THBD
The protein encoded by this intronless gene is an endothelial-specific type I membrane receptor that binds thrombin. This binding results in the activation of protein C, which degrades clotting factors Va and VIIIa and reduces the amount of thrombin generated. Mutations in this gene are a cause of thromboembolic disease, also known as inherited thrombophilia. [provided by RefSeq, Jul 2008]
Full Name
THBD Gene(Protein Coding) Thrombomodulin
Function
Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va and factor VIIIa, and thereby reduces the amount of thrombin generated.
Biological Process
Biological Process blood coagulationSource:ProtInc1 Publication
Biological Process blood coagulation, common pathwaySource:ComplexPortal1 Publication
Biological Process female pregnancySource:Ensembl
Biological Process negative regulation of blood coagulationSource:BHF-UCL1 Publication
Biological Process negative regulation of fibrinolysisSource:BHF-UCL1 Publication
Biological Process negative regulation of platelet activationSource:BHF-UCL1 Publication
Biological Process proteolysisSource:ComplexPortal1 Publication
Biological Process response to cAMPSource:Ensembl
Biological Process response to lipopolysaccharideSource:Ensembl
Biological Process response to X-raySource:Ensembl
Biological Process zymogen activationSource:ComplexPortal1 Publication
Cellular Location
Membrane
Involvement in disease
Thrombophilia due to thrombomodulin defect (THPH12):
A hemostatic disorder characterized by a tendency to thrombosis.
Hemolytic uremic syndrome atypical 6 (AHUS6):
An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease.
Topology
Extracellular: 19-515
Helical: 516-539
Cytoplasmic: 540-575
PTM
N-glycosylated.
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
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Datasheet