Pam
entrez
18484
canonical
uniprot
P97467
canonical
ensembl
ENSMUSG00000026335
resolver
ensp
ENSMUSP00000057112
resolver
ensp
ENSMUSP00000095228
resolver
ensp
ENSMUSP00000125418
resolver
ensp
ENSMUSP00000319544
resolver
ensp
ENSMUSP00000319545
resolver
ensp
ENSMUSP00000319546
resolver
ensp
ENSMUSP00000319547
resolver
ensp
ENSMUSP00000319548
resolver
ensp
ENSMUSP00000319549
resolver
ensp
ENSMUSP00000319550
resolver
ensp
ENSMUSP00000319551
resolver
ensp
ENSMUSP00000319552
resolver
ensp
ENSMUSP00000319553
resolver
ensp
ENSMUSP00000319555
resolver
ensp
ENSMUSP00000319564
resolver
ensp
ENSMUSP00000319567
resolver
ensp
ENSMUSP00000319568
resolver
ensp
ENSMUSP00000319569
resolver
enst
ENSMUST00000058762
resolver
enst
ENSMUST00000097625
resolver
enst
ENSMUST00000161567
resolver
genesymbol
Pam
resolver
uniprot
A1L331
resolver
uniprot
E9Q704
resolver
uniprot
E9QL07
resolver
uniprot
F8VQA4
resolver
uniprot_entry
A1L331_MOUSE
resolver
uniprot_entry
AMD_MOUSE
resolver
uniprot_entry
E9Q704_MOUSE
resolver
uniprot_entry
F8VQA4_MOUSE
resolver
uniprot_sec
E9QL07
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 (By similarity). {ECO:0000250|UniProtKB:P14925, ECO:0000250|UniProtKB:P19021}.
uniprot
proteins
amino_acid_sequence
MAGRARSRLLLLLGLLALQSSCLAFRSPLSVFKRFKETTRSFSNECLGTTRPITPIDSSDFTLDIRMPGVTPKESDTYFCMSMRLPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSLHLTRVPQPLIAGMYLMMSVNTVIPPGEKVVNSDISCHYKMYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVEHPVDVAFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDMFRTIPEEANIPIPVKSDMVMIHGHHKETENKEKSALIQQPKQGEEEAFEQGDFYSLLSKLLGEREDVVHVHKYNPTEKTESGSDLVAEIANVVQKKDLGRSDAREGAEHEEGGNAILVRDRIHKFHRLESTLRPAESRALSFQQPGEGPWEPELAGDFHVEEALEWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSKFVYQQRGLGPIEEDTILVIDPNKAEILQSSGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLVLGRSMQPGSDQNHFCQPTDVAVEPSTGAVFVSDGYCNSRIVQFSPSGKFITQWGEESSGSSPKPGQFSVPHSLALVPHLNQLCVADRENGRIQCFKTDTKEFVREIKHASFGRNVFAISYIPGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLTESRLEVEHRSVKKAGIEVPEIKEAEAVVEPKVKNKPTSSELQKMQEKKKLIKDPGSGVPVVLITTLLVIPVVVLLAIAMFIRWKKSRAFGDHDRKLESSSGRVLGRLRGKGSSGLNLGNFFASRKGYSRKGFDRVSTEGSDQEKDEDDGSESEEEYSAPLPTPAPSS
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:9562574, PubMed:16225857). Alpha-amidation is present at the C-terminus of many endocrine hormones and neuropeptides and is required for their activity (PubMed:9562574). 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 (By similarity). 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 (By similarity). 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 (By similarity). Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (PubMed:27016726). {ECO:0000250|UniProtKB:P19021, ECO:0000269|PubMed:16225857, ECO:0000269|PubMed:27016726, ECO:0000269|PubMed:9562574}.
uniprot
proteins
mass_dalton
108963
uniprot
proteins
protein_family
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase family; Copper type II ascorbate-dependent monooxygenase family
uniprot
proteins
pubmed
16225857
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
27016726
uniprot
proteins
pubmed
9562574
uniprot
proteins
sequence_length
979
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}.
uniprot
proteins
transmembrane_region
TRANSMEM 870..893; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins