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ADA2A_CAVPO
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   03-AUG-2022, entry version 116.
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   GeneID; 100135475; -.
DR   KEGG; cpoc:100135475; -.
DR   CTD; 150; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; Q60474; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   InterPro; IPR002233; ADR_fam.
DR   InterPro; IPR001946; ADRA2A_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
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   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
 
 
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