Pam Gene Summary [Mouse]
Predicted to enable several functions, including metal ion binding activity; peptidylamidoglycolate lyase activity; and peptidylglycine monooxygenase activity. Predicted to be involved in several processes, including fatty acid primary amide biosynthetic process; peptide amidation; and response to zinc ion. Predicted to be located in several cellular components, including perikaryon; secretory granule membrane; and trans-Golgi network. Predicted to be active in extracellular region. Is expressed in several structures, including alimentary system; central nervous system; forelimb bud; limb interdigital region; and sensory organ. Orthologous to human PAM (peptidylglycine alpha-amidating monooxygenase). [provided by Alliance of Genome Resources, Apr 2025]
Details
| Type | Protein Coding |
| Official Symbol | Pam |
| Official Name | peptidylglycine alpha-amidating monooxygenase [Source:MGI Symbol;Acc:MGI:97475] |
| Ensembl ID | ENSMUSG00000026335 |
| Bio databases IDs | |
| Aliases | peptidylglycine alpha-amidating monooxygenase |
| Synonyms | LOC102553671, PAL, PAM-1, peptidylglycine alpha-amidating monooxygenase, peptidylglycine α-amidating monooxygenase, PHM |
| Species | Mouse, Mus musculus |
| Orthologies |
Protein Domains
A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in mouse Pam often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- Copper type II ascorbate-dependent monooxygenase, C-terminal domain
- protein kinase binding
- signal response domain
- calcium ion binding
- chromatin binding
- enzyme
- protein binding
- NHL repeat unit of beta-propeller proteins
- identical protein binding
- peptidylamidoglycolate lyase
- internalization targeting signal
- copper ion binding
- cytoplasmic domain
- zinc ion binding
- peptidylglycine monooxygenase
- NHL repeat
- lumenal domain
- transmembrane domain
- Copper type II ascorbate-dependent monooxygenase, N-terminal domain
- pro domain
- targeting signal
Top Findings
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
disease
- non-insulin-dependent diabetes mellitus
- diabetic retinopathy
- insomnia
- COVID-19
- systemic lupus erythematosus
- obesity
- diabetes mellitus
- androgenic alopecia
- acute myeloid leukemia
- edema
role in cell
- expression in
- production in
- accumulation in
- morphology
- response
- formation
- organization
- branching
Subcellular Expression
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
- Plasma Membrane
- soluble fraction
- membrane fraction
- Cytoplasm
- cell surface
- Golgi region
- Extracellular Space
- perinuclear region
- cellular membrane
- endosomes
- vesicles
- secretory granule membrane
- cytosol
- trans Golgi network
- chromosome
- perinuclear vesicles
- secretory granules
- chromatin
- perikaryon
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the mouse Pam gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- response to zinc ion
- peptide amidation
Cellular Component
Where in the cell the gene product is active
- secretory granule membrane
- extracellular vesicular exosome
- transport vesicle membrane
- membrane
- extracellular region
Molecular Function
What the gene product does at the molecular level
- L-ascorbic acid binding
- zinc ion binding
- peptidylglycine monooxygenase activity
- protein binding
- copper ion binding
- calcium ion binding
- peptidylamidoglycolate lyase activity