ID   AA1R_PONAB              Reviewed;         326 AA.
AC   Q5RF57;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Adenosine receptor A1;
GN   Name=ADORA1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for adenosine. The activity of this receptor is
CC       mediated by G proteins which inhibit adenylyl cyclase (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; CR857304; CAH89600.1; -; mRNA.
DR   RefSeq; NP_001124711.1; NM_001131239.1.
DR   AlphaFoldDB; Q5RF57; -.
DR   SMR; Q5RF57; -.
DR   STRING; 9601.ENSPPYP00000000373; -.
DR   GeneID; 100171559; -.
DR   KEGG; pon:100171559; -.
DR   CTD; 134; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; Q5RF57; -.
DR   OrthoDB; 550297at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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:0001609; F:G protein-coupled adenosine receptor activity; IEA:InterPro.
DR   InterPro; IPR001068; Adeno_A1_rcpt.
DR   InterPro; IPR001634; Adenosn_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00552; ADENOSINEA1R.
DR   PRINTS; PR00424; ADENOSINER.
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   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..326
FT                   /note="Adenosine receptor A1"
FT                   /id="PRO_0000269716"
FT   TOPO_DOM        1..10
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..33
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..46
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..69
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        70..80
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..102
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..123
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..146
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..176
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..201
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..259
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        260..267
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..292
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        293..326
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           309
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        80..169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   326 AA;  36545 MW;  5CB621A8CDCCA5FC CRC64;
     MPPSISAFQA AYIGIEVLIA LVSVPGNVLV IWAVKVNQAL RDATFCFIVL LAVADVAVGA
     LVIPLAILIN IGPQTYFHTC LMVACPVLIL TQSSILALLT IAVDRYLRVK IPLRYKMVVT
     PRRAAVAIAG CWILSFVVGL TPMFGWNNLS AVERAWAANG SMGEPVIKCE FEKVISMEYM
     VYFNFFVWVL PPLLLMVLIY LEVFYLIRKQ LNKKVSASSG DPQKYYGKEL KIAKSLALIL
     FLFALSWLPL HILNCITLFC PSCHKPSILT YIAIFLTHGN SAMNPIVYAF RIQKFRVTFL
     KIWNDNFRCQ PAPPIDEDLP EERPDD