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| 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 |
|---|---|
| ELMs: | MOD_Cter_Amidation |
| Description: | Peptide C-terminal amidation |
| Pattern: | (.)G[RK][RK] (Probability: 0.0011550) |
| Present in taxons: | Metazoa |
| Interaction Domain: |
Cu2_monooxygen (PF01082) |
|
| 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 database of eukaryotic linear motifs (PMID:22110040)