Detail Information for IndEnz0002001455
IED ID IndEnz0002001455
Enzyme Type ID protease001455
Protein Name Proteinase-activated receptor 3
PAR-3
Coagulation factor II receptor-like 2
Thrombin receptor-like 2
Gene Name F2RL2 PAR3
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 MKALIFAAAGLLLLLPTFCQSGMENDTNNLAKPTLPIKTFRGAPPNSFEEFPFSALEGWTGATITVKIKCPEESASHLHVKNATMGYLTSSLSTKLIPAIYLLVFVVGVPANAVTLWMLFFRTRSICTTVFYTNLAIADFLFCVTLPFKIAYHLNGNNWVFGEVLCRATTVIFYGNMYCSILLLACISINRYLAIVHPFTYRGLPKHTYALVTCGLVWATVFLYMLPFFILKQEYYLVQPDITTCHDVHNTCESSSPFQLYYFISLAFFGFLIPFVLIIYCYAAIIRTLNAYDHRWLWYVKASLLILVIFTICFAPSNIILIIHHANYYYNNTDGLYFIYLIALCLGSLNSCLDPFLYFLMSKTRNHSTAYLTK
Enzyme Length 374
Uniprot Accession Number O00254
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. {ECO:0000269|PubMed:10079109}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Chain (1); Disulfide bond (1); Frameshift (1); Glycosylation (3); Mutagenesis (2); Natural variant (3); Propeptide (1); Signal peptide (1); Site (1); Topological domain (8); Transmembrane (7)
Keywords Alternative splicing;Blood coagulation;Cell membrane;Disulfide bond;G-protein coupled receptor;Glycoprotein;Hemostasis;Membrane;Receptor;Reference proteome;Signal;Transducer;Transmembrane;Transmembrane helix
Interact With P16333
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Modified Residue
Post Translational Modification PTM: A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10191087; 12805069; 14507634; 14515192; 14528298; 15504554; 15582715; 15850610; 16046705; 16102047; 1672265; 16754659; 17235357; 17347481; 17376866; 17474147; 18264801; 18577758; 18836030; 1905813; 19379695; 19473969; 19513616; 19586901; 19718071; 19806263; 19913121; 20155436; 20235792; 20390230; 20442298; 20454680; 20628086; 20930172; 21596928; 22541814; 23739922; 23921961; 24699825; 25320242; 26729042; 26742564; 3086311; 8290554; 8615752; 8664309; 873923; 8982657; 9618465;
Motif
Gene Encoded By
Mass 42,508
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda