calpain-8; stomach-specific M-type calpain; new calpain 2; nCL-2 (CAPN8, NCL2)
Jump to navigation
Jump to search
Function
- Ca+2-regulated non-lysosomal thiol-protease
- involved in membrane trafficking in gastric surface mucus cells (pit cells) & may involve the membrane trafficking of mucus cells via interactions with coat protein
- proteolytically cleaves the beta-subunit of coatomer complex (putative)
- undergoes autolytic cleavage between Ala-5 & Ala-6 which gives rise to fragments extending from Ala-6 to the C-terminus, Ala-6 to the EF-hand 2 domain & from Ala-6 to the beginning of domain III (putative)
- broad endopeptidase specificity
- interacts with GPS1, COPB1, EYA2, NME2, NME4 & TOMM70A (putative)
Cofactor: binds 2 Ca+2 (putative)
Structure
- monomer & homoligomer
- domain III mediates oligomerization (putative)
- belongs to the peptidase C2 family
- contains 1 calpain catalytic domain
- contains 3 EF-hand domains