ELM
The Eukaryotic Linear Motif resource for
Functional Sites in Proteins
«MOD_CMANNOS« »MOD_DYRK1A_RPxSP_1»

MOD_Cter_Amidation

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)
o 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.
o 4 GO-Terms:

o No Instance for MOD_Cter_Amidation
Please cite: ELM-the Eukaryotic Linear Motif resource-2024 update. (PMID:37962385)

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