Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9823-00796
Entry Name
UniProt Accession
Theoretical PI
9.8
Molecular Weight
48975.86
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Alpha-2A adrenergic receptor
Protein Synonyms/Alias
Alpha-2A adrenoreceptor; Alpha-2A adrenoceptor; Alpha-2AAR;
Gene Name
ADRA2A
Gene Synonyms/Alias
A2AR;
Created Date
01-NOV-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
442
Canonical
RAFKKILCRGDRKRI
[1]
S-Palmitoylation
Organism
Sus scrofa (Pig)
NCBI Taxa ID
9823
Reference
[1] Kennedy ME, Limbird LE. Mutations of the alpha 2A-adrenergic receptor thateliminate detectable palmitoylation do not perturb receptor-G-protein coupling. JBiol Chem. 1993 Apr 15;268(11):8003-11.[PMID:8385131]
Functional Description
Alpha-2 adrenergic receptors mediate the catecholamine- induced inhibition of adenylate cyclase through the action of G proteins.
Sequence Annotation
Topological domain: 1 33 Extracellular.
Transmembrane: 34 59 Helical; Name=1.
Topological domain: 60 70 Cytoplasmic.
Transmembrane: 71 96 Helical; Name=2.
Topological domain: 97 106 Extracellular.
Transmembrane: 107 129 Helical; Name=3.
Topological domain: 130 149 Cytoplasmic.
Transmembrane: 150 173 Helical; Name=4.
Topological domain: 174 192 Extracellular.
Transmembrane: 193 217 Helical; Name=5.
Topological domain: 218 374 Cytoplasmic.
Transmembrane: 375 399 Helical; Name=6.
Topological domain: 400 409 Extracellular.
Transmembrane: 410 430 Helical; Name=7.
Topological domain: 431 450 Cytoplasmic.
Functional site: 113 113 Implicated in ligand binding.
Functional site: 200 200 Implicated in catechol agonist binding.
Functional site: 204 204 Implicated in catechol agonist binding.
Protein Length
450 AA.
Protein Sequence
(Canonical)
MGSLQPEAGN ASWNGTEAPG GGARATPYSL QVTLTLVCLA GLLMLFTVFG NVLVIIAVFT  60
SRALKAPQNL FLVSLASADI LVATLVIPFS LANEVMGYWY FGKAWCEIYL ALDVLFCTSS  120
IVHLCAISLD RYWSITQAIE YNLKRTPRRI KAIIVTVWVI SAVISFPPLI SIEKKAGGGG  180
QQPAEPRCEI NDQKWYVISS CIGSFFAPCL IMILVYVRIY QIAKRRTRVP PSRRGPDAAA  240
ALPGGAERRP NGLGPERGVG RVGAEAEPLP VQLNGAPGEP APAGPRDADG LDLEESSSSE  300
HAERPPGPRR SERGPRAKSK ARASQVKPGD SLPRRGPGAP GPGAPATGAG EERGGVAKAS  360
RWRGRQNREK RFTFVLAVVI GVFVVCWFPF FFTYTLTAVG CSVPPTLFKF FFWFGYCNSS  420
LNPVIYTIFN HDFRRAFKKI LCRGDRKRIV                                   450
FASTA
(Canonical)
>LipidDB-9823-00796|P18871
MGSLQPEAGNASWNGTEAPGGGARATPYSLQVTLTLVCLAGLLMLFTVFGNVLVIIAVFT
SRALKAPQNLFLVSLASADILVATLVIPFSLANEVMGYWYFGKAWCEIYLALDVLFCTSS
IVHLCAISLDRYWSITQAIEYNLKRTPRRIKAIIVTVWVISAVISFPPLISIEKKAGGGG
QQPAEPRCEINDQKWYVISSCIGSFFAPCLIMILVYVRIYQIAKRRTRVPPSRRGPDAAA
ALPGGAERRPNGLGPERGVGRVGAEAEPLPVQLNGAPGEPAPAGPRDADGLDLEESSSSE
HAERPPGPRRSERGPRAKSKARASQVKPGDSLPRRGPGAPGPGAPATGAGEERGGVAKAS
RWRGRQNREKRFTFVLAVVIGVFVVCWFPFFFTYTLTAVGCSVPPTLFKFFFWFGYCNSS
LNPVIYTIFNHDFRRAFKKILCRGDRKRIV
Gene Ontology
GO:0005737; C:cytoplasm; IEA:Ensembl
GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL
GO:0043235; C:receptor complex; IEA:Ensembl
GO:0031692; F:alpha-1B adrenergic receptor binding; IPI:BHF-UCL
GO:0004938; F:alpha2-adrenergic receptor activity; IDA:BHF-UCL
GO:0051379; F:epinephrine binding; IDA:BHF-UCL
GO:0051380; F:norepinephrine binding; IEA:Ensembl
GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL
GO:0071883; P:activation of MAPK activity by adrenergic receptor signaling pathway; IEA:Ensembl
GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl
GO:0071881; P:adenylate cyclase-inhibiting adrenergic receptor signaling pathway; IEA:Ensembl
GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl
GO:0035625; P:epidermal growth factor-activated receptor transactivation by G-protein coupled receptor signaling pathway; IEA:Ensembl
GO:0042596; P:fear response; IEA:Ensembl
GO:0042593; P:glucose homeostasis; IEA:Ensembl
GO:0007194; P:negative regulation of adenylate cyclase activity; IDA:BHF-UCL
GO:0071878; P:negative regulation of adrenergic receptor signaling pathway; IDA:BHF-UCL
GO:1901020; P:negative regulation of calcium ion transmembrane transporter activity; IDA:BHF-UCL
GO:0051926; P:negative regulation of calcium ion transport; IDA:BHF-UCL
GO:0030818; P:negative regulation of cAMP biosynthetic process; IDA:BHF-UCL
GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl
GO:0050995; P:negative regulation of lipid catabolic process; IEA:Ensembl
GO:0071882; P:phospholipase C-activating adrenergic receptor signaling pathway; IEA:Ensembl
GO:0030168; P:platelet activation; IEA:InterPro
GO:0030335; P:positive regulation of cell migration; IEA:Ensembl
GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl
GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IEA:Ensembl
GO:0043268; P:positive regulation of potassium ion transport; IDA:BHF-UCL
GO:0090303; P:positive regulation of wound healing; IEA:Ensembl
GO:0006940; P:regulation of smooth muscle contraction; IEA:InterPro
GO:0019229; P:regulation of vasoconstriction; IEA:InterPro
Interpro
InterPro; IPR002233; ADR_fam
InterPro; IPR001946; ADRA2A_rcpt
InterPro; IPR000276; GPCR_Rhodpsn
InterPro; IPR017452; GPCR_Rhodpsn_7TM
Pfam
Pfam; PF00001; 7tm_1;
SMART
PROSITE
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1;
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2;
PRINTS
PRINTS; PR01103; ADRENERGICR;
PRINTS; PR00558; ADRENRGCA2AR;
PRINTS; PR00237; GPCRRHODOPSN;