Pam
entrez
25508
canonical
uniprot
P14925
canonical
ensembl
ENSRNOG00000033280
resolver
ensp
ENSRNOP00000098552
resolver
enst
ENSRNOT00000120994
resolver
genesymbol
Pam
resolver
uniprot
A0ABK0KWC4
resolver
uniprot
P70710
resolver
uniprot
Q64616
resolver
uniprot
Q64668
resolver
uniprot_entry
A0ABK0KWC4_RAT
resolver
uniprot_entry
AMD_RAT
resolver
uniprot_sec
P70710
resolver
uniprot_sec
Q64616
resolver
uniprot_sec
Q64668
resolver
activity_regulation
ACTIVITY REGULATION: PAM activity is inhibited by EDTA, phenylglyoxal and diethyl pyrocarbonate (By similarity). PAL activity is stimulated by cadmium and inhibited by mercury (PubMed:19604476). {ECO:0000250|UniProtKB:P19021, ECO:0000269|PubMed:19604476}.
uniprot
proteins
amino_acid_sequence
MAGRARSGLLLLLLGLLALQSSCLAFRSPLSVFKRFKETTRSFSNECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLTRVPQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFRTIPAEANIPIPVKPDMVMMHGHHKEAENKEKSALMQQPKQGEEEVLEQGDFYSLLSKLLGEREDVHVHKYNPTEKTESGSDLVAEIANVVQKKDLGRSDAREGAEHEEWGNAILVRDRIHRFHQLESTLRPAESRAFSFQQPGEGPWEPEPSGDFHVEEELDWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSKFVYQQRGLGPIEEDTILVIDPNNAEILQSSGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLILGRSMQPGSDQNHFCQPTDVAVEPSTGAVFVSDGYCNSRIVQFSPSGKFVTQWGEESSGSSPRPGQFSVPHSLALVPHLDQLCVADRENGRIQCFKTDTKEFVREIKHASFGRNVFAISYIPGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLTEKMEHRSVKKAGIEVQEIKEAEAVVEPKVENKPTSSELQKMQEKQKLSTEPGSGVSVVLITTLLVIPVLVLLAIVMFIRWKKSRAFGDHDRKLESSSGRVLGRFRGKGSGGLNLGNFFASRKGYSRKGFDRVSTEGSDQEKDEDDGTESEEEYSAPLPKPAPSS
uniprot
proteins
ec_number
1.14.17.3
uniprot
proteins
ec_number
4.3.2.5
uniprot
proteins
function
FUNCTION: Bifunctional enzyme that catalyzes amidation of the C-terminus of proteins (PubMed:10079066, PubMed:36880254, PubMed:7893699). Alpha-amidation is present at the C-terminus of many endocrine hormones and neuropeptides and is required for their activity (By similarity). C-terminal amidation also takes place in response to protein fragmentation triggered by oxidative stress, promoting degradation of amidated protein fragments by the proteasome (By similarity). Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme (PubMed:10079066). 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 (PubMed:10079066). 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 (PubMed:10079066). Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (PubMed:10079066). {ECO:0000250|UniProtKB:P19021, ECO:0000269|PubMed:10079066, ECO:0000269|PubMed:36880254, ECO:0000269|PubMed:7893699}.
uniprot
proteins
mass_dalton
108675
uniprot
proteins
mutagenesis
MUTAGEN 107; /note="H->A: Impaired Cu(2+)-binding."; /evidence="ECO:0000269|PubMed:30271955"; MUTAGEN 108; /note="H->A: Impaired Cu(2+)-binding; forms a closed conformer in the presence of citrate with a reduced Cu(2+)-Cu(2+) site separation of 4 Angstroms. Abolished peptidylglycine alpha-hydroxylating monooxygenase activity."; /evidence="ECO:0000269|PubMed:30271955, ECO:0000269|PubMed:7893699"; MUTAGEN 172; /note="H->A: Impaired Cu(2+)-binding."; /evidence="ECO:0000269|PubMed:30271955"; MUTAGEN 244; /note="H->A: Abolished peptidylglycine alpha-hydroxylating monooxygenase activity."; /evidence="ECO:0000269|PubMed:7893699"; MUTAGEN 272; /note="Q->E,A: Induces a fully open peptidylglycine monooxygenase structure with Cu(2+) distances of 14 Angstroms."; /evidence="ECO:0000269|PubMed:36880254"; MUTAGEN 314; /note="M->I: Abolished peptidylglycine alpha-hydroxylating monooxygenase activity."; /evidence="ECO:0000269|PubMed:7893699"; MUTAGEN 533; /note="R->A: Abolishes peptidyl-alpha-hydroxyglycine alpha-amidating lyase activity."; /evidence="ECO:0000269|PubMed:19604476"; MUTAGEN 533; /note="R->Q: Abolishes peptidyl-alpha-hydroxyglycine alpha-amidating lyase activity."; /evidence="ECO:0000269|PubMed:19604476"; MUTAGEN 706; /note="R->A: Abolishes peptidyl-alpha-hydroxyglycine alpha-amidating lyase activity."; /evidence="ECO:0000269|PubMed:19604476"; MUTAGEN 706; /note="R->Q: Reduces peptidyl-alpha-hydroxyglycine alpha-amidating lyase activity."; /evidence="ECO:0000269|PubMed:19604476"; MUTAGEN 784; /note="M->A: Abolishes peptidyl-alpha-hydroxyglycine alpha-amidating lyase activity."; /evidence="ECO:0000269|PubMed:19604476"; MUTAGEN 784; /note="M->Q: Abolishes peptidyl-alpha-hydroxyglycine alpha-amidating lyase activity."; /evidence="ECO:0000269|PubMed:19604476"; MUTAGEN 787; /note="D->A: Reduces peptidyl-alpha-hydroxyglycine alpha-amidating lyase activity."; /evidence="ECO:0000269|PubMed:19604476
uniprot
proteins
protein_family
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase family; Copper type II ascorbate-dependent monooxygenase family
uniprot
proteins
pubmed
10079066
uniprot
proteins
pubmed
10504734
uniprot
proteins
pubmed
12369828
uniprot
proteins
pubmed
1448112
uniprot
proteins
pubmed
15131304
uniprot
proteins
pubmed
16100265
uniprot
proteins
pubmed
1740449
uniprot
proteins
pubmed
19604476
uniprot
proteins
pubmed
1988445
uniprot
proteins
pubmed
20958070
uniprot
proteins
pubmed
2211657
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
23247335
uniprot
proteins
pubmed
2337358
uniprot
proteins
pubmed
2401356
uniprot
proteins
pubmed
2911604
uniprot
proteins
pubmed
30271955
uniprot
proteins
pubmed
36880254
uniprot
proteins
pubmed
7893699
uniprot
proteins
pubmed
9837933
uniprot
proteins
sequence_length
976
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P10731}; Single-pass membrane protein {ECO:0000250|UniProtKB:P10731}. Note=Secretory granules. {ECO:0000250|UniProtKB:P10731}.; SUBCELLULAR LOCATION: [Isoform PAM-1]: Membrane {ECO:0000305|PubMed:2401356}.; SUBCELLULAR LOCATION: [Isoform PAM-2]: Membrane {ECO:0000305|PubMed:2401356}.; SUBCELLULAR LOCATION: [Isoform PAM-3]: Secreted {ECO:0000305|PubMed:2401356}.; SUBCELLULAR LOCATION: [Isoform PAM-3A]: Secreted {ECO:0000305|PubMed:2401356}.; SUBCELLULAR LOCATION: [Isoform PAM-3B]: Membrane {ECO:0000305|PubMed:2401356}.; SUBCELLULAR LOCATION: [Isoform PAM-4]: Secreted {ECO:0000305|PubMed:2401356}.; SUBCELLULAR LOCATION: [Isoform PAM-5]: Secreted {ECO:0000305|PubMed:2401356}.
uniprot
proteins
transmembrane_region
TRANSMEM 867..890; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins