| Accession: | |
|---|---|
| Functional site class: | Peptide Amidation Site |
| Functional site description: | The processing of many secretory peptide hormones includes a cleavage and amidation step generating the C-terminus. |
| ELM Description: | Peptide C-terminal amidation |
| Pattern: | (.)G[RK][RK] |
| Pattern Probability: | 0.0011550 |
| Present in taxon: | Metazoa |
| Interaction Domain: |
Cu2_monooxygen (PF01082)
Copper type II ascorbate-dependent monooxygenase, N-terminal domain
(Stochiometry: 1 : 1)
|
 Abstract |
The enzyme peptidyl-glycine alpha-amidating monooxygenase (PAM) amidates C-termini of secretory peptides at sites approximating XG++. The two positive residues [KR] are targets for a dibasic cleavage enzyme. The G provides the amide group for attachment to residue X (any amino acid), which subsequently becomes the C-terminal residue. The process may occur in a post Golgi compartment. May be restricted to metazoans only. |
4 GO-Terms:
Please cite:
ELM-the Eukaryotic Linear Motif resource-2024 update.
(PMID:37962385)
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement