Proteinase-activated receptor 1

NameProteinase-activated receptor 1
Synonyms
  • CF2R
  • Coagulation factor II receptor
  • PAR-1
  • PAR1
  • Thrombin receptor
  • TR
Gene NameF2R
OrganismHuman
Amino acid sequence
>lcl|BSEQ0010652|Proteinase-activated receptor 1
MGPRRLLLVAACFSLCGPLLSARTRARRPESKATNATLDPRSFLLRNPNDKYEPFWEDEE
KNESGLTEYRLVSINKSSPLQKQLPAFISEDASGYLTSSWLTLFVPSVYTGVFVVSLPLN
IMAIVVFILKMKVKKPAVVYMLHLATADVLFVSVLPFKISYYFSGSDWQFGSELCRFVTA
AFYCNMYASILLMTVISIDRFLAVVYPMQSLSWRTLGRASFTCLAIWALAIAGVVPLLLK
EQTIQVPGLNITTCHDVLNETLLEGYYAYYFSAFSAVFFFVPLIISTVCYVSIIRCLSSS
AVANRSKKSRALFLSAAVFCIFIICFGPTNVLLIAHYSFLSHTSTTEAAYFAYLLCVCVS
SISCCIDPLIYYYASSECQRYVYSILCCKESSDPSSYNSSGQLMASKMDTCSSNLNNSIY
KKLLT
Number of residues425
Molecular Weight47439.83
Theoretical pI8.33
GO Classification
Functions
  • G-protein beta-subunit binding
  • receptor binding
  • thrombin receptor activity
  • G-protein coupled receptor activity
  • G-protein alpha-subunit binding
Processes
  • anatomical structure morphogenesis
  • G-protein coupled receptor signaling pathway
  • tyrosine phosphorylation of STAT protein
  • positive regulation of ERK1 and ERK2 cascade
  • positive regulation of smooth muscle contraction
  • connective tissue replacement involved in inflammatory response wound healing
  • negative regulation of neuron apoptotic process
  • positive regulation of blood coagulation
  • establishment of synaptic specificity at neuromuscular junction
  • activation of cysteine-type endopeptidase activity involved in apoptotic process
  • positive regulation of cell proliferation
  • homeostasis of number of cells within a tissue
  • inflammatory response
  • regulation of sensory perception of pain
  • positive regulation of collagen biosynthetic process
  • negative regulation of glomerular filtration
  • positive regulation of MAPK cascade
  • positive regulation of phosphatidylinositol 3-kinase signaling
  • positive regulation of release of sequestered calcium ion into cytosol
  • platelet activation
  • regulation of blood coagulation
  • response to wounding
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process
  • protein kinase C-activating G-protein coupled receptor signaling pathway
  • phospholipase C-activating G-protein coupled receptor signaling pathway
  • positive regulation of cytosolic calcium ion concentration
  • release of sequestered calcium ion into cytosol
  • negative regulation of renin secretion into blood stream
  • positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway
  • positive regulation of calcium ion transport
  • positive regulation of interleukin-6 secretion
  • response to lipopolysaccharide
  • positive regulation of cell migration
  • positive regulation of I-kappaB kinase/NF-kappaB signaling
  • positive regulation of JAK-STAT cascade
  • positive regulation of transcription, DNA-templated
  • positive regulation of interleukin-8 secretion
  • positive regulation of Rho protein signal transduction
  • platelet dense granule organization
  • activation of MAPKK activity
  • regulation of interleukin-1 beta production
  • blood coagulation
  • positive regulation of vasoconstriction
  • negative regulation of cell proliferation
  • STAT protein import into nucleus
Components
  • extracellular region
  • postsynaptic membrane
  • plasma membrane
  • cell surface
  • late endosome
  • early endosome
  • Golgi apparatus
  • neuromuscular junction
  • cytosol
  • integral component of plasma membrane
  • caveola
  • platelet dense tubular network
General FunctionThrombin receptor activity
Specific FunctionHigh affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development.
Pfam Domain Function
Transmembrane Regions103-128 138-157 177-198 219-239 269-288 312-334 351-374
GenBank Protein ID339677
UniProtKB IDP25116
UniProtKB Entry NamePAR1_HUMAN
Cellular LocationCell membrane
Gene sequence
>lcl|BSEQ0010653|Proteinase-activated receptor 1 (F2R)
ATGGGGCCGCGGCGGCTGCTGCTGGTGGCCGCCTGCTTCAGTCTGTGCGGCCCGCTGTTG
TCTGCCCGCACCCGGGCCCGCAGGCCAGAATCAAAAGCAACAAATGCCACCTTAGATCCC
CGGTCATTTCTTCTCAGGAACCCCAATGATAAATATGAACCATTTTGGGAGGATGAGGAG
AAAAATGAAAGTGGGTTAACTGAATACAGATTAGTCTCCATCAATAAAAGCAGTCCTCTT
CAAAAACAACTTCCTGCATTCATCTCAGAAGATGCCTCCGGATATTTGACCAGCTCCTGG
CTGACACTCTTTGTCCCATCTGTGTACACCGGAGTGTTTGTAGTCAGCCTCCCACTAAAC
ATCATGGCCATCGTTGTGTTCATCCTGAAAATGAAGGTCAAGAAGCCGGCGGTGGTGTAC
ATGCTGCACCTGGCCACGGCAGATGTGCTGTTTGTGTCTGTGCTCCCCTTTAAGATCAGC
TATTACTTTTCCGGCAGTGATTGGCAGTTTGGGTCTGAATTGTGTCGCTTCGTCACTGCA
GCATTTTACTGTAACATGTACGCCTCTATCTTGCTCATGACAGTCATAAGCATTGACCGG
TTTCTGGCTGTGGTGTATCCCATGCAGTCCCTCTCCTGGCGTACTCTGGGAAGGGCTTCC
TTCACTTGTCTGGCCATCTGGGCTTTGGCCATCGCAGGGGTAGTGCCTCTGCTCCTCAAG
GAGCAAACCATCCAGGTGCCCGGGCTCAACATCACTACCTGTCATGATGTGCTCAATGAA
ACCCTGCTCGAAGGCTACTATGCCTACTACTTCTCAGCCTTCTCTGCTGTCTTCTTTTTT
GTGCCGCTGATCATTTCCACGGTCTGTTATGTGTCTATCATTCGATGTCTTAGCTCTTCC
GCAGTTGCCAACCGCAGCAAGAAGTCCCGGGCTTTGTTCCTGTCAGCTGCTGTTTTCTGC
ATCTTCATCATTTGCTTCGGACCCACAAACGTCCTCCTGATTGCGCATTACTCATTCCTT
TCTCACACTTCCACCACAGAGGCTGCCTACTTTGCCTACCTCCTCTGTGTCTGTGTCAGC
AGCATAAGCTGCTGCATCGACCCCCTAATTTACTATTACGCTTCCTCTGAGTGCCAGAGG
TACGTCTACAGTATCTTATGCTGCAAAGAAAGTTCCGATCCCAGCAGTTATAACAGCAGT
GGGCAGTTGATGGCAAGTAAAATGGATACCTGCTCTAGTAACCTGAATAACAGCATATAC
AAAAAGCTGTTAACTTAG
GenBank Gene IDM62424
GeneCard IDNot Available
GenAtlas IDF2R
HGNC IDHGNC:3537
Chromosome Location5
Locus5q13
References
  1. Vu TK, Hung DT, Wheaton VI, Coughlin SR: Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell. 1991 Mar 22;64(6):1057-68. 1672265
  2. 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. 15489334
  3. Shapiro MJ, Trejo J, Zeng D, Coughlin SR: Role of the thrombin receptor's cytoplasmic tail in intracellular trafficking. Distinct determinants for agonist-triggered versus tonic internalization and intracellular localization. J Biol Chem. 1996 Dec 20;271(51):32874-80. 8955127
  4. Kahn ML, Nakanishi-Matsui M, Shapiro MJ, Ishihara H, Coughlin SR: Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin. J Clin Invest. 1999 Mar;103(6):879-87. 10079109
  5. Zania P, Gourni D, Aplin AC, Nicosia RF, Flordellis CS, Maragoudakis ME, Tsopanoglou NE: Parstatin, the cleaved peptide on proteinase-activated receptor 1 activation, is a potent inhibitor of angiogenesis. J Pharmacol Exp Ther. 2009 Feb;328(2):378-89. doi: 10.1124/jpet.108.145664. Epub 2008 Nov 6. 18988770
  6. Zampatis DE, Rutz C, Furkert J, Schmidt A, Wustenhagen D, Kubick S, Tsopanoglou NE, Schulein R: The protease-activated receptor 1 possesses a functional and cleavable signal peptide which is necessary for receptor expression. FEBS Lett. 2012 Jul 30;586(16):2351-9. doi: 10.1016/j.febslet.2012.05.042. Epub 2012 May 31. 22659187
  7. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. 10391209
  8. Mathews II, Padmanabhan KP, Ganesh V, Tulinsky A, Ishii M, Chen J, Turck CW, Coughlin SR, Fenton JW 2nd: Crystallographic structures of thrombin complexed with thrombin receptor peptides: existence of expected and novel binding modes. Biochemistry. 1994 Mar 22;33(11):3266-79. 8136362