(data stored in ACNUC26264 zone)

HOGENOM: HS3_PE4771

ID   HS3_PE4771                           STANDARD;      PRT;   373 AA.
AC   HS3_PE4771; P47900;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=P2Y purinoceptor 1; Short=P2Y1;AltName: Full=ATP
DE   receptor;AltName: Full=Purinergic receptor; (HS3.PE4771).
GN   Name=P2RY1;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS3.PE4771.
CC       Homo sapiens chromosome 3 GRCh37  sequence 1..197962430 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:P2RY1_HUMAN
CC   -!- FUNCTION: Receptor for extracellular adenine nucleotides such as
CC       ATP and ADP. In platelets binding to ADP leads to mobilization of
CC       intracellular calcium ions via activation of phospholipase C, a
CC       change in platelet shape, and probably to platelet aggregation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- INDUCTION: Repressed by the P2Y1 receptor-specific antagonists
CC       A3P5PS, A3P5P and A2P5P. These inhibit calcium ion mobilization
CC       and shape change in platelets.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -!- GENE_FAMILY: HOG000231307 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000169860;ENST00000305097;ENSP00000304767.
DR   EMBL; AF018284; - ;
DR   EMBL; AJ006945; - ;
DR   EMBL; AK313920; - ;
DR   EMBL; AY136752; - ;
DR   EMBL; BC074784; - ;
DR   EMBL; BC074785; - ;
DR   EMBL; S81950; - ;
DR   EMBL; U42029; - ;
DR   EMBL; U42030; - ;
DR   EMBL; Z49205; - ;
DR   UniProtKB/Swiss-Prot; P47900; -.
DR   EMBL; Z49205; CAA89066.1; -; mRNA.
DR   EMBL; U42030; AAA97873.1; -; mRNA.
DR   EMBL; U42029; AAA97872.1; -; mRNA.
DR   EMBL; S81950; AAB47091.1; -; Genomic_DNA.
DR   EMBL; AJ006945; CAA07339.1; -; Genomic_DNA.
DR   EMBL; AY136752; AAN01278.1; -; mRNA.
DR   EMBL; BC074784; AAH74784.1; -; mRNA.
DR   EMBL; BC074785; AAH74785.1; -; mRNA.
DR   EMBL; AF018284; AAB94556.1; -; mRNA.
DR   IPI; IPI00026825; -.
DR   PIR; JC4737; JC4737.
DR   RefSeq; NP_002554.1; NM_002563.2.
DR   UniGene; Hs.654526; -.
DR   PDB; 1Y36; Model; -; A=1-373.
DR   PDBsum; 1Y36; -.
DR   ProteinModelPortal; P47900; -.
DR   SMR; P47900; 136-167.
DR   STRING; P47900; -.
DR   PhosphoSite; P47900; -.
DR   PRIDE; P47900; -.
DR   Ensembl; ENST00000305097; ENSP00000304767; ENSG00000169860.
DR   GeneID; 5028; -.
DR   KEGG; hsa:5028; -.
DR   UCSC; uc003ezq.1; human.
DR   CTD; 5028; -.
DR   GeneCards; GC03P149943; -.
DR   H-InvDB; HIX0030700; -.
DR   HGNC; HGNC:8539; P2RY1.
DR   HPA; HPA015577; -.
DR   HPA; HPA017674; -.
DR   MIM; 601167; gene.
DR   neXtProt; NX_P47900; -.
DR   PharmGKB; PA32868; -.
DR   eggNOG; prNOG04390; -.
DR   GeneTree; ENSGT00600000084187; -.
DR   InParanoid; P47900; -.
DR   OMA; YSMCTTV; -.
DR   OrthoDB; EOG4MW868; -.
DR   PhylomeDB; P47900; -.
DR   Reactome; REACT_14797; Signaling by GPCR.
DR   Reactome; REACT_604; Hemostasis.
DR   NextBio; 19362; -.
DR   ArrayExpress; P47900; -.
DR   Bgee; P47900; -.
DR   CleanEx; HS_P2RY1; -.
DR   Genevestigator; P47900; -.
DR   GermOnline; ENSG00000169860; Homo sapiens.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR   GO; GO:0045028; F:purinergic nucleotide receptor activity, G-protein coupled; IEA:InterPro.
DR   GO; GO:0007200; P:activation of phospholipase C activity by G-protein coupled receptor protein signaling pathway coDR   GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR   GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR002286; P2_purnocptor.
DR   InterPro; IPR000142; P2Y_purnocptor.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00595; P2Y1PRNOCPTR.
DR   PRINTS; PR01157; P2YPURNOCPTR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   HOGENOMDNA; HS3.PE4771; -.
KW   ENSG000001698601755old_1320000031; ENSP000003047677901old_1320000031;
KW   B2R9U4_HUMAN; AF018284; AJ006945; AK313920; AY136752; BC074784; BC074785;
KW   U42029; U42030; Z49205;
KW   3D-structure; Blood coagulation; Cell membrane; Complete proteome;
KW   Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   373 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTEVLWPAVP NGTDAAFLAG PGSSWGNSTV ASTAAVSSSF KCALTKTGFQ FYYLPAVYIL
     VFIIGFLGNS VAIWMFVFHM KPWSGISVYM FNLALADFLY VLTLPALIFY YFNKTDWIFG
     DAMCKLQRFI FHVNLYGSIL FLTCISAHRY SGVVYPLKSL GRLKKKNAIC ISVLVWLIVV
     VAISPILFYS GTGVRKNKTI TCYDTTSDEY LRSYFIYSMC TTVAMFCVPL VLILGCYGLI
     VRALIYKDLD NSPLRRKSIY LVIIVLTVFA VSYIPFHVMK TMNLRARLDF QTPAMCAFND
     RVYATYQVTR GLASLNSCVD PILYFLAGDT FRRRLSRATR KASRRSEANL QSKSEDMTLN
     ILPEFKQNGD TSL
//

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