Search results for SERPIND1

Showing 6 results out of 6

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Species

Types

Compartments

Reaction types

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Protein (3 results from a total of 3)

Identifier: R-HSA-5578885
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: SERPIND1: P05546
Identifier: R-HSA-8956731
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: SERPIND1: P05546
Identifier: R-HSA-8956982
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: SERPIND1: P05546

Complex (1 results from a total of 1)

Identifier: R-HSA-5578881
Species: Homo sapiens
Compartment: extracellular region

Reaction (1 results from a total of 1)

Identifier: R-HSA-5578883
Species: Homo sapiens
Compartment: extracellular region
SERPIND1 (Heparin cofactor 2) is a serine endopeptidase inhibitor (SERPIN) that acts as a pseudosubstrate for activated thrombin, forming a stable complex which has the effect of inactivating thrombin protease activity (Church et al. 1985), although with slower kinetics than SERPINC1 (antithrombin-III). The presence of the glycosaminoglycans heparin or dermatan sulphate increases thrombin inactivation 1000-fold (Van Deerlin & Tollefsen 199) by facilitating the interaction between the active site of thrombin and the reactive site of SERPIND1. Thrombin specificity is conferred by a 90-residue N-terminal extension that contains two acidic motifs containing sulphated Tyr residues, resembling the C-terminus of hirudin (Tollefsen et al. 1997). SERPIND1 also inhibits chymotrypsin and neutrophil cathepsin G, but in a glycosaminoglycan independent manner (Church et al. 1985). In contrast to SERPINC1 deficiency, SERPIND1 deficiency is not associated with venous thrombosis (Corral et al. 2004).

Pathway (1 results from a total of 1)

Identifier: R-HSA-140875
Species: Homo sapiens
Compartment: extracellular region
The common pathway consists of the cascade of activation events leading from the formation of activated factor X to the formation of active thrombin, the cleavage of fibrinogen by thrombin, and the formation of cleaved fibrin into a stable multimeric, cross-linked complex. Thrombin also efficiently catalyzes the activation of several factors required earlier in the clotting cascade, thus acting in effect as a positive regulator of clotting. At the same time, thrombin activates protein C, which in turn catalyzes the inactivation of several of these upstream factors, thereby limiting the clotting process. Thrombin can be trapped in stable, inactive complexes with: antithrombin-III (SERPINC1), a circulating blood protein; heparin cofactor II (SERPIND1) which inhibits thrombin in a dermatan sulfate–dependent manner in the arterial vasculature; protein C inhibitor (SERPINA5) that inhibits thrombin in complex with thrombomodulin; and Protease nexin-1 (SERPINE2) that inhibits thrombin at the vessel wall and platelet surface. The quantitative interplay among these positive and negative modulators is critical to the normal regulation of clotting, facilitating the rapid formation of a protective clot at the site of injury, while limiting and physically confining the process.
These events are outlined in the drawing: black arrows connect the substrates (inputs) and products (outputs) of individual reactions, and blue lines connect output activated enzymes to the other reactions that they catalyze.
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