CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
6 | Special |
|
6.10 | Helix non-globular |
|
6.10.250 | Single alpha-helices involved in coiled-coils or other helix-helix interfaces |
|
6.10.250.3320 |
Domain Context
CATH Clusters
| Superfamily | 6.10.250.3320 |
| Functional Family | neuroendocrine convertase 1 |
Enzyme Information
| 3.4.21.93 |
Proprotein convertase 1.
based on mapping to UniProt P63239
Release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.
-!- A calcium dependent enzyme, maximally active at about pH 5.5. -!- Substrates include pro-opiomelanocortin, prorenin, proenkephalin, prodynorphin, prosomatostatin and proinsulin. -!- Unlike prohormone convertase 2, does not cleave proluteinizing- hormone-releasing hormone. -!- Usually processing of prodynorphin occurs at a bond in which P2 is Thr. -!- Present in the regulated secretory pathway of neuroendocrine cells, commonly actin co-operatively with prohormone convertase 2. -!- Belongs to peptidase family S8.
|
UniProtKB Entries (1)
| P63239 |
NEC1_MOUSE
Mus musculus
Neuroendocrine convertase 1
|
PDB Structure
| PDB | 2KDT |
| External Links | |
| Method | SOLUTION NMR |
| Organism | Escherichia |
| Primary Citation |
Functional and structural characterization of a dense core secretory granule sorting domain from the PC1/3 protease.
Proc.Natl.Acad.Sci.USA
|
