A0A5F8H1V1 · A0A5F8H1V1_MONDO
- ProteinPeptidylglycine alpha-amidating monooxygenase
- GenePAM
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids908 (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 | 103 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 104 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 168 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 238 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 240 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 310 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 517 | Ca2+ (UniProtKB | ChEBI); structural | |||
Binding site | 530 | C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI) | |||
Binding site | 582 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 584 | Ca2+ (UniProtKB | ChEBI); structural | |||
Binding site | 651 | C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI) | |||
Binding site | 687 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 703 | C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI) | |||
Binding site | 783 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 784 | 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 | peptidylamidoglycolate lyase activity | |
Molecular Function | peptidylglycine monooxygenase activity | |
Biological Process | peptide metabolic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Metatheria > Didelphimorphia > Didelphidae > Monodelphis
Accessions
- Primary accessionA0A5F8H1V1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle, secretory vesicle membrane ; Single-pass membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-21 | ||||
Chain | PRO_5023889420 | 22-908 | |||
Disulfide bond | 43↔182 | ||||
Disulfide bond | 77↔122 | ||||
Disulfide bond | 110↔127 | ||||
Disulfide bond | 223↔330 | ||||
Disulfide bond | 289↔311 | ||||
Disulfide bond | 631↔652 | ||||
Disulfide bond | 699↔710 | ||||
Keywords
- PTM
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, repeat.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 61-172 | Copper type II ascorbate-dependent monooxygenase N-terminal | |||
Domain | 197-341 | Copper type II ascorbate-dependent monooxygenase C-terminal | |||
Region | 466-491 | Disordered | |||
Compositional bias | 472-487 | Polar residues | |||
Repeat | 567-608 | NHL | |||
Repeat | 617-662 | NHL | |||
Repeat | 680-714 | NHL | |||
Repeat | 766-809 | NHL | |||
Region | 869-908 | 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
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length908
- Mass (Da)101,323
- Last updated2019-12-11 v1
- MD5 Checksum886DB2D265942E163D03090F9A1F1CE4
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F6SHA5 | F6SHA5_MONDO | PAM | 976 | ||
A0A5F8G7D0 | A0A5F8G7D0_MONDO | PAM | 818 | ||
A0A5F8G7W8 | A0A5F8G7W8_MONDO | PAM | 870 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 472-487 | Polar residues | |||
Keywords
- Technical term