Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-00748
Entry Name
UniProt Accession
Theoretical PI
9.7
Molecular Weight
48939.6
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Alpha-2A adrenergic receptor
Protein Synonyms/Alias
Alpha-2A adrenoreceptor; Alpha-2A adrenoceptor; Alpha-2AAR; Alpha-2D adrenergic receptor; CA2-47;
Gene Name
Adra2a
Gene Synonyms/Alias
Created Date
01-AUG-1991
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
442
Canonical
RAFKKILCRGDRKRI
[1]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Barclay E, O'Reilly M, Milligan G. Activation of analpha2A-adrenoceptor-Galphao1 fusion protein dynamically regulates thepalmitoylation status of the G protein but not of the receptor. Biochem J. 2005Jan 1;385(Pt 1):197-206.[PMID:15362975]
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)
MGSLQPDAGN SSWNGTEAPG GGTRATPYSL QVTLTLVCLA GLLMLFTVFG NVLVIIAVFT  60
SRALKAPQNL FLVSLASADI LVATLVIPFS LANEVMGYWY FGKVWCEIYL ALDVLFCTSS  120
IVHLCAISLD RYWSITQAIE YNLKRTPRRI KAIIVTVWVI SAVISFPPLI SIEKKGAGGG  180
QQPAEPSCKI NDQKWYVISS SIGSFFAPCL IMILVYVRIY QIAKRRTRVP PSRRGPDACS  240
APPGGADRRP NGLGPERGAG TAGAEAEPLP TQLNGAPGEP APTRPRDGDA LDLEESSSSE  300
HAERPQGPGK PERGPRAKGK TKASQVKPGD SLPRRGPGAA GPGASGSGQG EERAGGAKAS  360
RWRGRQNREK RFTFVLAVVI GVFVVCWFPF FFTYTLIAVG CPVPYQLFNF FFWFGYCNSS  420
LNPVIYTIFN HDFRRAFKKI LCRGDRKRIV                                   450
FASTA
(Canonical)
>LipidDB-10116-00748|P22909
MGSLQPDAGNSSWNGTEAPGGGTRATPYSLQVTLTLVCLAGLLMLFTVFGNVLVIIAVFT
SRALKAPQNLFLVSLASADILVATLVIPFSLANEVMGYWYFGKVWCEIYLALDVLFCTSS
IVHLCAISLDRYWSITQAIEYNLKRTPRRIKAIIVTVWVISAVISFPPLISIEKKGAGGG
QQPAEPSCKINDQKWYVISSSIGSFFAPCLIMILVYVRIYQIAKRRTRVPPSRRGPDACS
APPGGADRRPNGLGPERGAGTAGAEAEPLPTQLNGAPGEPAPTRPRDGDALDLEESSSSE
HAERPQGPGKPERGPRAKGKTKASQVKPGDSLPRRGPGAAGPGASGSGQGEERAGGAKAS
RWRGRQNREKRFTFVLAVVIGVFVVCWFPFFFTYTLIAVGCPVPYQLFNFFFWFGYCNSS
LNPVIYTIFNHDFRRAFKKILCRGDRKRIV
Gene Ontology
GO:0005737; C:cytoplasm; IDA:RGD
GO:0005887; C:integral component of plasma membrane; IEA:Ensembl
GO:0005886; C:plasma membrane; IDA:RGD
GO:0043235; C:receptor complex; IEA:Ensembl
GO:0045202; C:synapse; IDA:RGD
GO:0004938; F:alpha2-adrenergic receptor activity; IDA:RGD
GO:0051379; F:epinephrine binding; IEA:Ensembl
GO:0051380; F:norepinephrine binding; IEA:Ensembl
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:0002526; P:acute inflammatory response; IMP:RGD
GO:0071881; P:adenylate cyclase-inhibiting adrenergic receptor signaling pathway; IEA:Ensembl
GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl
GO:0006260; P:DNA replication; IMP:RGD
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:0007565; P:female pregnancy; IMP:RGD
GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:BHF-UCL
GO:0042593; P:glucose homeostasis; IMP:BHF-UCL
GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IMP:BHF-UCL
GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:BHF-UCL
GO:0050995; P:negative regulation of lipid catabolic process; IEA:Ensembl
GO:0070473; P:negative regulation of uterine smooth muscle contraction; IMP:RGD
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:0045909; P:positive regulation of vasodilation; IMP:RGD
GO:0090303; P:positive regulation of wound healing; IEA:Ensembl
GO:0019229; P:regulation of vasoconstriction; IEA:InterPro
GO:0007165; P:signal transduction; IEP:RGD
GO:0050955; P:thermoception; IDA:RGD
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;