Detail Information for IndEnz0002012235
IED ID IndEnz0002012235
Enzyme Type ID protease012235
Protein Name Tissue factor
TF
Coagulation factor III
CD antigen CD142
Gene Name F3 Cf3
Organism Rattus norvegicus (Rat)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat)
Enzyme Sequence MAIPMRPRLLAALAPTFLGFLLLQVAVGAGTPPGKAFNLTWISTDFKTILEWQPKPTNYTYTVQISDRSRNWKYKCTGTTDTECDLTDEIVKDVNWTYEARVLSVPWRNSTHGKETLFGTHGEEPPFTNARKFLPYRDTKIGQPVIQKYEQGGTKLKVTVKDSFTLVRKNGTFLTLRQVFGNDLGYILTYRKDSSTGRKTNTTHTNEFLIDVEKGVSYCFFAQAVIFSRKTNHKSPESITKCTEQWKSVLGETLIIVGAVVFLVTVFIILLTISLCKRRKNRAGQKRKNTPSRLA
Enzyme Length 295
Uniprot Accession Number P42533
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited proteolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Disulfide bond (2); Glycosylation (6); Lipidation (1); Motif (1); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords Blood coagulation;Disulfide bond;Glycoprotein;Hemostasis;Lipoprotein;Membrane;Palmitate;Reference proteome;Signal;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P13726}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P13726}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..28; /evidence=ECO:0000250
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10190887; 10780328; 10840019; 11750579; 12083485; 15293323; 15481788; 16113797; 16902157; 18315926; 19458308; 21229253; 21396682; 21423288; 21964405; 22140576; 24831016; 25772383; 25883098; 26311287; 26370456; 9426395; 9875493; 9916935; 9974408;
Motif MOTIF 246..248; /note=WKS motif
Gene Encoded By
Mass 33,444
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda