ADRA2A
entrez
150
canonical
uniprot
P08913
canonical
ensembl
ENSG00000150594
resolver
ensp
ENSP00000280155
resolver
enst
ENST00000280155
resolver
genesymbol
ADRA2A
resolver
genesymbol_syn
ADRA2R
resolver
genesymbol_syn
ADRAR
resolver
hgnc
HGNC:281
resolver
uniprot
B0LPF6
resolver
uniprot
Q2I8G2
resolver
uniprot
Q2XN99
resolver
uniprot
Q86TH8
resolver
uniprot
Q9BZK1
resolver
uniprot_entry
ADA2A_HUMAN
resolver
uniprot_sec
B0LPF6
resolver
uniprot_sec
Q2I8G2
resolver
uniprot_sec
Q2XN99
resolver
uniprot_sec
Q86TH8
resolver
uniprot_sec
Q9BZK1
resolver
amino_acid_sequence
MFRQEQPLAEGSFAPMGSLQPDAGNASWNGTEAPGGGARATPYSLQVTLTLVCLAGLLMLLTVFGNVLVIIAVFTSRALKAPQNLFLVSLASADILVATLVIPFSLANEVMGYWYFGKAWCEIYLALDVLFCTSSIVHLCAISLDRYWSITQAIEYNLKRTPRRIKAIIITVWVISAVISFPPLISIEKKGGGGGPQPAEPRCEINDQKWYVISSCIGSFFAPCLIMILVYVRIYQIAKRRTRVPPSRRGPDAVAAPPGGTERRPNGLGPERSAGPGGAEAEPLPTQLNGAPGEPAPAGPRDTDALDLEESSSSDHAERPPGPRRPERGPRGKGKARASQVKPGDSLPRRGPGATGIGTPAAGPGEERVGAAKASRWRGRQNREKRFTFVLAVVIGVFVVCWFPFFFTYTLTAVGCSVPRTLFKFFFWFGYCNSSLNPVIYTIFNHDFRRAFKKILCRGDRKRIV
uniprot
proteins
disease_involvement
DISEASE: Lipodystrophy, familial partial, 8 (FPLD8) [MIM:620679]: An autosomal dominant form of partial lipodystrophy, a disorder characterized by abnormal subcutaneous fat distribution. FPLD8 patients show selective loss of subcutaneous adipose tissue from the limbs, beginning around 13 to 15 years of age, and abnormal accumulation of subcutaneous adipose tissue in the dorsal neck and face, as well as in the posterior thoracic and abdominal regions. The disorder is associated with metabolic abnormalities, including diabetes mellitus and hyperlipidemia. {ECO:0000269|PubMed:27376152}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Alpha-2 adrenergic receptors are G protein-coupled receptors for catecholamines that activate the G(i/o) protein pathway, thereby promoting adenylyl cyclase inhibition, ERK1/2 stimulation, and voltage-gated calcium channels suppression (PubMed:2170371, PubMed:23105096, PubMed:2568356, PubMed:35245122, PubMed:27376152). Control a variety of physiological processes, such as regulation of blood pressure, lipolysis and insulin release (PubMed:2568356, PubMed:27376152). ADRA2A and ADRA2C mediates the presynaptic feedback inhibition of neurotransmitter release from noradrenergic nerve terminals in sympathetic and central nervous systems. ADRA2A inhibits transmitter release at high stimulation frequencies, whereas ADRA2C modulates neurotransmission at lower levels of nerve activity (By similarity). The rank order of potency for agonists of ADRA2A is oxymetazoline > clonidine > epinephrine > norepinephrine > phenylephrine > dopamine > p-synephrine > p-tyramine > serotonin = p-octopamine. For antagonists, the rank order is yohimbine > phentolamine = mianserine > chlorpromazine = spiperone = prazosin > propanolol > alprenolol = pindolol (PubMed:2170371, PubMed:2568356). {ECO:0000250|UniProtKB:Q01338, ECO:0000269|PubMed:2170371, ECO:0000269|PubMed:23105096, ECO:0000269|PubMed:2568356, ECO:0000269|PubMed:27376152, ECO:0000269|PubMed:35245122}.
uniprot
proteins
mass_dalton
50647
uniprot
proteins
mutagenesis
MUTAGEN 94; /note="D->N: No change in binding affinity. Eliminates guanine nucleotide-sensitive agonist binding."; /evidence="ECO:0000269|PubMed:1678850"; MUTAGEN 128; /note="D->A: Loss of receptor activation by norepinephrine."; /evidence="ECO:0000269|PubMed:35245122"; MUTAGEN 128; /note="D->N: No binding to yohimbine. Increase in adenylate cyclase activity."; /evidence="ECO:0000269|PubMed:1678850"; MUTAGEN 145; /note="D->N: Lower affinity for agonists. Eliminates guanine nucleotide-sensitive agonist binding."; /evidence="ECO:0000269|PubMed:1678850"; MUTAGEN 215; /note="S->A: Lower affinity for agonists. No change in guanine nucleotide-sensitive agonist binding. Impaired receptor activation by norepinephrine."; /evidence="ECO:0000269|PubMed:1678850, ECO:0000269|PubMed:35245122"; MUTAGEN 219; /note="S->A: Lower affinity for agonists. Reduced guanine nucleotide-sensitive agonist binding."; /evidence="ECO:0000269|PubMed:1678850"; MUTAGEN 409; /note="Y->A: Impaired receptor activation by norepinephrine."; /evidence="ECO:0000269|PubMed:35245122"; MUTAGEN 427; /note="F->A: Impaired receptor activation by norepinephrine."; /evidence="ECO:0000269|PubMed:35245122"; MUTAGEN 427; /note="F->N: 350-fold reduced affinity for alpha-2 antagonist yohimbine, 3000-fold increase for beta-antagonist alprenolol."; /evidence="ECO:0000269|PubMed:1678390"; MUTAGEN 431; /note="Y->A: Impaired receptor activation by norepinephrine."; /evidence="ECO:0000269|PubMed:35245122
uniprot
proteins
protein_family
ADRA2A sub-subfamily
uniprot
proteins
protein_family
Adrenergic receptor subfamily
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10948191
uniprot
proteins
pubmed
11888275
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16567612
uniprot
proteins
pubmed
1678390
uniprot
proteins
pubmed
1678850
uniprot
proteins
pubmed
1849485
uniprot
proteins
pubmed
2170371
uniprot
proteins
pubmed
23105096
uniprot
proteins
pubmed
2568356
uniprot
proteins
pubmed
27376152
uniprot
proteins
pubmed
2823383
uniprot
proteins
pubmed
35245122
uniprot
proteins
sequence_length
465
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23105096}; Multi-pass membrane protein {ECO:0000269|PubMed:35245122}.
uniprot
proteins
transmembrane_region
TRANSMEM 48..71; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:35245122, ECO:0007744|PDB:7EJ0"; TRANSMEM 86..107; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:35245122, ECO:0007744|PDB:7EJ0"; TRANSMEM 121..144; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:35245122, ECO:0007744|PDB:7EJ0"; TRANSMEM 168..181; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:35245122, ECO:0007744|PDB:7EJ0"; TRANSMEM 209..232; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:35245122, ECO:0007744|PDB:7EJ0"; TRANSMEM 389..413; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:35245122, ECO:0007744|PDB:7EJ0"; TRANSMEM 422..443; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:35245122, ECO:0007744|PDB:7EJ0
uniprot
proteins