A0A8C0RGS4 · A0A8C0RGS4_CANLF
- ProteinPeptidylglycine alpha-amidating monooxygenase
- GenePAM
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids962 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- a [peptide]-C-terminal (2S)-2-hydroxyglycine = a [peptide]-C-terminal amide + glyoxylate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 Cu2+ ions per subunit.
Note: Binds one Zn2+ ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 108 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 109 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 173 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 243 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 245 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 315 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 523 | Ca2+ (UniProtKB | ChEBI); structural | |||
Binding site | 536 | C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI) | |||
Binding site | 588 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 590 | Ca2+ (UniProtKB | ChEBI); structural | |||
Binding site | 657 | C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI) | |||
Binding site | 693 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 709 | C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI) | |||
Binding site | 789 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 790 | Ca2+ (UniProtKB | ChEBI); structural | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | transport vesicle membrane | |
Molecular Function | copper ion binding | |
Molecular Function | L-ascorbic acid binding | |
Molecular Function | lyase activity | |
Molecular Function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen | |
Biological Process | peptide metabolic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Canidae > Canis
Accessions
- Primary accessionA0A8C0RGS4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle, secretory vesicle membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 868-893 | Helical | |||
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-24 | ||||
Chain | PRO_5040636042 | 25-962 | |||
Disulfide bond | 48↔187 | ||||
Disulfide bond | 82↔127 | ||||
Disulfide bond | 115↔132 | ||||
Disulfide bond | 228↔335 | ||||
Disulfide bond | 294↔316 | ||||
Disulfide bond | 637↔658 | ||||
Disulfide bond | 705↔716 | ||||
Glycosylation | 768 | N-linked (GlcNAc...) asparagine | |||
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, repeat, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 66-177 | Copper type II ascorbate-dependent monooxygenase N-terminal | |||
Domain | 202-346 | Copper type II ascorbate-dependent monooxygenase C-terminal | |||
Repeat | 573-614 | NHL | |||
Repeat | 623-668 | NHL | |||
Repeat | 676-720 | NHL | |||
Repeat | 772-815 | NHL | |||
Region | 925-962 | Disordered | |||
Sequence similarities
In the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family.
In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length962
- Mass (Da)106,864
- Last updated2022-01-19 v1
- MD5 Checksum8818E6FCFEBBB9BB8E0F222C9DC1BAF6