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Sirtilin protease specificity - Sirtilins - the new old members of the vitamin K-dependent coagulation factor family

ABSTRACT: Here we describe an additional member of the Vitamin K-dependent protease family comprising the Gla-EGF1-EGF2-SP domain architecture. These proteases were found in different vertebrate classes including jawless fish, cartilaginous fish, bony fish, reptiles, birds and marsupials but not in other mammals. We have investigated for the first time the homolog of the garter snake Thamnophis sirtalis and thus called these proteases ‘sirtilins’.

INSTRUMENT(S): maXis

ORGANISM(S): Escherichia Coli

SUBMITTER: Fatih Demir

LAB HEAD: Pitter Florian Huesgen

PROVIDER: PXD010679 | Pride | 2019-02-22

REPOSITORIES: Pride

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			Action	DRS
	171110Svenf9LikePICSGluC1_GC3_01_4930.d.zip	Other
	171110Svenf9LikePICSGluC2_GC3_01_4931.d.zip	Other
	171110Svenf9LikePICSLegu1_GC6_01_4938.d.zip	Other
	171110Svenf9LikePICSLegu2_GC6_01_4939.d.zip	Other
	171110SvenhF10aPICSGluC1_GC2_01_4927.d.zip	Other

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Sirtilins - the new old members of the vitamin K-dependent coagulation factor family.

Dahms Sven O SO Demir Fatih F Huesgen Pitter F PF Thorn Karina K Brandstetter Hans H

Journal of thrombosis and haemostasis : JTH 20190213 3

Essentials Blood coagulation is driven by vitamin K (VK)-dependent proteases. We have identified and characterized 'sirtilin' as an additional VK-dependent protease. Sirtilins emerged early in the evolution of the coagulation system of vertebrates. Ubiquitous occurrence might indicate an important functional role of sirtilins. SUMMARY: Background Vitamin K (VK)-dependent proteases are major players in blood coagulation, including both the initiation and the regulation of the cascade. Five differ ...[more]

PMID: 30644641

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