P2X purinoceptor 1

Details

Name
P2X purinoceptor 1
Synonyms
  • ATP receptor
  • P2X1
  • Purinergic receptor
Gene Name
P2RX1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0052221|P2X purinoceptor 1
MARRFQEELAAFLFEYDTPRMVLVRNKKVGVIFRLIQLVVLVYVIGWVFLYEKGYQTSSG
LISSVSVKLKGLAVTQLPGLGPQVWDVADYVFPAQGDNSFVVMTNFIVTPKQTQGYCAEH
PEGGICKEDSGCTPGKAKRKAQGIRTGKCVAFNDTVKTCEIFGWCPVEVDDDIPRPALLR
EAENFTLFIKNSISFPRFKVNRRNLVEEVNAAHMKTCLFHKTLHPLCPVFQLGYVVQESG
QNFSTLAEKGGVVGITIDWHCDLDWHVRHCRPIYEFHGLYEEKNLSPGFNFRFARHFVEN
GTNYRHLFKVFGIRFDILVDGKAGKFDIIPTMTTIGSGIGIFGVATVLCDLLLLHILPKR
HYYKQKKFKYAEDMGPGAAERDLAATSSTLGLQENMRTS
Number of residues
399
Molecular Weight
44979.79
Theoretical pI
Not Available
GO Classification
Functions
ATP binding / cation channel activity / extracellularly ATP-gated cation channel activity / purinergic nucleotide receptor activity / zinc ion binding
Processes
activation of cysteine-type endopeptidase activity involved in apoptotic process / apoptotic process / blood coagulation / ceramide biosynthetic process / insemination / ion transport / neuronal action potential / neutrophil degranulation / platelet activation / positive regulation of ion transport / protein heterooligomerization / protein homooligomerization / regulation of blood pressure / regulation of calcium ion transport / regulation of presynaptic cytosolic calcium ion concentration / regulation of synaptic vesicle exocytosis / regulation of vascular smooth muscle contraction / response to ATP / serotonin secretion by platelet / signal transduction / synaptic transmission, glutamatergic
Components
external side of plasma membrane / glutamatergic synapse / integral component of nuclear inner membrane / integral component of plasma membrane / integral component of postsynaptic membrane / integral component of presynaptic active zone membrane / membrane raft / neuron projection / plasma membrane / protein-containing complex / secretory granule membrane / specific granule membrane
General Function
Ligand-gated ion channel with relatively high calcium permeability. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle. Seems to be linked to apoptosis, by increasing the intracellular concentration of calcium in the presence of ATP, leading to programmed cell death (By similarity).
Specific Function
Atp binding
Pfam Domain Function
Not Available
Transmembrane Regions
29-50 339-358
Cellular Location
Membrane
Gene sequence
>lcl|BSEQ0052222|P2X purinoceptor 1 (P2RX1)
ATGGCACGGCGGTTCCAGGAGGAGCTGGCCGCCTTCCTCTTCGAGTATGACACCCCCCGC
ATGGTGCTGGTGCGTAATAAGAAGGTGGGCGTTATCTTCCGACTGATCCAGCTGGTGGTC
CTGGTCTACGTCATCGGGTGGGTGTTTCTCTATGAGAAGGGCTACCAGACCTCGAGCGGC
CTCATCAGCAGTGTCTCTGTGAAACTCAAGGGCCTGGCCGTGACCCAGCTCCCTGGCCTC
GGCCCCCAGGTCTGGGATGTGGCTGACTACGTCTTCCCAGCCCAGGGGGACAACTCCTTC
GTGGTCATGACCAATTTCATCGTGACCCCGAAGCAGACTCAAGGCTACTGCGCAGAGCAC
CCAGAAGGGGGCATATGCAAGGAAGACAGTGGCTGTACCCCTGGGAAGGCCAAGAGGAAG
GCCCAAGGCATCCGCACGGGCAAGTGTGTGGCCTTCAACGACACTGTGAAGACGTGTGAG
ATCTTTGGCTGGTGCCCCGTGGAGGTGGATGACGACATCCCGCGCCCTGCCCTTCTCCGA
GAGGCCGAGAACTTCACTCTTTTCATCAAGAACAGCATCAGCTTTCCACGCTTCAAGGTC
AACAGGCGCAACCTGGTGGAGGAGGTGAATGCTGCCCACATGAAGACCTGCCTCTTTCAC
AAGACCCTGCACCCCCTGTGCCCAGTCTTCCAGCTTGGCTACGTGGTGCAAGAGTCAGGC
CAGAACTTCAGCACCCTGGCTGAGAAGGGTGGAGTGGTTGGCATCACCATCGACTGGCAC
TGTGACCTGGACTGGCACGTACGGCACTGCAGACCCATCTATGAGTTCCATGGGCTGTAC
GAAGAGAAAAATCTCTCCCCAGGCTTCAACTTCAGGTTTGCCAGGCACTTTGTGGAGAAC
GGGACCAACTACCGTCACCTCTTCAAGGTGTTTGGGATTCGCTTTGACATCCTGGTGGAC
GGCAAGGCCGGGAAGTTTGACATCATCCCTACAATGACCACCATCGGCTCTGGAATTGGC
ATCTTTGGGGTGGCCACAGTTCTCTGTGACCTGCTGCTGCTTCACATCCTGCCTAAGAGG
CACTACTACAAGCAGAAGAAGTTCAAATACGCTGAGGACATGGGGCCAGGGGCGGCTGAG
CGTGACCTCGCAGCTACCAGCTCCACCCTGGGCCTGCAGGAGAACATGAGGACATCCTGA
Chromosome Location
17
Locus
17p13.2
External Identifiers
ResourceLink
UniProtKB IDP51575
UniProtKB Entry NameP2RX1_HUMAN
HGNC IDHGNC:8533
General References
  1. Valera S, Talabot F, Evans RJ, Gos A, Antonarakis SE, Morris MA, Buell GN: Characterization and chromosomal localization of a human P2X receptor from the urinary bladder. Receptors Channels. 1995;3(4):283-9. [Article]
  2. Longhurst PA, Schwegel T, Folander K, Swanson R: The human P2x1 receptor: molecular cloning, tissue distribution, and localization to chromosome 17. Biochim Biophys Acta. 1996 Sep 11;1308(3):185-8. [Article]
  3. Sun B, Li J, Okahara K, Kambayashi J: P2X1 purinoceptor in human platelets. Molecular cloning and functional characterization after heterologous expression. J Biol Chem. 1998 May 8;273(19):11544-7. [Article]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  5. Ennion SJ, Evans RJ: Conserved cysteine residues in the extracellular loop of the human P2X(1) receptor form disulfide bonds and are involved in receptor trafficking to the cell surface. Mol Pharmacol. 2002 Feb;61(2):303-11. [Article]
  6. Roberts JA, Bottrill AR, Mistry S, Evans RJ: Mass spectrometry analysis of human P2X1 receptors; insight into phosphorylation, modelling and conformational changes. J Neurochem. 2012 Dec;123(5):725-35. doi: 10.1111/jnc.12012. Epub 2012 Oct 11. [Article]
  7. Oury C, Toth-Zsamboki E, Van Geet C, Thys C, Wei L, Nilius B, Vermylen J, Hoylaerts MF: A natural dominant negative P2X1 receptor due to deletion of a single amino acid residue. J Biol Chem. 2000 Jul 28;275(30):22611-4. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01069Promethazineapproved, investigationalunknowninhibitorDetails