Detail Information for IndEnz0002009618
IED ID IndEnz0002009618
Enzyme Type ID protease009618
Protein Name Proteinase-activated receptor 1
PAR-1
Coagulation factor II receptor
Thrombin receptor
Gene Name F2R CF2R PAR1 TR
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MGPRRLLLVAACFSLCGPLLSARTRARRPESKATNATLDPRSFLLRNPNDKYEPFWEDEEKNESGLTEYRLVSINKSSPLQKQLPAFISEDASGYLTSSWLTLFVPSVYTGVFVVSLPLNIMAIVVFILKMKVKKPAVVYMLHLATADVLFVSVLPFKISYYFSGSDWQFGSELCRFVTAAFYCNMYASILLMTVISIDRFLAVVYPMQSLSWRTLGRASFTCLAIWALAIAGVVPLLLKEQTIQVPGLNITTCHDVLNETLLEGYYAYYFSAFSAVFFFVPLIISTVCYVSIIRCLSSSAVANRSKKSRALFLSAAVFCIFIICFGPTNVLLIAHYSFLSHTSTTEAAYFAYLLCVCVSSISCCIDPLIYYYASSECQRYVYSILCCKESSDPSSYNSSGQLMASKMDTCSSNLNNSIYKKLLT
Enzyme Length 425
Uniprot Accession Number P25116
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development. {ECO:0000269|PubMed:10079109}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (3); Chain (1); Disulfide bond (1); Glycosylation (5); Helix (13); Modified residue (1); Mutagenesis (1); Natural variant (6); Propeptide (1); Sequence conflict (2); Signal peptide (1); Site (2); Topological domain (8); Transmembrane (7); Turn (2)
Keywords 3D-structure;Blood coagulation;Cell membrane;Disulfide bond;G-protein coupled receptor;Glycoprotein;Hemostasis;Membrane;Phosphoprotein;Receptor;Reference proteome;Signal;Transducer;Transmembrane;Transmembrane helix
Interact With Q03135; Q9UNN8
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Modified Residue MOD_RES 418; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163
Post Translational Modification PTM: Proteolytic cleavage by thrombin generates a new N-terminus that functions as a tethered ligand (PubMed:1672265, PubMed:7744748). Also proteolytically cleaved by cathepsin CTSG (PubMed:7744748). Cleavage at 41-Arg-|-Ser-42 by CTSG results in receptor activation while cleavage at 55-Phe-|-Trp-56 results in inhibition of receptor activation (PubMed:7744748). {ECO:0000269|PubMed:1672265, ECO:0000269|PubMed:7744748}.; PTM: Phosphorylated in the C-terminal tail; probably mediating desensitization prior to the uncoupling and internalization of the receptor. {ECO:0000269|PubMed:8955127}.
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000269|PubMed:22659187
Structure 3D X-ray crystallography (10)
Cross Reference PDB 1NRN; 1NRO; 1NRP; 1NRQ; 1NRR; 3BEF; 3HKI; 3HKJ; 3LU9; 3VW7;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 47,441
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda