Names & Taxonomy
- Uniprot ID:
- P19021
- Entry Name:
- AMD_HUMAN
- Status:
- reviewed
- Protein Names:
- Peptidyl-glycine alpha-amidating monooxygenase (PAM) [Includes: Peptidylglycine alpha-hydroxylating monooxygenase (PHM) (EC 1.14.17.3); Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (EC 4.3.2.5) (Peptidylamidoglycolate lyase) (PAL)]
- Gene Names:
- PAM
- Gene Names Primary:
- PAM
- Organism:
- Homo sapiens (Human)
Structure
- Length:
- 973
- Sequence:
- MAGRVPSLLVLLVFPSSCLAFRSPLSVFKRFKETTRPFSNECLGTTRPVVPIDSSDFALDIRMPGVTPKQSDTYFCMSMRIPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNNKDCSGVSLHLTRLPQPLIAGMYLMMSVDTVIPAGEKVVNSDISCHYKNYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVGHPVDVSFGDLLAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDMFRTIPPEANIPIPVKSDMVMMHEHHKETEYKDKIPLLQQPKREEEEVLDQGDFYSLLSKLLGEREDVVHVHKYNPTEKAESESDLVAEIANVVQKKDLGRSDAREGAEHERGNAILVRDRIHKFHRLVSTLRPPESRVFSLQQPPPGEGTWEPEHTGDFHMEEALDWPGVYLLPGQVSGVALDPKNNLVIFHRGDHVWDGNSFDSKFVYQQIGLGPIEEDTILVIDPNNAAVLQSSGKNLFYLPHGLSIDKDGNYWVTDVALHQVFKLDPNNKEGPVLILGRSMQPGSDQNHFCQPTDVAVDPGTGAIYVSDGYCNSRIVQFSPSGKFITQWGEESSGSSPLPGQFTVPHSLALVPLLGQLCVADRENGRIQCFKTDTKEFVREIKHSSFGRNVFAISYIPGLLFAVNGKPHFGDQEPVQGFVMNFSNGEIIDIFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLTEKLEHRSVKKAGIEVQEIKEAEAVVETKMENKPTSSELQKMQEKQKLIKEPGSGVPVVLITTLLVIPVVVLLAIAIFIRWKKSRAFGDSEHKLETSSGRVLGRFRGKGSGGLNLGNFFASRKGYSRKGFDRLSTEGSDQEKEDDGSESEEEYSAPLPALAPSSS
- Proteomes:
- UP000005640
Subcellular location
- Subcellular Location:
- Isoform 1: Membrane; Single-pass type I membrane protein.; Isoform 2: Membrane; Single-pass type I membrane protein.; Isoform 3: Secreted. Note=Secreted from secretory granules.; Isoform 4: Secreted. Note=Secreted from secretory granules.
Function
- Function:
- Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
- Catalytic Activity:
- Peptidylglycine + ascorbate + O(2) = peptidyl(2-hydroxyglycine) + dehydroascorbate + H(2)O.; Peptidylamidoglycolate = peptidyl amide + glyoxylate.
- Cofactor:
- COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
- Enzyme Regulation:
- ENZYME REGULATION: Inhibited by EDTA, phenylglyoxal and diethyl pyrocarbonate.
- Cross Reference Drug Bank:
- DB00126
- Gene Ontology Go:
- cell surface
extracellular exosome
extracellular space
integral component of membrane
membrane
neuron projection
perikaryon
perinuclear region of cytoplasm
plasma membrane
secretory granule membrane
trans-Golgi network
calcium ion binding
copper ion binding
L-ascorbic acid binding
peptidylamidoglycolate lyase activity
peptidylglycine monooxygenase activity
zinc ion binding
central nervous system development
heart development
lactation
limb development
long-chain fatty acid metabolic process
maternal process involved in female pregnancy
odontogenesis
ovulation cycle process
peptide amidation
protein amidation
protein homooligomerization
regulation of actin cytoskeleton organization
regulation of protein secretion
regulation of transcription from RNA polymerase II promoter
response to copper ion
response to drug
response to estradiol
response to glucocorticoid
response to hypoxia
response to pH
toxin metabolic process - Gene Ontology Biological Process:
- central nervous system development
heart development
lactation
limb development
long-chain fatty acid metabolic process
maternal process involved in female pregnancy
odontogenesis
ovulation cycle process
peptide amidation
protein amidation
protein homooligomerization
regulation of actin cytoskeleton organization
regulation of protein secretion
regulation of transcription from RNA polymerase II promoter
response to copper ion
response to drug
response to estradiol
response to glucocorticoid
response to hypoxia
response to pH
toxin metabolic process - Gene Ontology Molecular Function:
- calcium ion binding
copper ion binding
L-ascorbic acid binding
peptidylamidoglycolate lyase activity
peptidylglycine monooxygenase activity
zinc ion binding - Gene Ontology Cellular Component:
- cell surface
extracellular exosome
extracellular space
integral component of membrane
membrane
neuron projection
perikaryon
perinuclear region of cytoplasm
plasma membrane
secretory granule membrane
trans-Golgi network - Keywords:
- Alternative splicing
Cleavage on pair of basic residues
Complete proteome
Copper
Disulfide bond
Glycoprotein
Lyase
Membrane
Metal-binding
Monooxygenase
Multifunctional enzyme
Oxidoreductase
Phosphoprotein
Polymorphism
Reference proteome
Repeat
Secreted
Signal
Sulfation
Transmembrane
Transmembrane helix
Vitamin C
Zinc