:0000250}.
uniprot
proteins
protein_family
ADRA1A sub-subfamily
uniprot
proteins
protein_family
Adrenergic receptor subfamily
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10493934
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15179408
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
18802028
uniprot
proteins
pubmed
22120526
uniprot
proteins
pubmed
24567387
uniprot
proteins
pubmed
37563160
uniprot
proteins
pubmed
7737411
uniprot
proteins
pubmed
7815325
uniprot
proteins
pubmed
8024574
uniprot
proteins
pubmed
8183249
uniprot
proteins
pubmed
8196478
uniprot
proteins
pubmed
8396931
uniprot
proteins
pubmed
8564208
uniprot
proteins
pubmed
8832064
uniprot
proteins
pubmed
9490024
uniprot
proteins
sequence_length
466
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 (PubMed:18802028, PubMed:22120526). 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 28..51; /note="Helical; Name=1"; /evidence="ECO:0000250"; TRANSMEM 65..88; /note="Helical; Name=2"; /evidence="ECO:0000250"; TRANSMEM 100..122; /note="Helical; Name=3"; /evidence="ECO:0000250"; TRANSMEM 144..167; /note="Helical; Name=4"; /evidence="ECO:0000250"; TRANSMEM 182..205; /note="Helical; Name=5"; /evidence="ECO:0000250"; TRANSMEM 274..297; /note="Helical; Name=6"; /evidence="ECO:0000250"; TRANSMEM 306..329; /note="Helical; Name=7"; /evidence="ECO:0000250
uniprot
proteins