PAM — Peptidylglycine alpha-amidating monooxygenase
PAM belongs to a gene co-expression module in 4 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
PAM's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| CD4⁺ T cells | Vesicle Trafficking Signaling Housekeeping | ANK1, ANKRA2, B3GALNT2, C1orf216, C22orf39, CASC3, CCDC71L, CD80 +21 more | View in SCUBA |
| Lymphatic endothelial | Focal Adhesion Migration migration & adhesion | BIRC6, CDC42BPA, DOCK1, EIF4G3, GNAQ, LPP, NF1, PTK2 +2 more | View in SCUBA |
| Neutrophils | Neutrophil Differentiation Developmental | DACH1, DGKD, FAR1, MPP7, MSRA, PLCL2, PTBP2, RELL1 +1 more | |
| Smooth muscle cells | ER-Golgi Secretory Pathway Protein processing & ER | BZW1, CCT3, COL15A1, GPC6, IFT57, KDELR2, LRPAP1, NFATC4 +4 more | View in SCUBA |
About the gene
| Synonyms | PAL, PHM |
|---|---|
| Chromosome | 5: 102753981-103029730 |
| Predicted location | Intracellular, Membrane, Secreted |
| Essential gene | No |
| Protein class | Enzymes, Metabolic proteins, Plasma proteins, Predicted intracellular proteins, Predicted membrane proteins, Predicted secreted proteins |
| Molecular function | Lyase, Monooxygenase, Multifunctional enzyme, Oxidoreductase |
| Biological process | Lipid metabolism |
Function
Bifunctional enzyme that catalyzes amidation of the C- terminus of proteins. Alpha-amidation is present at the C-terminus of many endocrine hormones and neuropeptides and is required for their activity. C- terminal amidation also takes place in response to protein fragmentation triggered by oxidative stress, promoting degradation of amidated protein fragments by the proteasome. Alpha- amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. The first step, catalyzed by peptidyl alpha- hydroxylating monooxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate. The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc- dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate. Similarly, catalyzes the two- step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity).
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.