AA1R_HUMAN
ID AA1R_HUMAN Reviewed; 326 AA.
AC P30542; A6NFY5; A6NGP4; A8K1L3; B3KXQ4; D2CGD0; Q6FHK3; Q8TAM8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Adenosine receptor A1;
GN Name=ADORA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
RX PubMed=1530647; DOI=10.1016/0006-291x(92)91285-x;
RA Libert F., van Sande J., Lefort A., Czernilofsky A., Dumont J.E.,
RA Vassart G., Ensinger H.A., Mendla K.D.;
RT "Cloning and functional characterization of a human A1 adenosine
RT receptor.";
RL Biochem. Biophys. Res. Commun. 187:919-926(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=1339301; DOI=10.1016/0169-328x(92)90248-a;
RA Townsend-Nicholson A., Shine J.;
RT "Molecular cloning and characterisation of a human brain A1 adenosine
RT receptor cDNA.";
RL Brain Res. Mol. Brain Res. 16:365-370(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
RX PubMed=8300646; DOI=10.1016/s0021-9258(17)42054-0;
RA Ren H., Stiles G.L.;
RT "Characterization of the human A1 adenosine receptor gene. Evidence for
RT alternative splicing.";
RL J. Biol. Chem. 269:3104-3110(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Salvatore C.A., Luneau C.J., Johnson R.G., Jacobson M.;
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RA Hirabatake Y., Takao K., Hagiwara S., Kasanuki H., Hosoda S., Kokubun S.;
RT "Complete nucleotide sequence of an adenosine A1-receptor from heart.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Feng Y.-H., Cheng H., Qiu R.;
RT "Identification of a 3TM adenosine receptor subtype 1 variant.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-43;
RP PRO-50; HIS-105 AND GLN-261.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-170.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [15]
RP VARIANT SER-279, CHARACTERIZATION OF VARIANT SER-279, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27134041; DOI=10.1002/mds.26627;
RA Jaberi E., Rohani M., Shahidi G.A., Nafissi S., Arefian E., Soleimani M.,
RA Moghadam A., Arzenani M.K., Keramatian F., Klotzle B., Fan J.B., Turk C.,
RA Steemers F., Elahi E.;
RT "Mutation in ADORA1 identified as likely cause of early-onset parkinsonism
RT and cognitive dysfunction.";
RL Mov. Disord. 31:1004-1011(2016).
CC -!- FUNCTION: Receptor for adenosine. The activity of this receptor is
CC mediated by G proteins which inhibit adenylyl cyclase.
CC -!- INTERACTION:
CC P30542; P29274: ADORA2A; NbExp=4; IntAct=EBI-2903663, EBI-2902702;
CC P30542; P08588: ADRB1; NbExp=5; IntAct=EBI-2903663, EBI-991009;
CC P30542; P07550: ADRB2; NbExp=5; IntAct=EBI-2903663, EBI-491169;
CC P30542; P16473: TSHR; NbExp=2; IntAct=EBI-2903663, EBI-13939599;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27134041};
CC Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P30542-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30542-2; Sequence=VSP_034401, VSP_034402;
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S45235; AAB23388.1; -; mRNA.
DR EMBL; S56143; AAB25533.2; -; mRNA.
DR EMBL; L22214; AAA17544.1; -; mRNA.
DR EMBL; X68485; CAA48503.1; -; mRNA.
DR EMBL; AB004662; BAA20433.1; -; mRNA.
DR EMBL; EF057066; ABO25743.1; -; mRNA.
DR EMBL; AK127752; BAG54566.1; -; mRNA.
DR EMBL; AK289928; BAF82617.1; -; mRNA.
DR EMBL; AY136746; AAN01272.1; -; mRNA.
DR EMBL; BT019854; AAV38657.1; -; mRNA.
DR EMBL; CR541749; CAG46549.1; -; mRNA.
DR EMBL; AC105940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91465.1; -; Genomic_DNA.
DR EMBL; BC026340; AAH26340.1; -; mRNA.
DR CCDS; CCDS1434.1; -. [P30542-1]
DR PIR; A53005; A53005.
DR RefSeq; NP_000665.1; NM_000674.2. [P30542-1]
DR RefSeq; NP_001041695.1; NM_001048230.1. [P30542-1]
DR PDB; 5N2S; X-ray; 3.30 A; A=4-316.
DR PDB; 5UEN; X-ray; 3.20 A; A/B=2-211, A/B=228-311.
DR PDB; 6D9H; EM; 3.60 A; R=2-326.
DR PDB; 7LD3; EM; 3.20 A; R=2-326.
DR PDB; 7LD4; EM; 3.30 A; R=2-326.
DR PDBsum; 5N2S; -.
DR PDBsum; 5UEN; -.
DR PDBsum; 6D9H; -.
DR PDBsum; 7LD3; -.
DR PDBsum; 7LD4; -.
DR AlphaFoldDB; P30542; -.
DR SMR; P30542; -.
DR BioGRID; 106646; 17.
DR IntAct; P30542; 6.
DR MINT; P30542; -.
DR STRING; 9606.ENSP00000356205; -.
DR BindingDB; P30542; -.
DR ChEMBL; CHEMBL226; -.
DR DrugBank; DB00640; Adenosine.
DR DrugBank; DB01223; Aminophylline.
DR DrugBank; DB00201; Caffeine.
DR DrugBank; DB09061; Cannabidiol.
DR DrugBank; DB04932; Defibrotide.
DR DrugBank; DB00651; Dyphylline.
DR DrugBank; DB00824; Enprofylline.
DR DrugBank; DB00996; Gabapentin.
DR DrugBank; DB11757; Istradefylline.
DR DrugBank; DB00555; Lamotrigine.
DR DrugBank; DB06471; Naxifylline.
DR DrugBank; DB01303; Oxtriphylline.
DR DrugBank; DB00806; Pentoxifylline.
DR DrugBank; DB12670; Rolofylline.
DR DrugBank; DB04954; Tecadenoson.
DR DrugBank; DB01412; Theobromine.
DR DrugBank; DB00277; Theophylline.
DR DrugBank; DB12569; Tonapofylline.
DR DrugBank; DB00193; Tramadol.
DR DrugCentral; P30542; -.
DR GuidetoPHARMACOLOGY; 18; -.
DR TCDB; 9.A.14.3.4; the g-protein-coupled receptor (gpcr) family.
DR GlyConnect; 992; 6 N-Linked glycans (1 site).
DR GlyGen; P30542; 1 site, 6 N-linked glycans (1 site).
DR iPTMnet; P30542; -.
DR PhosphoSitePlus; P30542; -.
DR SwissPalm; P30542; -.
DR BioMuta; ADORA1; -.
DR DMDM; 231473; -.
DR jPOST; P30542; -.
DR MassIVE; P30542; -.
DR PaxDb; P30542; -.
DR PeptideAtlas; P30542; -.
DR PRIDE; P30542; -.
DR ProteomicsDB; 54718; -. [P30542-1]
DR Antibodypedia; 20660; 519 antibodies from 36 providers.
DR DNASU; 134; -.
DR Ensembl; ENST00000309502.7; ENSP00000308549.3; ENSG00000163485.17. [P30542-1]
DR Ensembl; ENST00000337894.9; ENSP00000338435.4; ENSG00000163485.17. [P30542-1]
DR Ensembl; ENST00000367235.1; ENSP00000356204.1; ENSG00000163485.17. [P30542-2]
DR Ensembl; ENST00000367236.8; ENSP00000356205.4; ENSG00000163485.17. [P30542-1]
DR Ensembl; ENST00000640524.1; ENSP00000491900.1; ENSG00000163485.17. [P30542-2]
DR GeneID; 134; -.
DR KEGG; hsa:134; -.
DR MANE-Select; ENST00000337894.9; ENSP00000338435.4; NM_000674.3; NP_000665.1.
DR UCSC; uc001gze.1; human. [P30542-1]
DR CTD; 134; -.
DR DisGeNET; 134; -.
DR GeneCards; ADORA1; -.
DR HGNC; HGNC:262; ADORA1.
DR HPA; ENSG00000163485; Tissue enhanced (brain, testis).
DR MIM; 102775; gene.
DR neXtProt; NX_P30542; -.
DR OpenTargets; ENSG00000163485; -.
DR PharmGKB; PA24583; -.
DR VEuPathDB; HostDB:ENSG00000163485; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234555; -.
DR HOGENOM; CLU_009579_11_5_1; -.
DR InParanoid; P30542; -.
DR OMA; IWAVKMN; -.
DR OrthoDB; 550297at2759; -.
DR PhylomeDB; P30542; -.
DR TreeFam; TF325296; -.
DR PathwayCommons; P30542; -.
DR Reactome; R-HSA-417973; Adenosine P1 receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P30542; -.
DR SIGNOR; P30542; -.
DR BioGRID-ORCS; 134; 12 hits in 1069 CRISPR screens.
DR ChiTaRS; ADORA1; human.
DR GeneWiki; Adenosine_A1_receptor; -.
DR GenomeRNAi; 134; -.
DR Pharos; P30542; Tclin.
DR PRO; PR:P30542; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P30542; protein.
DR Bgee; ENSG00000163485; Expressed in inferior vagus X ganglion and 178 other tissues.
DR ExpressionAtlas; P30542; baseline and differential.
DR Genevisible; P30542; HS.
DR GO; GO:0030673; C:axolemma; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
DR GO; GO:0001609; F:G protein-coupled adenosine receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:Ensembl.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:Ensembl.
DR GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR GO; GO:0032795; F:heterotrimeric G-protein binding; IEA:Ensembl.
DR GO; GO:0099582; F:neurotransmitter receptor activity involved in regulation of presynaptic cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0001883; F:purine nucleoside binding; IEA:Ensembl.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:ProtInc.
DR GO; GO:0110148; P:biomineralization; IDA:MGI.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0050890; P:cognition; IEA:Ensembl.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IEA:Ensembl.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0050900; P:leukocyte migration; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IEA:Ensembl.
DR GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl.
DR GO; GO:0070254; P:mucus secretion; IEA:Ensembl.
DR GO; GO:0002674; P:negative regulation of acute inflammatory response; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0042323; P:negative regulation of circadian sleep/wake cycle, non-REM sleep; IEA:Ensembl.
DR GO; GO:0014050; P:negative regulation of glutamate secretion; IEA:Ensembl.
DR GO; GO:0045822; P:negative regulation of heart contraction; IEA:Ensembl.
DR GO; GO:0046888; P:negative regulation of hormone secretion; IEA:Ensembl.
DR GO; GO:0002686; P:negative regulation of leukocyte migration; IEA:Ensembl.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IEA:Ensembl.
DR GO; GO:1900453; P:negative regulation of long-term synaptic depression; IEA:Ensembl.
DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0070256; P:negative regulation of mucus secretion; IEA:Ensembl.
DR GO; GO:0032900; P:negative regulation of neurotrophin production; IEA:Ensembl.
DR GO; GO:0035814; P:negative regulation of renal sodium excretion; IEA:Ensembl.
DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IEA:Ensembl.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0006909; P:phagocytosis; TAS:ProtInc.
DR GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; IEA:Ensembl.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
DR GO; GO:0032244; P:positive regulation of nucleoside transport; IEA:Ensembl.
DR GO; GO:0002793; P:positive regulation of peptide secretion; IEA:Ensembl.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; IEA:Ensembl.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IEA:Ensembl.
DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:0006612; P:protein targeting to membrane; IEA:Ensembl.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IEA:Ensembl.
DR GO; GO:0003093; P:regulation of glomerular filtration; IEA:Ensembl.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; IEA:Ensembl.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl.
DR GO; GO:0014074; P:response to purine-containing compound; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0001659; P:temperature homeostasis; IEA:Ensembl.
DR GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
DR DisProt; DP02651; -.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..326
FT /note="Adenosine receptor A1"
FT /id="PRO_0000068991"
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 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 115..125
FT /note="YKMVVTPRRAA -> RISQCMASTKS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_034401"
FT VAR_SEQ 126..326
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_034402"
FT VARIANT 43
FT /note="A -> S (in dbSNP:rs11547175)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_044138"
FT VARIANT 50
FT /note="S -> P (in dbSNP:rs11547174)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_044139"
FT VARIANT 105
FT /note="R -> H (in dbSNP:rs11547176)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_044140"
FT VARIANT 170
FT /note="E -> K (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs899207013)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035754"
FT VARIANT 261
FT /note="P -> Q (in dbSNP:rs17852405)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_044141"
FT VARIANT 279
FT /note="G -> S (found in a family with early-onset autosomal
FT recessive parkinsonism and intellectual disability; unknown
FT pathological significance; does not affect protein
FT abundance; does not affect expression at the cell surface;
FT dbSNP:rs748346254)"
FT /evidence="ECO:0000269|PubMed:27134041"
FT /id="VAR_078549"
FT CONFLICT 312
FT /note="A -> T (in Ref. 7; BAF82617)"
FT /evidence="ECO:0000305"
FT HELIX 7..36
FT /evidence="ECO:0007829|PDB:5UEN"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:5UEN"
FT HELIX 43..60
FT /evidence="ECO:0007829|PDB:5UEN"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:5UEN"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:7LD3"
FT HELIX 77..110
FT /evidence="ECO:0007829|PDB:5UEN"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:5UEN"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:5UEN"
FT HELIX 121..140
FT /evidence="ECO:0007829|PDB:5UEN"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:5UEN"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:5UEN"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:7LD3"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:5UEN"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:5UEN"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:5UEN"
FT HELIX 190..211
FT /evidence="ECO:0007829|PDB:5UEN"
FT HELIX 228..259
FT /evidence="ECO:0007829|PDB:5UEN"
FT HELIX 267..291
FT /evidence="ECO:0007829|PDB:5UEN"
FT HELIX 293..306
FT /evidence="ECO:0007829|PDB:5UEN"
SQ SEQUENCE 326 AA; 36512 MW; 1B555893BCDEC9A6 CRC64;
MPPSISAFQA AYIGIEVLIA LVSVPGNVLV IWAVKVNQAL RDATFCFIVS LAVADVAVGA
LVIPLAILIN IGPQTYFHTC LMVACPVLIL TQSSILALLA IAVDRYLRVK IPLRYKMVVT
PRRAAVAIAG CWILSFVVGL TPMFGWNNLS AVERAWAANG SMGEPVIKCE FEKVISMEYM
VYFNFFVWVL PPLLLMVLIY LEVFYLIRKQ LNKKVSASSG DPQKYYGKEL KIAKSLALIL
FLFALSWLPL HILNCITLFC PSCHKPSILT YIAIFLTHGN SAMNPIVYAF RIQKFRVTFL
KIWNDHFRCQ PAPPIDEDLP EERPDD
