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 04-NOV-2026, entry version 218. 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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF HIS-108; HIS-244 RP AND MET-314. RX PubMed=7893699; DOI=10.1021/bi00009a016; RA Eipper B.A., Quon A.S., Mains R.E., Boswell J.S., Blackburn N.J.; RT "The catalytic core of peptidylglycine alpha-hydroxylating monooxygenase: RT investigation by site-directed mutagenesis, Cu X-ray absorption RT spectroscopy, and electron paramagnetic resonance."; RL Biochemistry 34:2857-2865(1995). RN [9] 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 [10] 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 [11] 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 [12] 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 [13] {ECO:0007744|PDB:1OPM, ECO:0007744|PDB:3PHM} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH CU(2+), 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 [14] {ECO:0007744|PDB:1SDW} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH CU(2+), COFACTOR, SUBUNIT, AND RP DISULFIDE BONDS. RX PubMed=15131304; DOI=10.1126/science.1094583; RA Prigge S.T., Eipper B.A., Mains R.E., Amzel L.M.; RT "Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme RT complex."; RL Science 304:864-867(2004). RN [15] {ECO:0007744|PDB:1YI9, ECO:0007744|PDB:1YIP, ECO:0007744|PDB:1YJK, ECO:0007744|PDB:1YJL} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH CU(2+), COFACTOR, AND DISULFIDE RP BONDS. RX PubMed=16100265; DOI=10.1529/biophysj.105.066100; RA Siebert X., Eipper B.A., Mains R.E., Prigge S.T., Blackburn N.J., RA Amzel L.M.; RT "The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase RT also plays a critical structural role."; RL Biophys. J. 89:3312-3319(2005). RN [16] {ECO:0007744|PDB:3FVZ, ECO:0007744|PDB:3FW0} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ZINC; CALCIUM AND RP ALPHA-HYDROXYHIPPURIC ACID, SUBUNIT, COFACTOR, MUTAGENESIS OF ARG-533; RP ARG-706; MET-784 AND ASP-787, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY RP REGULATION, AND 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). RN [17] {ECO:0007744|PDB:3MIB, ECO:0007744|PDB:3MIC, ECO:0007744|PDB:3MID, ECO:0007744|PDB:3MIE, ECO:0007744|PDB:3MIF, ECO:0007744|PDB:3MIG, ECO:0007744|PDB:3MIH, ECO:0007744|PDB:3MLJ, ECO:0007744|PDB:3MLK, ECO:0007744|PDB:3MLL} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH CU(2+), SUBUNIT, COFACTOR, AND RP DISULFIDE BONDS. RX PubMed=20958070; DOI=10.1021/ja103117r; RA Chufan E.E., Prigge S.T., Siebert X., Eipper B.A., Mains R.E., Amzel L.M.; RT "Differential reactivity between two copper sites in peptidylglycine alpha- RT hydroxylating monooxygenase."; RL J. Am. Chem. Soc. 132:15565-15572(2010). RN [18] {ECO:0007744|PDB:4E4Z} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH CU(2+), SUBUNIT, COFACTOR, AND RP DISULFIDE BONDS. RX PubMed=23247335; DOI=10.1007/s00775-012-0967-z; RA Rudzka K., Moreno D.M., Eipper B., Mains R., Estrin D.A., Amzel L.M.; RT "Coordination of peroxide to the Cu(M) center of peptidylglycine alpha- RT hydroxylating monooxygenase (PHM): structural and computational study."; RL J. Biol. Inorg. Chem. 18:223-232(2013). RN [19] {ECO:0007744|PDB:5WJA, ECO:0007744|PDB:5WKW, ECO:0007744|PDB:5WM0, ECO:0007744|PDB:6ALA, ECO:0007744|PDB:6ALV, ECO:0007744|PDB:6AMP, ECO:0007744|PDB:6AN3, ECO:0007744|PDB:6AO6, ECO:0007744|PDB:6AY0} RP X-RAY CRYSTALLOGRAPHY OF MUTANT ALA-107; ALA-108 AND ALA-172 IN COMPLEX RP WITH CU(2+), SUBUNIT, COFACTOR, DISULFIDE BONDS, AND MUTAGENESIS OF RP HIS-107; HIS-108 AND HIS-172. RX PubMed=30271955; DOI=10.1038/s42003-018-0082-y; RA Maheshwari S., Shimokawa C., Rudzka K., Kline C.D., Eipper B.A., RA Mains R.E., Gabelli S.B., Blackburn N., Amzel L.M.; RT "Effects of copper occupancy on the conformational landscape of RT peptidylglycine alpha-hydroxylating monooxygenase."; RL Commun. Biol. 1:74-74(2018). RN [20] {ECO:0007744|PDB:8DSJ, ECO:0007744|PDB:8DSL, ECO:0007744|PDB:8DSN} RP X-RAY CRYSTALLOGRAPHY OF MUTANT ALA-272IN COMPLEX WITH CU(2+), COFACTOR, RP DISULFIDE BONDS, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, AND MUTAGENESIS OF GLN-272. RX PubMed=36880254; DOI=10.1002/pro.4615; RA Arias R.J., Welch E.F., Blackburn N.J.; RT "New structures reveal flexible dynamics between the subdomains of RT peptidylglycine monooxygenase. Implications for an open to closed RT mechanism."; RL Protein Sci. 32:e4615-e4615(2023). CC -!- FUNCTION: Bifunctional enzyme that catalyzes amidation of the C- CC terminus of proteins (PubMed:10079066, PubMed:36880254, CC PubMed:7893699). Alpha-amidation is present at the C-terminus of many CC endocrine hormones and neuropeptides and is required for their activity CC (By similarity). C-terminal amidation also takes place in response to CC protein fragmentation triggered by oxidative stress, promoting CC degradation of amidated protein fragments by the proteasome (By CC similarity). Alpha-amidation involves two sequential reactions, both of CC which are catalyzed by separate catalytic domains of the enzyme CC (PubMed:10079066). The first step, catalyzed by peptidyl alpha- CC hydroxylating monooxygenase (PHM) domain, is the copper-, ascorbate-, CC and O2- dependent stereospecific hydroxylation (with S stereochemistry) CC at the alpha-carbon (C-alpha) of the C-terminal glycine of the CC peptidylglycine substrate (PubMed:10079066). The second step, catalyzed CC by the 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:P19021, CC ECO:0000269|PubMed:10079066, ECO:0000269|PubMed:36880254, CC ECO:0000269|PubMed:7893699}. 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:0000269|PubMed:10079066, ECO:0000269|PubMed:36880254, CC ECO:0000269|PubMed:7893699}; 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=N-dodecanoylglycine + 2 L-ascorbate + O2 = N-dodecanoyl-(2S)- CC hydroxyglycine + 2 monodehydro-L-ascorbate radical + H2O; 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=N-(9Z,12Z,15Z)-octadecatrienoylglycine + 2 L-ascorbate + O2 = CC N-(9Z,12Z,15Z)-octadecatrienoyl-(2S)-hydroxyglycine + 2 monodehydro- CC L-ascorbate radical + H2O; Xref=Rhea:RHEA:58548, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, CC 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=N-(9Z-octadecenoyl)glycine + 2 L-ascorbate + O2 = N-(9Z- CC octadecenoyl)-(2S)-hydroxyglycine + 2 monodehydro-L-ascorbate radical CC + H2O; Xref=Rhea:RHEA:58600, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:CHEBI:133992, CC ChEBI:CHEBI:142696; 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=N-tetradecanoylglycine + 2 L-ascorbate + O2 = N-tetradecanoyl- CC (2S)-hydroxyglycine + 2 monodehydro-L-ascorbate radical + H2O; CC Xref=Rhea:RHEA:58544, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:CHEBI:86500, CC ChEBI:CHEBI:142694; Evidence={ECO:0000269|PubMed:10079066}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-tetradecanoyl-(2S)-hydroxyglycine = tetradecamide + CC glyoxylate; 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=N-decanoylglycine + 2 L-ascorbate + O2 = N-decanoyl-(2S)- CC hydroxyglycine + 2 monodehydro-L-ascorbate radical + H2O; 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=N-octanoylglycine + 2 L-ascorbate + O2 = N-octanoyl-(2S)- CC hydroxyglycine + 2 monodehydro-L-ascorbate radical + H2O; 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 = octanamide + glyoxylate; 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 Evidence={ECO:0000269|PubMed:19604476}; CC Note=Binds one Zn(2+) ion per subunit. {ECO:0000269|PubMed:19604476}; CC -!- COFACTOR: CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; CC Evidence={ECO:0000269|PubMed:10504734, ECO:0000269|PubMed:15131304, CC ECO:0000269|PubMed:16100265, ECO:0000269|PubMed:20958070, CC ECO:0000269|PubMed:23247335, ECO:0000269|PubMed:30271955, CC ECO:0000269|PubMed:36880254, ECO:0000269|PubMed:7893699}; CC Note=Binds 2 Cu(2+) ions per subunit. {ECO:0000269|PubMed:10504734, CC ECO:0000269|PubMed:15131304, ECO:0000269|PubMed:16100265, CC ECO:0000269|PubMed:20958070, ECO:0000269|PubMed:23247335, CC ECO:0000269|PubMed:30271955, ECO:0000269|PubMed:36880254}; 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 KM=6.3 uM for Ac-Tyr-Val-Gly peptide {ECO:0000269|PubMed:36880254}; CC Note=kcat is 15 sec(-1) with Ac-Tyr-Val-Gly peptide as substrate. CC {ECO:0000269|PubMed:36880254}; CC -!- SUBUNIT: Monomer (PubMed:15131304, PubMed:16100265, PubMed:19604476, CC PubMed:20958070, PubMed:23247335, PubMed:30271955). Interacts with CC RASSF9 (PubMed:9837933). {ECO:0000269|PubMed:15131304, CC ECO:0000269|PubMed:16100265, ECO:0000269|PubMed:19604476, CC ECO:0000269|PubMed:20958070, ECO:0000269|PubMed:23247335, CC ECO:0000269|PubMed:30271955, 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 -!- SUBCELLULAR LOCATION: [Isoform PAM-1]: Membrane CC {ECO:0000305|PubMed:2401356}. CC -!- SUBCELLULAR LOCATION: [Isoform PAM-2]: Membrane CC {ECO:0000305|PubMed:2401356}. CC -!- SUBCELLULAR LOCATION: [Isoform PAM-3]: Secreted CC {ECO:0000305|PubMed:2401356}. CC -!- SUBCELLULAR LOCATION: [Isoform PAM-3A]: Secreted CC {ECO:0000305|PubMed:2401356}. CC -!- SUBCELLULAR LOCATION: [Isoform PAM-3B]: Membrane CC {ECO:0000305|PubMed:2401356}. CC -!- SUBCELLULAR LOCATION: [Isoform PAM-4]: Secreted CC {ECO:0000305|PubMed:2401356}. CC -!- SUBCELLULAR LOCATION: [Isoform PAM-5]: Secreted CC {ECO:0000305|PubMed:2401356}. 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 -!- 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U52650; AAC05602.1; -; Genomic_DNA. DR EMBL; U52639; AAC05602.1; JOINED; Genomic_DNA. DR EMBL; U52640; AAC05602.1; JOINED; Genomic_DNA. DR EMBL; U52641; AAC05602.1; JOINED; Genomic_DNA. DR EMBL; U52642; AAC05602.1; JOINED; Genomic_DNA. DR EMBL; U52643; AAC05602.1; JOINED; Genomic_DNA. DR EMBL; U52644; AAC05602.1; JOINED; Genomic_DNA. DR EMBL; U52645; AAC05602.1; JOINED; Genomic_DNA. DR EMBL; U52646; AAC05602.1; JOINED; Genomic_DNA. DR EMBL; U52647; AAC05602.1; JOINED; Genomic_DNA. DR EMBL; U52648; AAC05602.1; JOINED; Genomic_DNA. DR EMBL; U52649; AAC05602.1; JOINED; Genomic_DNA. DR EMBL; U52653; AAC05603.1; -; Genomic_DNA. DR EMBL; U52639; AAC05603.1; JOINED; Genomic_DNA. DR EMBL; U52640; AAC05603.1; JOINED; Genomic_DNA. DR EMBL; U52641; AAC05603.1; JOINED; Genomic_DNA. DR EMBL; U52642; AAC05603.1; JOINED; Genomic_DNA. DR EMBL; U52643; AAC05603.1; JOINED; Genomic_DNA. DR EMBL; U52644; AAC05603.1; JOINED; Genomic_DNA. DR EMBL; U52645; AAC05603.1; JOINED; Genomic_DNA. DR EMBL; U52646; AAC05603.1; JOINED; Genomic_DNA. DR EMBL; U52647; AAC05603.1; JOINED; Genomic_DNA. DR EMBL; U52648; AAC05603.1; JOINED; Genomic_DNA. DR EMBL; U52649; AAC05603.1; JOINED; Genomic_DNA. DR EMBL; U52651; AAC05603.1; JOINED; Genomic_DNA. DR EMBL; U52652; AAC05603.1; JOINED; Genomic_DNA. DR EMBL; U52664; AAC05607.1; -; Genomic_DNA. DR EMBL; U52639; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52640; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52641; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52642; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52643; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52644; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52645; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52646; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52647; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52648; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52649; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52651; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52652; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52653; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52654; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52655; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52656; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52657; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52658; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52659; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52660; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52661; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52662; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52663; AAC05607.1; JOINED; Genomic_DNA. DR EMBL; U52664; AAC05605.1; -; Genomic_DNA. DR EMBL; U52639; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52640; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52641; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52642; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52643; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52644; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52645; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52646; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52647; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52648; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52649; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52651; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52652; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52654; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52655; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52656; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52657; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52658; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52659; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52660; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52661; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52662; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52663; AAC05605.1; JOINED; Genomic_DNA. DR EMBL; U52664; AAC05604.1; -; Genomic_DNA. DR EMBL; U52639; AAC05604.1; JOINED; Genomic_DNA. DR EMBL; U52640; AAC05604.1; JOINED; Genomic_DNA. DR EMBL; U52641; AAC05604.1; JOINED; Genomic_DNA. DR EMBL; U52642; AAC05604.1; JOINED; Genomic_DNA. DR EMBL; U52643; AAC05604.1; JOINED; Genomic_DNA. 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_013000.3. [P14925-1] DR RefSeq; XP_038938968.1; XM_039083040.2. [P14925-1] DR RefSeq; XP_038938972.1; XM_039083044.2. [P14925-2] DR RefSeq; XP_038938975.1; XM_039083047.2. [P14925-5] DR RefSeq; XP_038938976.1; XM_039083048.2. [P14925-4] DR RefSeq; XP_038938977.1; XM_039083049.2. [P14925-3] DR RefSeq; XP_063122756.1; XM_063266686.1. [P14925-1] DR RefSeq; XP_063122758.1; XM_063266688.1. [P14925-2] DR RefSeq; XP_063122759.1; XM_063266689.1. [P14925-2] DR RefSeq; XP_063122761.1; XM_063266691.1. [P14925-5] DR RefSeq; XP_063122762.1; XM_063266692.1. [P14925-5] DR RefSeq; XP_063122764.1; XM_063266694.1. [P14925-4] DR RefSeq; XP_063122765.1; XM_063266695.1. [P14925-3] 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 PDB; 8DSJ; X-ray; 2.80 A; A/K=45-354. DR PDB; 8DSL; X-ray; 2.05 A; A/B=45-354. DR PDB; 8DSN; X-ray; 2.80 A; A/K=45-354. DR AlphaFoldDB; P14925; -. DR MDposit; P14925; -. DR SMR; P14925; -. DR BioGRID; 247540; 4. DR FunCoup; P14925; 853. DR IntAct; P14925; 3. DR STRING; 10116.ENSRNOP00000046774; -. DR BindingDB; P14925; -. DR ChEMBL; CHEMBL4963; -. DR GlyCosmos; P14925; 1 site, No reported glycans. DR GlyGen; P14925; 1 site. DR iPTMnet; P14925; -. DR PhosphoSitePlus; P14925; -. DR jPOST; P14925; -. DR PaxDb; 10116-ENSRNOP00000046774; -. DR Ensembl; ENSRNOT00000118414.2; ENSRNOP00000087123.2; ENSRNOG00000033280.9. [P14925-7] DR GeneID; 25508; -. DR KEGG; rno:25508; -. DR AGR; RGD:3252; -. 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; AADHRFG; -. 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 cell types or tissues. DR ExpressionAtlas; P14925; baseline and differential. 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; 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:0030141; C:secretory granule; 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: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:0062112; P:fatty acid primary amide biosynthetic process; IDA:UniProtKB. DR GO; GO:0007507; P:heart development; 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: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:0051604; P:protein maturation; ISO:RGD. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; 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 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; 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; Secreted; KW Signal; 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 /evidence="ECO:0000269|PubMed:10504734" 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 COMPBIAS 952..965 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 107 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:10504734, FT ECO:0000269|PubMed:15131304, ECO:0000269|PubMed:16100265, FT ECO:0000269|PubMed:20958070, ECO:0000269|PubMed:23247335, FT ECO:0000269|PubMed:36880254, ECO:0007744|PDB:1OPM, FT ECO:0007744|PDB:1SDW, ECO:0007744|PDB:1YIP, FT ECO:0007744|PDB:3MIB, ECO:0007744|PDB:3PHM, FT ECO:0007744|PDB:4E4Z, ECO:0007744|PDB:8DSJ" FT BINDING 108 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:10504734, FT ECO:0000269|PubMed:15131304, ECO:0000269|PubMed:16100265, FT ECO:0000269|PubMed:20958070, ECO:0000269|PubMed:23247335, FT ECO:0000269|PubMed:36880254, ECO:0007744|PDB:1OPM, FT ECO:0007744|PDB:1SDW, ECO:0007744|PDB:1YIP, FT ECO:0007744|PDB:3MIB, ECO:0007744|PDB:3PHM, FT ECO:0007744|PDB:4E4Z, ECO:0007744|PDB:8DSJ" FT BINDING 172 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:10504734, FT ECO:0000269|PubMed:15131304, ECO:0000269|PubMed:16100265, FT ECO:0000269|PubMed:20958070, ECO:0000269|PubMed:23247335, FT ECO:0000269|PubMed:36880254, ECO:0007744|PDB:1OPM, FT ECO:0007744|PDB:1SDW, ECO:0007744|PDB:1YIP, FT ECO:0007744|PDB:3MIB, ECO:0007744|PDB:3PHM, FT ECO:0007744|PDB:4E4Z, ECO:0007744|PDB:8DSJ" FT BINDING 242 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:10504734, FT ECO:0000269|PubMed:15131304, ECO:0000269|PubMed:16100265, FT ECO:0000269|PubMed:20958070, ECO:0000269|PubMed:23247335, FT ECO:0000269|PubMed:30271955, ECO:0000269|PubMed:36880254, FT ECO:0007744|PDB:1OPM, ECO:0007744|PDB:1SDW, FT ECO:0007744|PDB:1YIP, ECO:0007744|PDB:3MIB, FT ECO:0007744|PDB:3PHM, ECO:0007744|PDB:4E4Z, FT ECO:0007744|PDB:6ALV, ECO:0007744|PDB:8DSJ" FT BINDING 244 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:10504734, FT ECO:0000269|PubMed:15131304, ECO:0000269|PubMed:16100265, FT ECO:0000269|PubMed:20958070, ECO:0000269|PubMed:23247335, FT ECO:0000269|PubMed:30271955, ECO:0000269|PubMed:36880254, FT ECO:0007744|PDB:1OPM, ECO:0007744|PDB:1SDW, FT ECO:0007744|PDB:1YIP, ECO:0007744|PDB:3MIB, FT ECO:0007744|PDB:3PHM, ECO:0007744|PDB:4E4Z, FT ECO:0007744|PDB:6ALV, ECO:0007744|PDB:8DSJ" FT BINDING 314 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:10504734, FT ECO:0000269|PubMed:15131304, ECO:0000269|PubMed:20958070, FT ECO:0000269|PubMed:23247335, ECO:0000269|PubMed:30271955, FT ECO:0000269|PubMed:36880254, ECO:0007744|PDB:1OPM, FT ECO:0007744|PDB:1SDW, ECO:0007744|PDB:3MIB, FT ECO:0007744|PDB:3PHM, ECO:0007744|PDB:4E4Z, FT ECO:0007744|PDB:6ALV, ECO:0007744|PDB:8DSJ" 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="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:0000305|PubMed:19604476, FT ECO:0007744|PDB:3FW0" 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="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:0000305|PubMed:19604476, FT ECO:0007744|PDB:3FW0" 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="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:0000305|PubMed:19604476, FT ECO:0007744|PDB:3FW0" 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 ECO:0000269|PubMed:15131304, ECO:0000269|PubMed:16100265, FT ECO:0000269|PubMed:20958070, ECO:0000269|PubMed:23247335, FT ECO:0000269|PubMed:30271955, ECO:0000269|PubMed:36880254, FT ECO:0007744|PDB:1SDW, ECO:0007744|PDB:1YIP, FT ECO:0007744|PDB:4E4Z, ECO:0007744|PDB:8DSJ" FT DISULFID 81..126 FT /evidence="ECO:0000269|PubMed:12369828, FT ECO:0000269|PubMed:15131304, ECO:0000269|PubMed:16100265, FT ECO:0000269|PubMed:20958070, ECO:0000269|PubMed:23247335, FT ECO:0000269|PubMed:30271955, ECO:0000269|PubMed:36880254, FT ECO:0007744|PDB:1SDW, ECO:0007744|PDB:1YIP, FT ECO:0007744|PDB:4E4Z, ECO:0007744|PDB:8DSJ" FT DISULFID 114..131 FT /evidence="ECO:0000269|PubMed:12369828, FT ECO:0000269|PubMed:15131304, ECO:0000269|PubMed:16100265, FT ECO:0000269|PubMed:20958070, ECO:0000269|PubMed:23247335, FT ECO:0000269|PubMed:30271955, ECO:0000269|PubMed:36880254, FT ECO:0007744|PDB:1SDW, ECO:0007744|PDB:1YIP, FT ECO:0007744|PDB:4E4Z, ECO:0007744|PDB:8DSJ" FT DISULFID 227..334 FT /evidence="ECO:0000269|PubMed:12369828, FT ECO:0000269|PubMed:15131304, ECO:0000269|PubMed:16100265, FT ECO:0000269|PubMed:20958070, ECO:0000269|PubMed:23247335, FT ECO:0000269|PubMed:30271955, ECO:0000269|PubMed:36880254, FT ECO:0007744|PDB:1SDW, ECO:0007744|PDB:1YIP, FT ECO:0007744|PDB:4E4Z, ECO:0007744|PDB:8DSJ" FT DISULFID 293..315 FT /evidence="ECO:0000269|PubMed:12369828, FT ECO:0000269|PubMed:15131304, ECO:0000269|PubMed:16100265, FT ECO:0000269|PubMed:20958070, ECO:0000269|PubMed:23247335, FT ECO:0000269|PubMed:30271955, ECO:0000269|PubMed:36880254, FT ECO:0007744|PDB:1SDW, ECO:0007744|PDB:1YIP, FT ECO:0007744|PDB:4E4Z, ECO:0007744|PDB:8DSJ" 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 107 FT /note="H->A: Impaired Cu(2+)-binding." FT /evidence="ECO:0000269|PubMed:30271955" FT MUTAGEN 108 FT /note="H->A: Impaired Cu(2+)-binding; forms a closed FT conformer in the presence of citrate with a reduced FT Cu(2+)-Cu(2+) site separation of 4 Angstroms. Abolished FT peptidylglycine alpha-hydroxylating monooxygenase FT activity." FT /evidence="ECO:0000269|PubMed:30271955, FT ECO:0000269|PubMed:7893699" FT MUTAGEN 172 FT /note="H->A: Impaired Cu(2+)-binding." FT /evidence="ECO:0000269|PubMed:30271955" FT MUTAGEN 244 FT /note="H->A: Abolished peptidylglycine alpha-hydroxylating FT monooxygenase activity." FT /evidence="ECO:0000269|PubMed:7893699" FT MUTAGEN 272 FT /note="Q->E,A: Induces a fully open peptidylglycine FT monooxygenase structure with Cu(2+) distances of 14 FT Angstroms." FT /evidence="ECO:0000269|PubMed:36880254" FT MUTAGEN 314 FT /note="M->I: Abolished peptidylglycine alpha-hydroxylating FT monooxygenase activity." FT /evidence="ECO:0000269|PubMed:7893699" FT MUTAGEN 533 FT /note="R->A: Abolishes peptidyl-alpha-hydroxyglycine FT alpha-amidating lyase activity." FT /evidence="ECO:0000269|PubMed:19604476" FT MUTAGEN 533 FT /note="R->Q: Abolishes peptidyl-alpha-hydroxyglycine FT alpha-amidating lyase activity." FT /evidence="ECO:0000269|PubMed:19604476" FT MUTAGEN 706 FT /note="R->A: Abolishes peptidyl-alpha-hydroxyglycine FT alpha-amidating lyase activity." FT /evidence="ECO:0000269|PubMed:19604476" FT MUTAGEN 706 FT /note="R->Q: Reduces peptidyl-alpha-hydroxyglycine FT alpha-amidating lyase activity." FT /evidence="ECO:0000269|PubMed:19604476" FT MUTAGEN 784 FT /note="M->A: Abolishes peptidyl-alpha-hydroxyglycine FT alpha-amidating lyase activity." FT /evidence="ECO:0000269|PubMed:19604476" FT MUTAGEN 784 FT /note="M->Q: Abolishes peptidyl-alpha-hydroxyglycine FT alpha-amidating lyase activity." FT /evidence="ECO:0000269|PubMed:19604476" FT MUTAGEN 787 FT /note="D->A: Reduces peptidyl-alpha-hydroxyglycine FT alpha-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 HELIX 146..151 FT /evidence="ECO:0007829|PDB:1YJK" 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:1YIP" 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 268..270 FT /evidence="ECO:0007829|PDB:8DSJ" FT STRAND 275..283 FT /evidence="ECO:0007829|PDB:1YI9" FT STRAND 288..296 FT /evidence="ECO:0007829|PDB:1YI9" FT STRAND 297..299 FT /evidence="ECO:0007829|PDB:8DSN" FT STRAND 304..306 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 TURN 540..542 FT /evidence="ECO:0007829|PDB:3FW0" 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 HELIX 749..752 FT /evidence="ECO:0007829|PDB:3FW0" 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 //