ID ADA2A_CAVPO Reviewed; 464 AA.
AC Q60474;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2019, sequence version 2.
DT 22-FEB-2023, entry version 118.
DE RecName: Full=Alpha-2A adrenergic receptor {ECO:0000250|UniProtKB:P08913};
DE AltName: Full=Alpha-2A adrenoreceptor;
DE Short=Alpha-2A adrenoceptor;
DE Short=Alpha-2AAR;
GN Name=ADRA2A {ECO:0000250|UniProtKB:P08913};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hartley;
RX PubMed=8573196; DOI=10.1016/0006-2952(95)02179-5;
RA Svensson S.P., Bailey T.J., Porter A.C., Richman J.G., Regan J.W.;
RT "Heterologous expression of the cloned guinea pig alpha 2A, alpha 2B, and
RT alpha 2C adrenoceptor subtypes. Radioligand binding and functional coupling
RT to a cAMP-responsive reporter gene.";
RL Biochem. Pharmacol. 51:291-300(1996).
CC -!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-
CC induced inhibition of adenylate cyclase through the action of G
CC proteins. Component of the ATAC complex, a complex with histone
CC acetyltransferase activity on histones H3 and H4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the ADA2A-containing complex (ATAC), composed of
CC KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Adrenergic receptor subfamily. ADRA2A sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-15 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA67074.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U25722; AAA67074.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_001166317.1; NM_001172846.1.
DR AlphaFoldDB; Q60474; -.
DR SMR; Q60474; -.
DR STRING; 10141.ENSCPOP00000018153; -.
DR BindingDB; Q60474; -.
DR GlyCosmos; Q60474; 2 sites, No reported glycans.
DR GeneID; 100135475; -.
DR KEGG; cpoc:100135475; -.
DR CTD; 150; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q60474; -.
DR OrthoDB; 3087922at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004938; F:alpha2-adrenergic receptor activity; IEA:InterPro.
DR GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:InterPro.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR CDD; cd15322; 7tmA_alpha2A_AR; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR002233; ADR_fam.
DR InterPro; IPR001946; ADRA2A_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR24248:SF24; ALPHA-2A ADRENERGIC RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
DR PRINTS; PR00558; ADRENRGCA2AR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Methylation; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..464
FT /note="Alpha-2A adrenergic receptor"
FT /id="PRO_0000069079"
FT TOPO_DOM 1..47
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 48..73
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 74..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 85..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 111..120
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 121..143
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 144..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 164..187
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 188..206
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 207..231
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 232..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 389..413
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 414..423
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 424..444
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 445..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 13..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 127
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250"
FT SITE 213
FT /note="Implicated in agonist binding and receptor
FT activation"
FT /evidence="ECO:0000250"
FT SITE 217
FT /note="Implicated in agonist binding and receptor
FT activation"
FT /evidence="ECO:0000250"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22909"
FT MOD_RES 367
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01338"
FT LIPID 456
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 464 AA; 50851 MW; C48AF9AD7297A183 CRC64;
MFRQEQRWPR QLWPMGSLQP DSGNASWNGT EGPGGGTRAT PYSLQVTVTL VCLVGLLILL
TVFGNVLVII AVFTSRALKA PQNLFLVSLA SADILVATLV IPFSLANEVM GYWYFGKAWC
EIYLALDVLF CTSSIVHLCA ISLDRYWSIT QAIEYNLKRT PRRIKAIIVT VWVISAVISF
PPLISFEKAG GGGQQPAEPR CEINDQKWYV ISSSIGSFFA PCLIMILVYV RIYQIAKRRT
RVPPSRRGPD AHAAAPPGGA ERRPNGLGLE RGVGPGGAEA EPLPTQVNGA PGEPAPAGPR
DAEALDLEES SSSEHAERPP GARRPERGLR AKSKARASQV KPGDSLPRRA PGAAGSGTSG
SGPGEERGGG AKASRWRGRQ NREKRFTFVL AVVIGVFVVC WFPFFFTYTL TAVGCSVPRT
LFKFFFWFGY CNSSLNPVIY TIFNHDFRRA FKKILCRGDR KRIV
//
