AMD_RAT
ID AMD_RAT Reviewed; 976 AA.
AC P14925; P70710; Q64616; Q64668;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Peptidylglycine alpha-amidating monooxygenase {ECO:0000303|PubMed:10504734};
DE Short=PAM {ECO:0000303|PubMed:10504734};
DE Includes:
DE RecName: Full=Peptidylglycine alpha-hydroxylating monooxygenase {ECO:0000303|PubMed:10504734};
DE Short=PHM {ECO:0000303|PubMed:10504734};
DE EC=1.14.17.3 {ECO:0000269|PubMed:10079066};
DE Includes:
DE RecName: Full=Peptidyl-alpha-hydroxyglycine alpha-amidating lyase {ECO:0000303|PubMed:10504734};
DE EC=4.3.2.5 {ECO:0000269|PubMed:10079066};
DE AltName: Full=Peptidylamidoglycolate lyase {ECO:0000303|PubMed:10079066};
DE Short=PAL {ECO:0000303|PubMed:10079066};
DE Flags: Precursor;
GN Name=Pam {ECO:0000303|PubMed:10079066, ECO:0000312|RGD:3252};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (PAM-1/2).
RC STRAIN=Sprague-Dawley; TISSUE=Heart atrium;
RX PubMed=2911604; DOI=10.1073/pnas.86.2.735;
RA Stoffers D.A., Green C.B.R., Eipper B.A.;
RT "Alternative mRNA splicing generates multiple forms of peptidyl-glycine
RT alpha-amidating monooxygenase in rat atrium.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:735-739(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (PAM-3/4).
RC STRAIN=Sprague-Dawley; TISSUE=Heart atrium;
RX PubMed=1988445; DOI=10.1016/s0021-9258(18)52352-8;
RA Stoffers D.A., Ouafik L., Eipper B.A.;
RT "Characterization of novel mRNAs encoding enzymes involved in peptide
RT alpha-amidation.";
RL J. Biol. Chem. 266:1701-1707(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (PAM-1 TO 5).
RC STRAIN=Wistar; TISSUE=Pituitary;
RX PubMed=2401356; DOI=10.1016/0014-5793(90)81184-p;
RA Kato I., Yonekura H., Yamamoto H., Okamoto H.;
RT "Isolation and functional expression of pituitary peptidylglycine alpha-
RT amidating enzyme mRNA. A variant lacking the transmembrane domain.";
RL FEBS Lett. 269:319-323(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (PAM-4).
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2337358; DOI=10.1016/0003-9861(90)90466-c;
RA Bertelsen A.H., Beaudry G.A., Galella E.A., Jones B.N., Ray M.L.,
RA Mehta N.M.;
RT "Cloning and characterization of two alternatively spliced rat alpha-
RT amidating enzyme cDNAs from rat medullary thyroid carcinoma.";
RL Arch. Biochem. Biophys. 279:87-96(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=1740449; DOI=10.1016/s0021-9258(19)50625-1;
RA Eipper B.A., Green C.B., Campbell T.A., Stoffers D.A., Keutmann H.T.,
RA Mains R.E., Ouafik L.;
RT "Alternative splicing and endoproteolytic processing generate tissue-
RT specific forms of pituitary peptidylglycine alpha-amidating monooxygenase
RT (PAM).";
RL J. Biol. Chem. 267:4008-4015(1992).
RN [6]
RP PROTEIN SEQUENCE OF 26-42, AND GLYCOSYLATION AT ASN-765.
RX PubMed=2211657; DOI=10.1016/s0021-9258(18)38219-x;
RA Beaudry G.A., Mehta N.M., Ray M.L., Bertelsen A.H.;
RT "Purification and characterization of functional recombinant alpha-
RT amidating enzyme secreted from mammalian cells.";
RL J. Biol. Chem. 265:17694-17699(1990).
RN [7]
RP ALTERNATIVE SPLICING.
RX PubMed=1448112; DOI=10.1210/mend.6.10.1448112;
RA Ouafik L.H., Stoffers D.A., Campbell T.A., Johnson R.C., Bloomquist B.T.,
RA Mains R.E., Eipper B.A.;
RT "The multifunctional peptidylglycine alpha-amidating monooxygenase gene:
RT exon/intron organization of catalytic, processing, and routing domains.";
RL Mol. Endocrinol. 6:1571-1584(1992).
RN [8]
RP INTERACTION WITH RASSF9.
RX PubMed=9837933; DOI=10.1074/jbc.273.50.33524;
RA Chen L., Johnson R.C., Milgram S.L.;
RT "P-CIP1, a novel protein that interacts with the cytosolic domain of
RT peptidylglycine alpha-amidating monooxygenase, is associated with
RT endosomes.";
RL J. Biol. Chem. 273:33524-33532(1998).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10079066; DOI=10.1021/bi982255j;
RA Wilcox B.J., Ritenour-Rodgers K.J., Asser A.S., Baumgart L.E.,
RA Baumgart M.A., Boger D.L., DeBlassio J.L., deLong M.A., Glufke U.,
RA Henz M.E., King L. III, Merkler K.A., Patterson J.E., Robleski J.J.,
RA Vederas J.C., Merkler D.J.;
RT "N-acylglycine amidation: implications for the biosynthesis of fatty acid
RT primary amides.";
RL Biochemistry 38:3235-3245(1999).
RN [10]
RP DISULFIDE BONDS IN CATALYTIC DOMAIN.
RX PubMed=12369828; DOI=10.1021/bi0260280;
RA Kolhekar A.S., Bell J., Shiozaki E.N., Jin L., Keutmann H.T., Hand T.A.,
RA Mains R.E., Eipper B.A.;
RT "Essential features of the catalytic core of peptidyl-alpha-hydroxyglycine
RT alpha-amidating lyase.";
RL Biochemistry 41:12384-12394(2002).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-945; SER-949; THR-959 AND
RP SER-961, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 45-354 IN COMPLEX WITH COPPER,
RP AND COFACTOR.
RX PubMed=10504734; DOI=10.1038/13351;
RA Prigge S.T., Kolhekar A.S., Eipper B.A., Mains R.E., Amzel L.M.;
RT "Substrate-mediated electron transfer in peptidylglycine alpha-
RT hydroxylating monooxygenase.";
RL Nat. Struct. Biol. 6:976-983(1999).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 498-820 IN COMPLEX WITH ZINC
RP CALCIUM AND SUBSTRATE, COFACTOR, MUTAGENESIS OF ARG-533; ARG-706; MET-784
RP AND ASP-787, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP REGION.
RX PubMed=19604476; DOI=10.1016/j.str.2009.05.008;
RA Chufan E.E., De M., Eipper B.A., Mains R.E., Amzel L.M.;
RT "Amidation of bioactive peptides: the structure of the lyase domain of the
RT amidating enzyme.";
RL Structure 17:965-973(2009).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the post-translational
CC modification of inactive peptidylglycine precursors to the
CC corresponding bioactive alpha-amidated peptides, a terminal
CC modification in biosynthesis of many neural and endocrine peptides (By
CC similarity). Alpha-amidation involves two sequential reactions, both of
CC which are catalyzed by separate catalytic domains of the enzyme. The
CC first step, catalyzed by peptidyl alpha-hydroxylating monooxygenase
CC (PHM) domain, is the copper-, ascorbate-, and O2- dependent
CC stereospecific hydroxylation (with S stereochemistry) at the alpha-
CC carbon (C-alpha) of the C-terminal glycine of the peptidylglycine
CC substrate (PubMed:10079066). The second step, catalyzed by the
CC peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-
CC dependent cleavage of the N-C-alpha bond, producing the alpha-amidated
CC peptide and glyoxylate (PubMed:10079066). Similarly, catalyzes the two-
CC step conversion of an N-fatty acylglycine to a primary fatty acid amide
CC and glyoxylate (PubMed:10079066). {ECO:0000250|UniProtKB:P10731,
CC ECO:0000250|UniProtKB:P19021, ECO:0000269|PubMed:10079066}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a
CC [peptide]-C-terminal (2S)-2-hydroxyglycine + H2O + 2 monodehydro-L-
CC ascorbate radical; 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:0000269|PubMed:10079066};
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:0000269|PubMed:10079066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-ascorbate + N-dodecanoylglycine + O2 = H2O + 2
CC monodehydro-L-ascorbate radical + N-dodecanoyl-(2S)-hydroxyglycine;
CC Xref=Rhea:RHEA:58540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:CHEBI:142678,
CC ChEBI:CHEBI:142693; Evidence={ECO:0000269|PubMed:10079066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-dodecanoyl-(2S)-hydroxyglycine = dodecanamide + glyoxylate;
CC Xref=Rhea:RHEA:58624, ChEBI:CHEBI:34726, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:142693; Evidence={ECO:0000269|PubMed:10079066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-ascorbate + N-(9Z,12Z,15Z)-octadecatrienoylglycine + O2 =
CC H2O + 2 monodehydro-L-ascorbate radical + N-(9Z,12Z,15Z)-
CC octadecatrienoyl-(2S)-hydroxyglycine; Xref=Rhea:RHEA:58548,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:38290,
CC ChEBI:CHEBI:59513, ChEBI:CHEBI:142679, ChEBI:CHEBI:142697;
CC Evidence={ECO:0000269|PubMed:10079066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(9Z,12Z,15Z)-octadecatrienoyl-(2S)-hydroxyglycine =
CC (9Z,12Z,15Z)-octadecatrienamide + glyoxylate; Xref=Rhea:RHEA:58644,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:142684, ChEBI:CHEBI:142697;
CC Evidence={ECO:0000269|PubMed:10079066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-ascorbate + N-(9Z-octadecenoyl)glycine + O2 = H2O + 2
CC monodehydro-L-ascorbate radical + N-(9Z-octadecenoyl)-(2S)-
CC hydroxyglycine; Xref=Rhea:RHEA:58600, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513,
CC ChEBI:CHEBI:133992, ChEBI:CHEBI:142696;
CC Evidence={ECO:0000269|PubMed:10079066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(9Z-octadecenoyl)-(2S)-hydroxyglycine = (9Z)-octadecenamide
CC + glyoxylate; Xref=Rhea:RHEA:58636, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:116314, ChEBI:CHEBI:142696;
CC Evidence={ECO:0000269|PubMed:10079066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-ascorbate + N-tetradecanoylglycine + O2 = H2O + 2
CC monodehydro-L-ascorbate radical + N-tetradecanoyl-(2S)-
CC hydroxyglycine; Xref=Rhea:RHEA:58544, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513,
CC ChEBI:CHEBI:86500, ChEBI:CHEBI:142694;
CC Evidence={ECO:0000269|PubMed:10079066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-tetradecanoyl-(2S)-hydroxyglycine = glyoxylate +
CC tetradecamide; Xref=Rhea:RHEA:58632, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:137125, ChEBI:CHEBI:142694;
CC Evidence={ECO:0000269|PubMed:10079066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-ascorbate + N-decanoylglycine + O2 = H2O + 2 monodehydro-
CC L-ascorbate radical + N-decanoyl-(2S)-hydroxyglycine;
CC Xref=Rhea:RHEA:58608, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:CHEBI:142680,
CC ChEBI:CHEBI:142692; Evidence={ECO:0000269|PubMed:10079066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-decanoyl-(2S)-hydroxyglycine = decanamide + glyoxylate;
CC Xref=Rhea:RHEA:58620, ChEBI:CHEBI:36655, ChEBI:CHEBI:38833,
CC ChEBI:CHEBI:142692; Evidence={ECO:0000269|PubMed:10079066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-ascorbate + N-octanoylglycine + O2 = H2O + 2 monodehydro-
CC L-ascorbate radical + N-octanoyl-(2S)-hydroxyglycine;
CC Xref=Rhea:RHEA:58612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:CHEBI:142681,
CC ChEBI:CHEBI:142691; Evidence={ECO:0000269|PubMed:10079066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-octanoyl-(2S)-hydroxyglycine = glyoxylate + octanamide;
CC Xref=Rhea:RHEA:58616, ChEBI:CHEBI:36655, ChEBI:CHEBI:142682,
CC ChEBI:CHEBI:142691; Evidence={ECO:0000269|PubMed:10079066};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds one Zn(2+) ion per subunit. {ECO:0000269|PubMed:19604476};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Note=Binds 2 Cu(2+) ions per subunit. {ECO:0000269|PubMed:10504734};
CC -!- ACTIVITY REGULATION: PAM activity is inhibited by EDTA, phenylglyoxal
CC and diethyl pyrocarbonate (By similarity). PAL activity is stimulated
CC by cadmium and inhibited by mercury (PubMed:19604476).
CC {ECO:0000250|UniProtKB:P19021, ECO:0000269|PubMed:19604476}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.8 uM for [peptide]-C-terminal (2S)-2-hydroxyglycine
CC {ECO:0000269|PubMed:19604476};
CC -!- SUBUNIT: Monomer. Interacts with RASSF9. {ECO:0000269|PubMed:9837933}.
CC -!- INTERACTION:
CC P14925; O88869: Rassf9; NbExp=3; IntAct=EBI-1395008, EBI-1395057;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000250|UniProtKB:P10731}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P10731}. Note=Secretory granules.
CC {ECO:0000250|UniProtKB:P10731}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=PAM-1;
CC IsoId=P14925-1; Sequence=Displayed;
CC Name=PAM-2;
CC IsoId=P14925-2; Sequence=VSP_001232;
CC Name=PAM-3;
CC IsoId=P14925-3; Sequence=VSP_001232, VSP_001234;
CC Name=PAM-3A;
CC IsoId=P14925-4; Sequence=VSP_001232, VSP_001233;
CC Name=PAM-3B;
CC IsoId=P14925-5; Sequence=VSP_001232, VSP_001235;
CC Name=PAM-4;
CC IsoId=P14925-6; Sequence=VSP_001236, VSP_001237;
CC Name=PAM-5;
CC IsoId=P14925-7; Sequence=VSP_001230, VSP_001231;
CC -!- MISCELLANEOUS: [Isoform PAM-1]: Membrane-bound.
CC -!- MISCELLANEOUS: [Isoform PAM-2]: Membrane-bound. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform PAM-3]: Soluble. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform PAM-3A]: Soluble. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform PAM-3B]: Membrane-bound. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform PAM-4]: Soluble. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform PAM-5]: Soluble. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidyl-alpha-
CC hydroxyglycine alpha-amidating lyase family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the copper type II
CC ascorbate-dependent monooxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA42068.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; U52642; AAC05604.1; JOINED; Genomic_DNA.
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DR EMBL; U52644; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52645; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52646; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52647; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52648; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52649; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52651; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52652; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52654; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52655; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52656; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52657; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52658; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52659; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52660; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52661; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52662; AAC05604.1; JOINED; Genomic_DNA.
DR EMBL; U52664; AAC05608.1; -; Genomic_DNA.
DR EMBL; U52639; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52640; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52641; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52642; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52643; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52644; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52645; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52646; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52647; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52648; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52649; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52651; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52652; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52654; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52655; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52656; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52657; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52658; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52659; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52660; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52661; AAC05608.1; JOINED; Genomic_DNA.
DR EMBL; U52664; AAC05606.1; -; Genomic_DNA.
DR EMBL; U52639; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52640; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52641; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52642; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52643; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52644; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52645; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52646; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52647; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52648; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52649; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52651; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52652; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52654; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52655; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52656; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52657; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52658; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52659; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52660; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52661; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; U52663; AAC05606.1; JOINED; Genomic_DNA.
DR EMBL; M25732; AAA41803.1; -; mRNA.
DR EMBL; M25719; AAA41804.1; -; mRNA.
DR EMBL; M63662; AAA42068.1; ALT_SEQ; mRNA.
DR EMBL; X59685; CAA42206.1; -; mRNA.
DR EMBL; X59686; CAA42207.1; -; mRNA.
DR EMBL; X59687; CAA42208.1; -; mRNA.
DR EMBL; X59688; CAA42209.1; -; mRNA.
DR EMBL; X59689; CAA42210.1; -; mRNA.
DR EMBL; M82845; AAB00162.1; -; mRNA.
DR PIR; A32193; URRTAP.
DR RefSeq; NP_037132.2; NM_013000.2. [P14925-1]
DR RefSeq; XP_006245660.1; XM_006245598.3. [P14925-2]
DR RefSeq; XP_006245661.1; XM_006245599.3. [P14925-5]
DR PDB; 1OPM; X-ray; 2.10 A; A=45-354.
DR PDB; 1PHM; X-ray; 1.90 A; A=45-354.
DR PDB; 1SDW; X-ray; 1.85 A; A=43-356.
DR PDB; 1YI9; X-ray; 1.70 A; A=47-355.
DR PDB; 1YIP; X-ray; 2.20 A; A=45-355.
DR PDB; 1YJK; X-ray; 2.00 A; A=50-355.
DR PDB; 1YJL; X-ray; 2.40 A; A=50-355.
DR PDB; 3FVZ; X-ray; 2.35 A; A=498-820.
DR PDB; 3FW0; X-ray; 2.52 A; A=498-820.
DR PDB; 3MIB; X-ray; 2.35 A; A=43-356.
DR PDB; 3MIC; X-ray; 2.42 A; A=43-356.
DR PDB; 3MID; X-ray; 3.06 A; A=43-356.
DR PDB; 3MIE; X-ray; 3.26 A; A=43-356.
DR PDB; 3MIF; X-ray; 2.00 A; A=43-356.
DR PDB; 3MIG; X-ray; 2.70 A; A=43-356.
DR PDB; 3MIH; X-ray; 2.74 A; A=43-356.
DR PDB; 3MLJ; X-ray; 2.15 A; A=43-356.
DR PDB; 3MLK; X-ray; 3.10 A; A=43-356.
DR PDB; 3MLL; X-ray; 3.25 A; A=43-356.
DR PDB; 3PHM; X-ray; 2.10 A; A=45-354.
DR PDB; 4E4Z; X-ray; 1.98 A; A=45-356.
DR PDB; 5WJA; X-ray; 2.30 A; A/D=45-356.
DR PDB; 5WKW; X-ray; 1.79 A; A=45-356.
DR PDB; 5WM0; X-ray; 2.40 A; A=1-976.
DR PDB; 6ALA; X-ray; 2.59 A; A/C=45-356.
DR PDB; 6ALV; X-ray; 3.50 A; A=45-356.
DR PDB; 6AMP; X-ray; 2.48 A; A=45-356.
DR PDB; 6AN3; X-ray; 2.05 A; A=45-356.
DR PDB; 6AO6; X-ray; 2.98 A; A=45-356.
DR PDB; 6AY0; X-ray; 2.60 A; A=45-356.
DR PDB; 6NCK; X-ray; 2.70 A; A=45-356.
DR PDBsum; 1OPM; -.
DR PDBsum; 1PHM; -.
DR PDBsum; 1SDW; -.
DR PDBsum; 1YI9; -.
DR PDBsum; 1YIP; -.
DR PDBsum; 1YJK; -.
DR PDBsum; 1YJL; -.
DR PDBsum; 3FVZ; -.
DR PDBsum; 3FW0; -.
DR PDBsum; 3MIB; -.
DR PDBsum; 3MIC; -.
DR PDBsum; 3MID; -.
DR PDBsum; 3MIE; -.
DR PDBsum; 3MIF; -.
DR PDBsum; 3MIG; -.
DR PDBsum; 3MIH; -.
DR PDBsum; 3MLJ; -.
DR PDBsum; 3MLK; -.
DR PDBsum; 3MLL; -.
DR PDBsum; 3PHM; -.
DR PDBsum; 4E4Z; -.
DR PDBsum; 5WJA; -.
DR PDBsum; 5WKW; -.
DR PDBsum; 5WM0; -.
DR PDBsum; 6ALA; -.
DR PDBsum; 6ALV; -.
DR PDBsum; 6AMP; -.
DR PDBsum; 6AN3; -.
DR PDBsum; 6AO6; -.
DR PDBsum; 6AY0; -.
DR PDBsum; 6NCK; -.
DR AlphaFoldDB; P14925; -.
DR SMR; P14925; -.
DR BioGRID; 247540; 3.
DR IntAct; P14925; 3.
DR STRING; 10116.ENSRNOP00000046774; -.
DR BindingDB; P14925; -.
DR ChEMBL; CHEMBL4963; -.
DR GlyGen; P14925; 1 site.
DR iPTMnet; P14925; -.
DR PhosphoSitePlus; P14925; -.
DR jPOST; P14925; -.
DR PaxDb; P14925; -.
DR PRIDE; P14925; -.
DR Ensembl; ENSRNOT00000041418; ENSRNOP00000050784; ENSRNOG00000033280. [P14925-6]
DR Ensembl; ENSRNOT00000056457; ENSRNOP00000053295; ENSRNOG00000033280. [P14925-5]
DR Ensembl; ENSRNOT00000117663; ENSRNOP00000089015; ENSRNOG00000033280. [P14925-4]
DR Ensembl; ENSRNOT00000118414; ENSRNOP00000087123; ENSRNOG00000033280. [P14925-3]
DR GeneID; 25508; -.
DR KEGG; rno:25508; -.
DR CTD; 5066; -.
DR RGD; 3252; Pam.
DR VEuPathDB; HostDB:ENSRNOG00000033280; -.
DR eggNOG; KOG3567; Eukaryota.
DR GeneTree; ENSGT00940000156369; -.
DR HOGENOM; CLU_891273_0_0_1; -.
DR InParanoid; P14925; -.
DR OMA; KRNPQWP; -.
DR OrthoDB; 476471at2759; -.
DR PhylomeDB; P14925; -.
DR BRENDA; 1.14.17.3; 5301.
DR BRENDA; 4.3.2.5; 5301.
DR SABIO-RK; P14925; -.
DR EvolutionaryTrace; P14925; -.
DR PRO; PR:P14925; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000033280; Expressed in heart and 19 other tissues.
DR Genevisible; P14925; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0000793; C:condensed chromosome; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0030667; C:secretory granule membrane; IDA:RGD.
DR GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0004598; F:peptidylamidoglycolate lyase activity; IDA:UniProtKB.
DR GO; GO:0004504; F:peptidylglycine monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0008270; F:zinc ion binding; IDA:RGD.
DR GO; GO:0007417; P:central nervous system development; IEP:RGD.
DR GO; GO:0062112; P:fatty acid primary amide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0007507; P:heart development; IEP:RGD.
DR GO; GO:0007595; P:lactation; IEP:RGD.
DR GO; GO:0060173; P:limb development; IEP:RGD.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:RGD.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
DR GO; GO:0007076; P:mitotic chromosome condensation; ISO:RGD.
DR GO; GO:0042476; P:odontogenesis; IEP:RGD.
DR GO; GO:0022602; P:ovulation cycle process; IEP:RGD.
DR GO; GO:0001519; P:peptide amidation; IDA:UniProtKB.
DR GO; GO:0006518; P:peptide metabolic process; IDA:RGD.
DR GO; GO:0018032; P:protein amidation; IDA:RGD.
DR GO; GO:0019538; P:protein metabolic process; IDA:RGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:RGD.
DR GO; GO:0050708; P:regulation of protein secretion; IMP:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0046688; P:response to copper ion; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0009268; P:response to pH; IDA:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0010043; P:response to zinc ion; ISO:RGD.
DR GO; GO:0009404; P:toxin metabolic process; IDA:RGD.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 2.60.120.230; -; 1.
DR Gene3D; 2.60.120.310; -; 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 Pfam; PF03712; Cu2_monoox_C; 1.
DR Pfam; PF01082; Cu2_monooxygen; 1.
DR Pfam; PF01436; NHL; 3.
DR PRINTS; PR00790; PAMONOXGNASE.
DR SUPFAM; SSF49742; SSF49742; 2.
DR PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1.
DR PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1.
DR PROSITE; PS51125; NHL; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium;
KW Cleavage on pair of basic residues; Copper; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Lipid metabolism;
KW Lyase; Membrane; Metal-binding; Monooxygenase; Multifunctional enzyme;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Sulfation; Transmembrane; Transmembrane helix; Vitamin C; Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:2211657"
FT PROPEP 26..35
FT /id="PRO_0000006365"
FT CHAIN 36..976
FT /note="Peptidylglycine alpha-amidating monooxygenase"
FT /id="PRO_0000006366"
FT TOPO_DOM 36..866
FT /note="Intragranular"
FT /evidence="ECO:0000255"
FT TRANSMEM 867..890
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 891..976
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 501..544
FT /note="NHL 1"
FT REPEAT 570..611
FT /note="NHL 2"
FT REPEAT 620..665
FT /note="NHL 3"
FT REPEAT 673..717
FT /note="NHL 4"
FT REPEAT 769..812
FT /note="NHL 5"
FT REGION 1..497
FT /note="Peptidylglycine alpha-hydroxylating monooxygenase"
FT REGION 498..820
FT /note="Peptidyl-alpha-hydroxyglycine alpha-amidating lyase"
FT /evidence="ECO:0000269|PubMed:19604476"
FT REGION 928..945
FT /note="Interaction with RASSF9"
FT /evidence="ECO:0000269|PubMed:9837933"
FT REGION 940..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10504734,
FT ECO:0007744|PDB:1OPM, ECO:0007744|PDB:3PHM"
FT BINDING 108
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10504734,
FT ECO:0007744|PDB:1OPM, ECO:0007744|PDB:3PHM"
FT BINDING 172
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10504734,
FT ECO:0007744|PDB:1OPM, ECO:0007744|PDB:3PHM"
FT BINDING 242
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10504734,
FT ECO:0007744|PDB:1OPM, ECO:0007744|PDB:3PHM"
FT BINDING 244
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10504734,
FT ECO:0007744|PDB:1OPM, ECO:0007744|PDB:3PHM"
FT BINDING 314
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10504734,
FT ECO:0007744|PDB:1OPM, ECO:0007744|PDB:3PHM"
FT BINDING 520
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:19604476,
FT ECO:0007744|PDB:3FVZ, ECO:0007744|PDB:3FW0"
FT BINDING 533
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19604476"
FT BINDING 585
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19604476,
FT ECO:0007744|PDB:3FVZ"
FT BINDING 587
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:19604476,
FT ECO:0007744|PDB:3FVZ, ECO:0007744|PDB:3FW0"
FT BINDING 654
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19604476"
FT BINDING 690
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19604476,
FT ECO:0007744|PDB:3FVZ"
FT BINDING 706
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19604476"
FT BINDING 786
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19604476,
FT ECO:0007744|PDB:3FVZ"
FT BINDING 787
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:19604476,
FT ECO:0007744|PDB:3FVZ, ECO:0007744|PDB:3FW0"
FT MOD_RES 921
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19021"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19021"
FT MOD_RES 945
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 946
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19021"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 959
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 961
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2211657"
FT DISULFID 47..186
FT /evidence="ECO:0000269|PubMed:12369828"
FT DISULFID 81..126
FT /evidence="ECO:0000269|PubMed:12369828"
FT DISULFID 114..131
FT /evidence="ECO:0000269|PubMed:12369828"
FT DISULFID 227..334
FT /evidence="ECO:0000269|PubMed:12369828"
FT DISULFID 293..315
FT /evidence="ECO:0000269|PubMed:12369828"
FT DISULFID 634..655
FT /evidence="ECO:0000269|PubMed:12369828"
FT DISULFID 702..713
FT /evidence="ECO:0000269|PubMed:12369828"
FT VAR_SEQ 308..312
FT /note="GTSSD -> FKDTF (in isoform PAM-5)"
FT /evidence="ECO:0000305"
FT /id="VSP_001230"
FT VAR_SEQ 313..976
FT /note="Missing (in isoform PAM-5)"
FT /evidence="ECO:0000305"
FT /id="VSP_001231"
FT VAR_SEQ 393..497
FT /note="Missing (in isoform PAM-2, isoform PAM-3, isoform
FT PAM-3A and isoform PAM-3B)"
FT /evidence="ECO:0000305"
FT /id="VSP_001232"
FT VAR_SEQ 498..517
FT /note="DFHVEEELDWPGVYLLPGQV -> GASRISFTQKKKCVKHCNPH (in
FT isoform PAM-4)"
FT /evidence="ECO:0000305"
FT /id="VSP_001236"
FT VAR_SEQ 518..917
FT /note="Missing (in isoform PAM-4)"
FT /evidence="ECO:0000305"
FT /id="VSP_001237"
FT VAR_SEQ 832..917
FT /note="Missing (in isoform PAM-3)"
FT /evidence="ECO:0000305"
FT /id="VSP_001234"
FT VAR_SEQ 832..899
FT /note="Missing (in isoform PAM-3A)"
FT /evidence="ECO:0000305"
FT /id="VSP_001233"
FT VAR_SEQ 900..917
FT /note="Missing (in isoform PAM-3B)"
FT /evidence="ECO:0000305"
FT /id="VSP_001235"
FT MUTAGEN 533
FT /note="R->A: Abolishes peptidyl-alpha-hydroxyglycine alpha-
FT amidating lyase activity."
FT /evidence="ECO:0000269|PubMed:19604476"
FT MUTAGEN 533
FT /note="R->Q: Abolishes peptidyl-alpha-hydroxyglycine alpha-
FT amidating lyase activity."
FT /evidence="ECO:0000269|PubMed:19604476"
FT MUTAGEN 706
FT /note="R->A: Abolishes peptidyl-alpha-hydroxyglycine alpha-
FT amidating lyase activity."
FT /evidence="ECO:0000269|PubMed:19604476"
FT MUTAGEN 706
FT /note="R->Q: Reduces peptidyl-alpha-hydroxyglycine alpha-
FT amidating lyase activity."
FT /evidence="ECO:0000269|PubMed:19604476"
FT MUTAGEN 784
FT /note="M->A: Abolishes peptidyl-alpha-hydroxyglycine alpha-
FT amidating lyase activity."
FT /evidence="ECO:0000269|PubMed:19604476"
FT MUTAGEN 784
FT /note="M->Q: Abolishes peptidyl-alpha-hydroxyglycine alpha-
FT amidating lyase activity."
FT /evidence="ECO:0000269|PubMed:19604476"
FT MUTAGEN 787
FT /note="D->A: Reduces peptidyl-alpha-hydroxyglycine alpha-
FT amidating lyase activity."
FT /evidence="ECO:0000269|PubMed:19604476"
FT CONFLICT 959
FT /note="T -> S (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1PHM"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 58..67
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6ALV"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:1YI9"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 106..118
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1YI9"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:1YI9"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:1YI9"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:1SDW"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 199..209
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:5WKW"
FT STRAND 219..228
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 234..245
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 247..256
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:5WKW"
FT STRAND 315..324
FT /evidence="ECO:0007829|PDB:1YI9"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:5WKW"
FT HELIX 340..345
FT /evidence="ECO:0007829|PDB:1YI9"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:1YI9"
FT STRAND 498..503
FT /evidence="ECO:0007829|PDB:3FVZ"
FT HELIX 508..511
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 517..522
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 528..532
FT /evidence="ECO:0007829|PDB:3FVZ"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 562..565
FT /evidence="ECO:0007829|PDB:3FVZ"
FT TURN 567..569
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 572..576
FT /evidence="ECO:0007829|PDB:3FVZ"
FT TURN 578..580
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 582..589
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:3FVZ"
FT TURN 600..603
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 604..608
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 617..622
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 634..641
FT /evidence="ECO:0007829|PDB:3FVZ"
FT TURN 643..645
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 648..652
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 658..662
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 668..672
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 678..680
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 689..695
FT /evidence="ECO:0007829|PDB:3FVZ"
FT TURN 696..699
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 700..705
FT /evidence="ECO:0007829|PDB:3FVZ"
FT TURN 706..709
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 710..715
FT /evidence="ECO:0007829|PDB:3FVZ"
FT TURN 716..718
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 721..725
FT /evidence="ECO:0007829|PDB:3FVZ"
FT TURN 728..732
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 734..740
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 743..748
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 761..765
FT /evidence="ECO:0007829|PDB:3FVZ"
FT TURN 766..768
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 771..775
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 778..780
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 783..790
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 794..803
FT /evidence="ECO:0007829|PDB:3FVZ"
FT STRAND 806..813
FT /evidence="ECO:0007829|PDB:3FVZ"
FT MOD_RES P14925-3:774
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000305"
FT MOD_RES P14925-4:792
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 976 AA; 108675 MW; 7233021BEBEFD9B9 CRC64;
MAGRARSGLL LLLLGLLALQ SSCLAFRSPL SVFKRFKETT RSFSNECLGT IGPVTPLDAS
DFALDIRMPG VTPKESDTYF CMSMRLPVDE EAFVIDFKPR ASMDTVHHML LFGCNMPSST
GSYWFCDEGT CTDKANILYA WARNAPPTRL PKGVGFRVGG ETGSKYFVLQ VHYGDISAFR
DNHKDCSGVS VHLTRVPQPL IAGMYLMMSV DTVIPPGEKV VNADISCQYK MYPMHVFAYR
VHTHHLGKVV SGYRVRNGQW TLIGRQNPQL PQAFYPVEHP VDVTFGDILA ARCVFTGEGR
TEATHIGGTS SDEMCNLYIM YYMEAKYALS FMTCTKNVAP DMFRTIPAEA NIPIPVKPDM
VMMHGHHKEA ENKEKSALMQ QPKQGEEEVL EQGDFYSLLS KLLGEREDVH VHKYNPTEKT
ESGSDLVAEI ANVVQKKDLG RSDAREGAEH EEWGNAILVR DRIHRFHQLE STLRPAESRA
FSFQQPGEGP WEPEPSGDFH VEEELDWPGV YLLPGQVSGV ALDSKNNLVI FHRGDHVWDG
NSFDSKFVYQ QRGLGPIEED TILVIDPNNA EILQSSGKNL FYLPHGLSID TDGNYWVTDV
ALHQVFKLDP HSKEGPLLIL GRSMQPGSDQ NHFCQPTDVA VEPSTGAVFV SDGYCNSRIV
QFSPSGKFVT QWGEESSGSS PRPGQFSVPH SLALVPHLDQ LCVADRENGR IQCFKTDTKE
FVREIKHASF GRNVFAISYI PGFLFAVNGK PYFGDQEPVQ GFVMNFSSGE IIDVFKPVRK
HFDMPHDIVA SEDGTVYIGD AHTNTVWKFT LTEKMEHRSV KKAGIEVQEI KEAEAVVEPK
VENKPTSSEL QKMQEKQKLS TEPGSGVSVV LITTLLVIPV LVLLAIVMFI RWKKSRAFGD
HDRKLESSSG RVLGRFRGKG SGGLNLGNFF ASRKGYSRKG FDRVSTEGSD QEKDEDDGTE
SEEEYSAPLP KPAPSS
