PRTN3

Myeloblastin

256 amino acids

Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro) (PubMed:3198760, PubMed:2033050, PubMed:28240246). By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration (PubMed:23202369). May play a role in neutrophil transendothelial migration, probably when associated with CD177 (PubMed:22266279).

Belongs to the peptidase S1 family. Elastase subfamily.

27.807 kDa

MAHRPPSPALASVLLALLLSGAARAAEIVGGHEAQPHSRPYMASLQMRGNPGSHFCGGTLIHPSFVLTAAHCLRDIPQRLVNVVLGAHNVRTQEPTQQHFSVAQVFLNNYDAENKLNDVLLIQLSSPANLSASVATVQLPQQDQPVPHGTQCLAMGWGRVGAHDPPAQVLQELNVTVVTFFCRPHNICTFVPRRKAGICFGDSGGPLICDGIIQGIDSFVIWGCATRLFPDFFTRVALYVDWIRSTLRRVEAKGRP

Prtn3

Myeloblastin

254 amino acids

Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro). By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration. May play a role in neutrophil transendothelial migration, probably when associated with CD177.

Belongs to the peptidase S1 family. Elastase subfamily.

27.626 kDa

MSGSYPSPKGIHPFLLLALVVGGAVQASKIVGGHEARPHSRPYVASLQLSRFPGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLLSSEPEQQKFTISQVFQNNYNPEENLNDVLLLQLNRTASLGKEVAVASLPQQDQTLSQGTQCLAMGWGRLGTQAPTPRVLQELNVTVVTFLCREHNVCTLVPRRAAGICFGDSGGPLICNGILHGVDSFVIRECASLQFPDFFARVSMYVDWIQNVLRGAEP