ID Q5XGP4_XENLA Unreviewed; 392 AA.
AC Q5XGP4;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Adenosine receptor A2 {ECO:0000256|RuleBase:RU201114};
GN Name=adora2a.L {ECO:0000313|RefSeq:NP_001088336.1,
GN ECO:0000313|Xenbase:XB-GENE-970786};
GN Synonyms=adora2a {ECO:0000313|RefSeq:NP_001088336.1,
GN ECO:0000313|Xenbase:XB-GENE-970786}, LOC495175
GN {ECO:0000313|EMBL:AAH84390.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH84390.1};
RN [1] {ECO:0000313|RefSeq:NP_001088336.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH84390.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Whole {ECO:0000313|EMBL:AAH84390.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001088336.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for adenosine. The activity of this receptor is
CC mediated by G proteins which activate adenylyl cyclase.
CC {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; BC084390; AAH84390.1; -; mRNA.
DR RefSeq; NP_001088336.1; NM_001094867.1.
DR DNASU; 495175; -.
DR GeneID; 495175; -.
DR KEGG; xla:495175; -.
DR AGR; Xenbase:XB-GENE-970786; -.
DR CTD; 495175; -.
DR Xenbase; XB-GENE-970786; adora2a.L.
DR OrthoDB; 2909020at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 495175; Expressed in lung and 18 other cell types or tissues.
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; cd15068; 7tmA_Adenosine_R_A2A; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR001513; Adeno_A2A_rcpt.
DR InterPro; IPR001634; Adenosn_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24246:SF47; ADENOSINE RECEPTOR A2A; 1.
DR PANTHER; PTHR24246; OLFACTORY RECEPTOR AND ADENOSINE RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00553; ADENOSINA2AR.
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 2: Evidence at transcript level;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU201114};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU201114};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU201114};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
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 13..37
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU201114"
FT TRANSMEM 49..72
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU201114"
FT TRANSMEM 78..106
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU201114"
FT TRANSMEM 127..149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU201114"
FT TRANSMEM 180..206
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU201114"
FT TRANSMEM 232..251
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU201114"
FT TRANSMEM 271..292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU201114"
FT DOMAIN 29..290
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT REGION 361..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 43916 MW; E68A03AE514AF634 CRC64;
MVTVSNNKNP EDLVYIVLEV AIAVLSILGN VLVCWAVCIN SNLQNATNYF VVSLAAADIA
VGVLAIPFSI AISTGFCATF HACLFIACFV LVLTQSSIFS LLAIAADRYI AIRIPLRYNS
LVTSRRANAI IAVCWLLSFV IGLTPLLGWH KEVPPTGNTT CRSPMIECLF ENVVTMDYMV
FYNFFACVLV PLLLMLGIYL RIFMAARHQL KQMKMKVTCG ERSRSTLQRE VHAAKSLAII
VGLFALCWLP LHIINCFTLF CKACDRPPLW IMYIAILLSH ANSVVNPLIY AYRIREFRNT
FRKILRQHLF GQGQPIKTRT ASAKSLTYYG VDEETGITQV RFSSCNLGTH TNGSVCKLKE
ERRQNGCPSQ HQEKRTGSSR YSGQKKEMME IS
//
