LC2

Snaclec coagulation factor X-activating enzyme light chain 2

158 amino acids

Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner.

Belongs to the snaclec family.

18.337 kDa

MGRFISVSFGLLVVFLSLSGTGAGLDCPPDSSLYRYFCYRVFKEHKTWEAAERFCMEHPNNGHLVSIESMEEAEFVAKLLSNTTGKFITHFWIGLMIKDKEQECSSEWSDGSSVSYDKLGKQEFRKCFVLEKESGYRMWFNRNCEERYLFVCKVPPEC

LC2

Snaclec coagulation factor X-activating enzyme light chain 2

158 amino acids

Regulatory subunit of the blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond at position 234, activates coagulation factor IX (F9) by cleaving the Arg-Val bond at position 226 and is also able to activate protein C (PROC). May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) in a calcium-dependent manner.

Belongs to the snaclec family.

18.094 kDa

MGRSISVSFGLLAVFLSLSGTGAGLDCPPDSSPYRYFCYRVFKEQKNWADAERFCAERPNNGHLVSIESMEEAEFVAQLLSKITGKFITHFWIGLRIEDKKQQCRSEWSDGSSVSYDNLLKREFRKCFGLEKGTGYRSWFNLNCEEPYPFVCKVPPNC

LC2

Snaclec factor X-activator 2 light chain 2

16 amino acids

Regulatory subunit of the blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) in a calcium-dependent manner by cleaving the Arg-Ile bond at position 234. Weakly hydrolyzes insulin B chain, fibrinogen and some components of the extracellular matrix in vitro, but does not activate prothrombin or plasminogen.

Belongs to the snaclec family.

1.815 kDa

single

AFCCPSGWSAYDQNCY

LC2

Snaclec factor X-activator 1 light chain 2

11 amino acids

Regulatory subunit of the blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) in a calcium-dependent manner by cleaving the Arg-Ile bond at position 234. Weakly hydrolyzes insulin B chain, fibrinogen and some components of the extracellular matrix in vitro, but does not activate prothrombin or plasminogen.

Belongs to the snaclec family.

1.273 kDa

single

LFDPPDSXPXY