P47900 · P2RY1_HUMAN
- ProteinP2Y purinoceptor 1
- GeneP2RY1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids373 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor for extracellular adenine nucleotides such as ADP (PubMed:25822790, PubMed:9038354, PubMed:9442040).
In platelets, binding to ADP leads to mobilization of intracellular calcium ions via activation of phospholipase C, a change in platelet shape, and ultimately platelet aggregation (PubMed:9442040).
In platelets, binding to ADP leads to mobilization of intracellular calcium ions via activation of phospholipase C, a change in platelet shape, and ultimately platelet aggregation (PubMed:9442040).
Activity regulation
ATP functions as antagonist and inhibits ADP-induced mobilization of Ca2+ (PubMed:9038354).
The P2Y1 receptor-specific antagonists A3P5PS, A3P5P and A2P5P inhibit downstream signaling mediated by mobilization of Ca2+ from intracellular stores, and platelet shape changes in response to extracellular ADP (PubMed:9442040).
The P2Y1 receptor-specific antagonists A3P5PS, A3P5P and A2P5P inhibit downstream signaling mediated by mobilization of Ca2+ from intracellular stores, and platelet shape changes in response to extracellular ADP (PubMed:9442040).
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameP2Y purinoceptor 1
- Short namesP2Y1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP47900
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-51 | Extracellular | ||||
Sequence: MTEVLWPAVPNGTDAAFLAGPGSSWGNSTVASTAAVSSSFKCALTKTGFQF | ||||||
Transmembrane | 52-74 | Helical; Name=1 | ||||
Sequence: YYLPAVYILVFIIGFLGNSVAIW | ||||||
Topological domain | 75-87 | Cytoplasmic | ||||
Sequence: MFVFHMKPWSGIS | ||||||
Transmembrane | 88-109 | Helical; Name=2 | ||||
Sequence: VYMFNLALADFLYVLTLPALIF | ||||||
Topological domain | 110-125 | Extracellular | ||||
Sequence: YYFNKTDWIFGDAMCK | ||||||
Transmembrane | 126-147 | Helical; Name=3 | ||||
Sequence: LQRFIFHVNLYGSILFLTCISA | ||||||
Topological domain | 148-166 | Cytoplasmic | ||||
Sequence: HRYSGVVYPLKSLGRLKKK | ||||||
Transmembrane | 167-188 | Helical; Name=4 | ||||
Sequence: NAICISVLVWLIVVVAISPILF | ||||||
Topological domain | 189-214 | Extracellular | ||||
Sequence: YSGTGVRKNKTITCYDTTSDEYLRSY | ||||||
Transmembrane | 215-237 | Helical; Name=5 | ||||
Sequence: FIYSMCTTVAMFCVPLVLILGCY | ||||||
Topological domain | 238-260 | Cytoplasmic | ||||
Sequence: GLIVRALIYKDLDNSPLRRKSIY | ||||||
Transmembrane | 261-284 | Helical; Name=6 | ||||
Sequence: LVIIVLTVFAVSYIPFHVMKTMNL | ||||||
Topological domain | 285-303 | Extracellular | ||||
Sequence: RARLDFQTPAMCAFNDRVY | ||||||
Transmembrane | 304-325 | Helical; Name=7 | ||||
Sequence: ATYQVTRGLASLNSCVDPILYF | ||||||
Topological domain | 326-373 | Cytoplasmic | ||||
Sequence: LAGDTFRRRLSRATRKASRRSEANLQSKSEDMTLNILPEFKQNGDTSL |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 44 | Loss of ADP analog binding. | ||||
Sequence: L → A | ||||||
Mutagenesis | 110 | Loss of ADP analog binding. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 203 | Loss of ADP analog binding. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 205 | Loss of ADP analog binding. | ||||
Sequence: T → A | ||||||
Mutagenesis | 283 | Loss of ADP analog binding. | ||||
Sequence: N → A | ||||||
Mutagenesis | 306 | Strongly decreased affinity for ADP analog. | ||||
Sequence: Y → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 373 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000070006 | 1-373 | P2Y purinoceptor 1 | |||
Sequence: MTEVLWPAVPNGTDAAFLAGPGSSWGNSTVASTAAVSSSFKCALTKTGFQFYYLPAVYILVFIIGFLGNSVAIWMFVFHMKPWSGISVYMFNLALADFLYVLTLPALIFYYFNKTDWIFGDAMCKLQRFIFHVNLYGSILFLTCISAHRYSGVVYPLKSLGRLKKKNAICISVLVWLIVVVAISPILFYSGTGVRKNKTITCYDTTSDEYLRSYFIYSMCTTVAMFCVPLVLILGCYGLIVRALIYKDLDNSPLRRKSIYLVIIVLTVFAVSYIPFHVMKTMNLRARLDFQTPAMCAFNDRVYATYQVTRGLASLNSCVDPILYFLAGDTFRRRLSRATRKASRRSEANLQSKSEDMTLNILPEFKQNGDTSL | ||||||
Glycosylation | 11 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 27 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 42↔296 | |||||
Sequence: CALTKTGFQFYYLPAVYILVFIIGFLGNSVAIWMFVFHMKPWSGISVYMFNLALADFLYVLTLPALIFYYFNKTDWIFGDAMCKLQRFIFHVNLYGSILFLTCISAHRYSGVVYPLKSLGRLKKKNAICISVLVWLIVVVAISPILFYSGTGVRKNKTITCYDTTSDEYLRSYFIYSMCTTVAMFCVPLVLILGCYGLIVRALIYKDLDNSPLRRKSIYLVIIVLTVFAVSYIPFHVMKTMNLRARLDFQTPAMC | ||||||
Glycosylation | 113 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 124↔202 | |||||
Sequence: CKLQRFIFHVNLYGSILFLTCISAHRYSGVVYPLKSLGRLKKKNAICISVLVWLIVVVAISPILFYSGTGVRKNKTITC | ||||||
Glycosylation | 197 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P47900 | NHERF1 O14745 | 2 | EBI-8677223, EBI-349787 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length373
- Mass (Da)42,072
- Last updated1996-02-01 v1
- Checksum4DC7C668B4145392
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 138 | in Ref. 1; CAA89066 | ||||
Sequence: Missing |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z49205 EMBL· GenBank· DDBJ | CAA89066.1 EMBL· GenBank· DDBJ | mRNA | ||
U42030 EMBL· GenBank· DDBJ | AAA97873.1 EMBL· GenBank· DDBJ | mRNA | ||
U42029 EMBL· GenBank· DDBJ | AAA97872.1 EMBL· GenBank· DDBJ | mRNA | ||
S81950 EMBL· GenBank· DDBJ | AAB47091.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ006945 EMBL· GenBank· DDBJ | CAA07339.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY136752 EMBL· GenBank· DDBJ | AAN01278.1 EMBL· GenBank· DDBJ | mRNA | ||
BC074784 EMBL· GenBank· DDBJ | AAH74784.1 EMBL· GenBank· DDBJ | mRNA | ||
BC074785 EMBL· GenBank· DDBJ | AAH74785.1 EMBL· GenBank· DDBJ | mRNA | ||
AF018284 EMBL· GenBank· DDBJ | AAB94556.1 EMBL· GenBank· DDBJ | mRNA |