ID   Q6AXD8_MOUSE            Unreviewed;       326 AA.
AC   Q6AXD8;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   22-APR-2020, entry version 86.
DE   RecName: Full=Adenosine receptor A1 {ECO:0000256|RuleBase:RU201114};
GN   Name=Adora1 {ECO:0000313|EMBL:AAH79624.1, ECO:0000313|MGI:MGI:99401};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH79624.1};
RN   [1] {ECO:0000313|EMBL:AAH79624.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6 {ECO:0000313|EMBL:AAH79624.1};
RC   TISSUE=Brain {ECO:0000313|EMBL:AAH79624.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Receptor for adenosine. The activity of this receptor is
CC       mediated by G proteins which inhibit adenylyl cyclase.
CC       {ECO:0000256|RuleBase:RU201114}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU201114};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU201114}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000256|RuleBase:RU201114}.
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DR   EMBL; BC079624; AAH79624.1; -; mRNA.
DR   RefSeq; NP_001278857.1; NM_001291928.1.
DR   GeneID; 11539; -.
DR   CTD; 134; -.
DR   MGI; MGI:99401; Adora1.
DR   eggNOG; KOG3656; Eukaryota.
DR   eggNOG; ENOG410XRW9; LUCA.
DR   ChiTaRS; Adora1; mouse.
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:UniProtKB-UniRule.
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 {ECO:0000256|RuleBase:RU201114};
KW   Disulfide bond {ECO:0000256|RuleBase:RU201114};
KW   G-protein coupled receptor {ECO:0000256|RuleBase:RU201114};
KW   Glycoprotein {ECO:0000256|RuleBase:RU201114};
KW   Membrane {ECO:0000256|RuleBase:RU201114};
KW   Receptor {ECO:0000256|RuleBase:RU201114};
KW   Transducer {ECO:0000256|RuleBase:RU201114};
KW   Transmembrane {ECO:0000256|RuleBase:RU201114};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU201114}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU201114"
FT   TRANSMEM        45..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU201114"
FT   TRANSMEM        75..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU201114"
FT   TRANSMEM        124..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU201114"
FT   TRANSMEM        185..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU201114"
FT   TRANSMEM        232..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU201114"
FT   TRANSMEM        268..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU201114"
FT   DOMAIN          26..288
FT                   /note="G_PROTEIN_RECEP_F1_2"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
SQ   SEQUENCE   326 AA;  36666 MW;  AB3A01D57483408E CRC64;
     MPPYISAFQA AYIGIEVLIA LVSVPGNVLV IWAVKVNQAL RDATFCFIVS LAVADVAVGA
     LVIPLAILIN IGPQTYFHTC LMVACPVLIL TQSSILVLLA IAVDRYLRVK IPLRYKTVVT
     QRRAAVAIAG CWILSLVVGL TPMFGWNNLS EVEQAWIANG SVGEPVIKCE FEKVISMEYM
     VYFNFFVWVL PPLLLMVLIY LEVFYLIRKQ LNKKVSASSG DPQKYYGKEL KIAKSLALIL
     FLFALSWLPL HILNCITLFC PTCQKPSILI YIAIFLTHGN SAMNPIVYAF RIHKFRVTFL
     KIWNDHFRCQ PKPPIEEDIP EEKADD
//