Search results for P25116

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Results (5 results from a total of 5)

Identifier: R-HSA-61309
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: F2R: P25116
This is the inactive form of the receptor, before protease activation. Proteinase (protease) activated receptors are activated by the cleavage of an N-terminal extracellular segment by serine proteases, particularly thrombin which activates PAR1, 3 and 4. The cleaved fragment is an activating ligand for the receptor; synthetic peptide mimics of the N-terminal fragment can activate uncleaved receptors.
Identifier: R-HSA-114531
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: F2R: P25116
Identifier: R-HSA-9708861
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: F2R: P25116
Identifier: R-HSA-114586
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: F2R: P25116
Thrombin recognizes the N-terminal exodomain of PAR1 by interacting with sites both amino and carboxyl terminal to the thrombin cleavage site. Thrombin cleaves the peptide bond between receptor residues Arg41 and Ser42. This serves to unmask a new amino terminus beginning with the sequence SFLLRN that functions as a tethered ligand, docking intramolecularly with the body of the receptor to effect transmembrane signaling. A synthetic peptide of sequence SFLLRN, which mimics the tethered ligand sequence, will function as an agonist for PAR1 independent of receptor cleavage. Thus PAR1 is, in essence, a peptide receptor that carries its own ligand, the latter being active only after receptor cleavage.
Species: Homo sapiens
Curator: Steve Jupe
Designer: Cristoffer Sevilla
PAR1,3,4 icon
Proteinase-activated receptor 1, 3 and 4
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