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Database: UniProt/TrEMBL
Entry: L5KWL9_PTEAL
LinkDB: L5KWL9_PTEAL
Original site: L5KWL9_PTEAL 
ID   L5KWL9_PTEAL            Unreviewed;       326 AA.
AC   L5KWL9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Adenosine receptor A1 {ECO:0000256|ARBA:ARBA00021736, ECO:0000256|RuleBase:RU201114};
GN   ORFNames=PAL_GLEAN10000796 {ECO:0000313|EMBL:ELK15849.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK15849.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- FUNCTION: Receptor for adenosine. The activity of this receptor is
CC       mediated by G proteins which inhibit adenylyl cyclase.
CC       {ECO:0000256|ARBA:ARBA00025048, ECO:0000256|RuleBase:RU201114}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC       ECO:0000256|RuleBase:RU201114}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU201114}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000256|RuleBase:RU201114}.
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DR   EMBL; KB030502; ELK15849.1; -; Genomic_DNA.
DR   RefSeq; XP_006908369.1; XM_006908307.1.
DR   AlphaFoldDB; L5KWL9; -.
DR   STRING; 9402.L5KWL9; -.
DR   GeneID; 102881697; -.
DR   KEGG; pale:102881697; -.
DR   CTD; 134; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; L5KWL9; -.
DR   OrthoDB; 2909020at2759; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
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   CDD; cd15071; 7tmA_Adenosine_R_A1; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR001068; Adeno_A1_rcpt.
DR   InterPro; IPR001634; Adenosn_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24246:SF1; ADENOSINE RECEPTOR A1; 1.
DR   PANTHER; PTHR24246; OLFACTORY RECEPTOR AND ADENOSINE RECEPTOR; 1.
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   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 {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU201114};
KW   Disulfide bond {ECO:0000256|RuleBase:RU201114};
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW   ECO:0000256|RuleBase:RU201114};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW   ECO:0000256|RuleBase:RU201114};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU201114};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU201114};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU201114};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU201114};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   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        236..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU201114"
FT   TRANSMEM        271..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU201114"
FT   DOMAIN          26..288
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
SQ   SEQUENCE   326 AA;  36101 MW;  8F8A9D0E606092DE CRC64;
     MPPTVTAFQA AYIGIEVLIA LVSVPGNVLV IWAVKVNPAL RDATFCFIVS LAVADVAVGA
     LVIPLAILIN IGPQTYFHTC LMVACPVLIL TQSSILALLA IAVDRYLRVK IPLRYKTVVT
     PRRAAAAIAG CWALSFVVGL TPMFGWNNLR EVERAWAANG SVGEPVIHCE FEKVISMEYM
     VYFNFFAWVL PPLLLMALVY LEVFYLIRKQ LSKKASASSG DPHKYYGKEL GIAKSLALVL
     LLFALSWLPL HILNCVTLFC PACRKPSTLT YVAIFLTHGN SAMNPIVYAF RIQKFRATFL
     KIFNDHFRCR LAPPAEEGPP EERPDD
//
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