ID   A0A8C2TBA7_COTJA        Unreviewed;       846 AA.
AC   A0A8C2TBA7;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   10-JUN-2026, entry version 21.
DE   SubName: Full=Peptidylglycine alpha-amidating monooxygenase {ECO:0000313|Ensembl:ENSCJPP00005011212.1};
GN   Name=PAM {ECO:0000313|Ensembl:ENSCJPP00005011212.1};
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934 {ECO:0000313|Ensembl:ENSCJPP00005011212.1, ECO:0000313|Proteomes:UP000694412};
RN   [1] {ECO:0000313|Ensembl:ENSCJPP00005011212.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   International Coturnix japonica Genome Analysis Consortium;
RA   Warren W., Burt D.W., Antin P.B., Lanford R., Gros J., Wilson R.K.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJPP00005011212.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a [peptide]-C-terminal (2S)-2-hydroxyglycine = a [peptide]-C-
CC         terminal amide + glyoxylate; Xref=Rhea:RHEA:20924, Rhea:RHEA-
CC         COMP:13485, Rhea:RHEA-COMP:15321, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:137001, ChEBI:CHEBI:142768; EC=4.3.2.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00000686};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a
CC         [peptide]-C-terminal (2S)-2-hydroxyglycine + 2 monodehydro-L-
CC         ascorbate radical + H2O; Xref=Rhea:RHEA:21452, Rhea:RHEA-COMP:13486,
CC         Rhea:RHEA-COMP:15321, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:CHEBI:137000,
CC         ChEBI:CHEBI:142768; EC=1.14.17.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00048431};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|PIRSR:PIRSR600720-2};
CC       Note=Binds 2 Cu(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR600720-
CC       2};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR600720-2};
CC       Note=Binds one Zn(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR600720-
CC       2};
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC       {ECO:0000256|ARBA:ARBA00004160}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004160}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidyl-alpha-
CC       hydroxyglycine alpha-amidating lyase family.
CC       {ECO:0000256|ARBA:ARBA00006026}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the copper type II
CC       ascorbate-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010263}.
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DR   AlphaFoldDB; A0A8C2TBA7; -.
DR   Ensembl; ENSCJPT00005016444.1; ENSCJPP00005011212.1; ENSCJPG00005009667.1.
DR   GeneTree; ENSGT00940000156369; -.
DR   Proteomes; UP000694412; Chromosome Z.
DR   GO; GO:0005576; C:extracellular region; IEA:TreeGrafter.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004598; F:peptidylamidoglycolate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004504; F:peptidylglycine monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001519; P:peptide amidation; IEA:UniProtKB-ARBA.
DR   CDD; cd14958; NHL_PAL_like; 1.
DR   FunFam; 2.60.120.230:FF:000002; Peptidyl-glycine alpha-amidating monooxygenase B; 1.
DR   FunFam; 2.120.10.30:FF:000016; peptidyl-glycine alpha-amidating monooxygenase isoform X1; 1.
DR   FunFam; 2.60.120.310:FF:000001; peptidyl-glycine alpha-amidating monooxygenase isoform X1; 1.
DR   Gene3D; 2.60.120.230; -; 1.
DR   Gene3D; 2.60.120.310; Copper type II, ascorbate-dependent monooxygenase, N-terminal domain; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
DR   InterPro; IPR020611; Cu2_ascorb_mOase_CS-1.
DR   InterPro; IPR014783; Cu2_ascorb_mOase_CS-2.
DR   InterPro; IPR000323; Cu2_ascorb_mOase_N.
DR   InterPro; IPR036939; Cu2_ascorb_mOase_N_sf.
DR   InterPro; IPR024548; Cu2_monoox_C.
DR   InterPro; IPR001258; NHL_repeat.
DR   InterPro; IPR000720; PHM/PAL.
DR   InterPro; IPR008977; PHM/PNGase_F_dom_sf.
DR   PANTHER; PTHR10680; PEPTIDYL-GLYCINE ALPHA-AMIDATING MONOOXYGENASE; 1.
DR   PANTHER; PTHR10680:SF14; PEPTIDYL-GLYCINE ALPHA-AMIDATING MONOOXYGENASE; 1.
DR   Pfam; PF03712; Cu2_monoox_C; 1.
DR   Pfam; PF01082; Cu2_monooxygen; 1.
DR   Pfam; PF01436; NHL; 3.
DR   PRINTS; PR00790; PAMONOXGNASE.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR   SUPFAM; SSF49742; PHM/PNGase F; 2.
DR   PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1.
DR   PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1.
DR   PROSITE; PS51125; NHL; 4.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR600720-2};
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR600720-2};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR600720-3};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR600720-
KW   4}; Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR600720-2};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694412};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR600720-2}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..846
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5034013025"
FT   TRANSMEM        734..758
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          61..172
FT                   /note="Copper type II ascorbate-dependent monooxygenase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01082"
FT   DOMAIN          197..342
FT                   /note="Copper type II ascorbate-dependent monooxygenase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03712"
FT   REPEAT          438..479
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          487..532
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          540..584
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          637..680
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REGION          808..846
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        821..834
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..846
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         103
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-2"
FT   BINDING         104
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-2"
FT   BINDING         168
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-2"
FT   BINDING         238
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-2"
FT   BINDING         240
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-2"
FT   BINDING         310
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-2"
FT   BINDING         388
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-2"
FT   BINDING         401
FT                   /ligand="a protein"
FT                   /ligand_id="ChEBI:CHEBI:16541"
FT                   /ligand_part="C-terminal Xaa-(2S)-2-hydroxyglycine residue"
FT                   /ligand_part_id="ChEBI:CHEBI:142768"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-1"
FT   BINDING         453
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-2"
FT   BINDING         455
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-2"
FT   BINDING         521
FT                   /ligand="a protein"
FT                   /ligand_id="ChEBI:CHEBI:16541"
FT                   /ligand_part="C-terminal Xaa-(2S)-2-hydroxyglycine residue"
FT                   /ligand_part_id="ChEBI:CHEBI:142768"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-1"
FT   BINDING         557
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-2"
FT   BINDING         573
FT                   /ligand="a protein"
FT                   /ligand_id="ChEBI:CHEBI:16541"
FT                   /ligand_part="C-terminal Xaa-(2S)-2-hydroxyglycine residue"
FT                   /ligand_part_id="ChEBI:CHEBI:142768"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-1"
FT   BINDING         654
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-2"
FT   BINDING         655
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-2"
FT   CARBOHYD        633
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-4"
FT   DISULFID        43..182
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-3"
FT   DISULFID        77..122
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-3"
FT   DISULFID        110..127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-3"
FT   DISULFID        223..330
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-3"
FT   DISULFID        289..311
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-3"
FT   DISULFID        501..522
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-3"
FT   DISULFID        569..580
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600720-3"
SQ   SEQUENCE   846 AA;  94498 MW;  84B823DD0945D85F CRC64;
     MAGLINNLLI LILVLQNICL GFRSPLSVFK RYKDATRSLS SECFGSARPV ISFRLSDFTL
     DIRMPGVTPK QSDTYLCMSV PLPVDDEAYV VDFKPHASMD TVHHMLLFGC NEPSSNENYW
     DCDEGICKDK SNILYAWARN APPTRLPKGV GFRVGGETGS KFFVLQVHYG DISAFRDKHK
     DCSGVTLHLT HQKQPLIAGM YLMMSVNTVI PPGEKEVDAD IACHYKRFPM HLFAYRVHTH
     RLGKVVSGYR VRNGQWTLIG RQSPQVPQAF YPVEHPVDVS YDDILAARCV FSGEGRTTET
     HIGGTANDEM CNFYIMYYME AKHAVSYITC TQNANPEMFR NIPQEANIPI PVKPDMLKMA
     HGHHEDFHIE EAMEWPGLDL KLGQVSGLAL DRENNLVIFH RGDHVWDENS FDSKFVYQQR
     GLGPIEQNTI LVLNPSNAEL LHSTGRNLFY LPHGLSIDKD GNYWVTDVAL HQVFKLGVDT
     KEPLLILGVA LQPGSDHSHF CQPTDVAVDP VTGSIYVSDG YCNSRIIQFS PNGLYIKQWG
     EETSSGKAGP AQFRIPHSLA LIPELSQLCV ADRENGRIQC FRLETAEFVR EIKHKSFGRE
     LFAVSYAPGG LLFAVNGMPY PGESEPVQGF VMNFSTGEII DTFIPLRKSF EMPHDIVASE
     DKTVFVGDVH ARTVWKFASS EKMEHRSVKK AGIEVQEIKA SETVVEARLK NNPEPTDTLK
     KQEKQHLVRR ASTGVSFVLI TTLLIIPIVI LLAILVFIRW RKTAVYGADG EHKLDSNSGR
     ILGRLRGKAG GGLNLGNFFA SHKGYSRKGF DRLSTEGSDQ EKDEDDGSDS EEEYSAPPPP
     QALSSS
//