ID   P2RY4_XENLA             Reviewed;         537 AA.
AC   P79928;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=P2Y purinoceptor 4;
DE            Short=P2Y4;
DE   AltName: Full=P2Y purinoceptor 8;
DE            Short=P2Y8;
GN   Name=p2ry4; Synonyms=p2ry8;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Neural plate;
RX   PubMed=9139711; DOI=10.1074/jbc.272.19.12583;
RA   Bogdanov Y.D., Dale L., King B.F., Whittock N., Burnstock G.;
RT   "Early expression of a novel nucleotide receptor in the neural plate of
RT   Xenopus embryos.";
RL   J. Biol. Chem. 272:12583-12590(1997).
CC   -!- FUNCTION: Receptor for extracellular ATP, UTP, CTP, GTP and ITP. The
CC       activity of this receptor is mediated by G proteins which activate a
CC       phosphatidylinositol-calcium second messenger system. May play a key
CC       role in the early development of neural tissue.
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; X99953; CAA68213.1; -; mRNA.
DR   AlphaFoldDB; P79928; -.
DR   SMR; P79928; -.
DR   Proteomes; UP000186698; Genome assembly.
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:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IEA:InterPro.
DR   GO; GO:0030321; P:transepithelial chloride transport; IEA:InterPro.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000018; P2Y4.
DR   PANTHER; PTHR24231:SF21; PTHR24231:SF21; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01066; P2Y4PRNOCPTR.
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   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..537
FT                   /note="P2Y purinoceptor 4"
FT                   /id="PRO_0000070024"
FT   TOPO_DOM        1..49
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..79
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..118
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        140..161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..210
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..254
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        276..292
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..316
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        317..537
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          401..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        116..193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   537 AA;  62024 MW;  B2CF24812F3C19F2 CRC64;
     MTEDIMATSY PTFLTTPYLP MKLLMNLTND TEDICVFDEG FKFLLLPVSY SAVFMVGLPL
     NIAAMWIFIA KMRPWNPTTV YMFNLALSDT LYVLSLPTLV YYYADKNNWP FGEVLCKLVR
     FLFYANLYSS ILFLTCISVH RYRGVCHPIT SLRRMNAKHA YVICALVWLS VTLCLVPNLI
     FVTVSPKVKN TICHDTTRPE DFARYVEYST AIMCLLFGIP CLIIAGCYGL MTRELMKPIV
     SGNQQTLPSY KKRSIKTIIF VMIAFAICFM PFHITRTLYY YARLLGIKCY ALNVINVTYK
     VTRPLASANS CIDPILYFLA NDRYRRRLIR TVRRRSSVPN RRCMHTNHPQ TEPHMTAGPL
     PVISAEEIPS NGSMVRDENG EGSREHRVEW TDTKEINQMM NRRSTIKRNS TDKNDMKENR
     HGENYLPYVE VVEKEDYETK RENRKTTEQS SKTNAEQDEL QTQIDSRLKR GKWQLSSKKG
     AAQENEKGHM EPSFEGEGTS TWNLLTPKMY GKKDRLAKNV EEVGYGKEKE LQNFPKA