AMD_MOUSE
ID AMD_MOUSE Reviewed; 979 AA.
AC P97467; E9QL07;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Peptidyl-glycine alpha-amidating monooxygenase {ECO:0000250|UniProtKB:P19021};
DE Short=PAM {ECO:0000250|UniProtKB:P19021};
DE Includes:
DE RecName: Full=Peptidylglycine alpha-hydroxylating monooxygenase {ECO:0000250|UniProtKB:P19021};
DE Short=PHM {ECO:0000250|UniProtKB:P19021};
DE EC=1.14.17.3 {ECO:0000250|UniProtKB:P19021};
DE Includes:
DE RecName: Full=Peptidyl-alpha-hydroxyglycine alpha-amidating lyase;
DE EC=4.3.2.5 {ECO:0000250|UniProtKB:P19021};
DE AltName: Full=Peptidylamidoglycolate lyase {ECO:0000250|UniProtKB:P19021};
DE Short=PAL {ECO:0000250|UniProtKB:P19021};
DE Flags: Precursor;
GN Name=Pam;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jeong J.H., Baek S.J., Park D.H.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924; SER-925 AND SER-935, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION.
RX PubMed=27016726; DOI=10.1194/jlr.m062042;
RA Jeffries K.A., Dempsey D.R., Farrell E.K., Anderson R.L., Garbade G.J.,
RA Gurina T.S., Gruhonjic I., Gunderson C.A., Merkler D.J.;
RT "Glycine N-acyltransferase-like 3 is responsible for long-chain N-
RT acylglycine formation in N18TG2 cells.";
RL J. Lipid Res. 57:781-790(2016).
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 (By similarity). 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 (By similarity). Similarly, catalyzes the two-
CC step conversion of an N-fatty acylglycine to a primary fatty acid amide
CC and glyoxylate (Probable). {ECO:0000250|UniProtKB:P10731,
CC ECO:0000250|UniProtKB:P14925, ECO:0000250|UniProtKB:P19021,
CC ECO:0000305|PubMed:27016726}.
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:0000250|UniProtKB:P14925};
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:0000250|UniProtKB:P14925};
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:0000250|UniProtKB:P14925};
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:0000250|UniProtKB:P14925};
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:0000250|UniProtKB:P14925};
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:0000250|UniProtKB:P14925};
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:0000250|UniProtKB:P14925};
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:0000250|UniProtKB:P14925};
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:0000250|UniProtKB:P14925};
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:0000250|UniProtKB:P14925};
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:0000250|UniProtKB:P14925};
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:0000250|UniProtKB:P14925};
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:0000250|UniProtKB:P14925};
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:0000250|UniProtKB:P14925};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P14925};
CC Note=Binds one Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:P14925};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:P14925};
CC Note=Binds 2 Cu(2+) ions per subunit. {ECO:0000250|UniProtKB:P14925};
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 (By similarity).
CC {ECO:0000250|UniProtKB:P14925, ECO:0000250|UniProtKB:P19021}.
CC -!- SUBUNIT: Monomer. Interacts with RASSF9.
CC {ECO:0000250|UniProtKB:P14925}.
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 -!- 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}.
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DR EMBL; U79523; AAB38364.1; -; mRNA.
DR EMBL; AC102191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC157923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS87863.1; -.
DR RefSeq; NP_038654.2; NM_013626.3.
DR RefSeq; XP_006529307.1; XM_006529244.3.
DR AlphaFoldDB; P97467; -.
DR SMR; P97467; -.
DR BioGRID; 202023; 4.
DR IntAct; P97467; 2.
DR STRING; 10090.ENSMUSP00000057112; -.
DR GlyGen; P97467; 1 site.
DR iPTMnet; P97467; -.
DR PhosphoSitePlus; P97467; -.
DR CPTAC; non-CPTAC-3445; -.
DR MaxQB; P97467; -.
DR PaxDb; P97467; -.
DR PRIDE; P97467; -.
DR ProteomicsDB; 281968; -.
DR Antibodypedia; 25194; 154 antibodies from 33 providers.
DR DNASU; 18484; -.
DR Ensembl; ENSMUST00000058762; ENSMUSP00000057112; ENSMUSG00000026335.
DR GeneID; 18484; -.
DR KEGG; mmu:18484; -.
DR UCSC; uc007cfp.1; mouse.
DR CTD; 5066; -.
DR MGI; MGI:97475; Pam.
DR VEuPathDB; HostDB:ENSMUSG00000026335; -.
DR eggNOG; KOG3567; Eukaryota.
DR GeneTree; ENSGT00940000156369; -.
DR InParanoid; P97467; -.
DR OMA; KRNPQWP; -.
DR OrthoDB; 476471at2759; -.
DR PhylomeDB; P97467; -.
DR TreeFam; TF320698; -.
DR BRENDA; 1.14.17.3; 3474.
DR BioGRID-ORCS; 18484; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Pam; mouse.
DR PRO; PR:P97467; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P97467; protein.
DR Bgee; ENSMUSG00000026335; Expressed in aortic valve and 223 other tissues.
DR ExpressionAtlas; P97467; baseline and differential.
DR Genevisible; P97467; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:MGI.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0030667; C:secretory granule membrane; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0004598; F:peptidylamidoglycolate lyase activity; ISS:UniProtKB.
DR GO; GO:0004504; F:peptidylglycine monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR GO; GO:0062112; P:fatty acid primary amide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:0060173; P:limb development; IEA:Ensembl.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISO:MGI.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
DR GO; GO:0022602; P:ovulation cycle process; IEA:Ensembl.
DR GO; GO:0001519; P:peptide amidation; ISS:UniProtKB.
DR GO; GO:0006518; P:peptide metabolic process; ISO:MGI.
DR GO; GO:0018032; P:protein amidation; ISO:MGI.
DR GO; GO:0019538; P:protein metabolic process; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0050708; P:regulation of protein secretion; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0046688; P:response to copper ion; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0009268; P:response to pH; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0010043; P:response to zinc ion; ISO:MGI.
DR GO; GO:0009404; P:toxin metabolic process; ISO:MGI.
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 Calcium; Cleavage on pair of basic residues; Copper; Cytoplasmic vesicle;
KW Disulfide bond; Glycoprotein; Lipid metabolism; Lyase; Membrane;
KW Metal-binding; Monooxygenase; Multifunctional enzyme; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Vitamin C; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT PROPEP 25..34
FT /evidence="ECO:0000250"
FT /id="PRO_0000006363"
FT CHAIN 35..979
FT /note="Peptidyl-glycine alpha-amidating monooxygenase"
FT /id="PRO_0000006364"
FT TOPO_DOM 35..869
FT /note="Intragranular"
FT /evidence="ECO:0000255"
FT TRANSMEM 870..893
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 894..979
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:0000250"
FT REGION 498..823
FT /note="Peptidyl-alpha-hydroxyglycine alpha-amidating lyase"
FT /evidence="ECO:0000250"
FT REGION 931..948
FT /note="Interaction with RASSF9"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT REGION 943..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 107
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 171
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 241
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 243
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 313
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 520
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 533
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 585
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 587
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 654
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 690
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 706
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 786
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 787
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 925
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19021"
FT MOD_RES 949
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19021"
FT MOD_RES 952
FT /note="Phosphoserine; by UHMK1"
FT /evidence="ECO:0000250|UniProtKB:P19021"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..185
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT DISULFID 80..125
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT DISULFID 113..130
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT DISULFID 226..333
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT DISULFID 292..314
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT DISULFID 634..655
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT DISULFID 702..713
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT CONFLICT 970
FT /note="A -> R (in Ref. 1; AAB38364)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 979 AA; 108963 MW; 1F4C7276567A741A CRC64;
MAGRARSRLL LLLGLLALQS SCLAFRSPLS VFKRFKETTR SFSNECLGTT RPITPIDSSD
FTLDIRMPGV TPKESDTYFC MSMRLPVDEE AFVIDFKPRA SMDTVHHMLL FGCNMPSSTG
SYWFCDEGTC TDKANILYAW ARNAPPTRLP KGVGFRVGGE TGSKYFVLQV HYGDISAFRD
NHKDCSGVSL HLTRVPQPLI AGMYLMMSVN TVIPPGEKVV NSDISCHYKM YPMHVFAYRV
HTHHLGKVVS GYRVRNGQWT LIGRQSPQLP QAFYPVEHPV DVAFGDILAA RCVFTGEGRT
EATHIGGTSS DEMCNLYIMY YMEAKHAVSF MTCTQNVAPD MFRTIPEEAN IPIPVKSDMV
MIHGHHKETE NKEKSALIQQ PKQGEEEAFE QGDFYSLLSK LLGEREDVVH VHKYNPTEKT
ESGSDLVAEI ANVVQKKDLG RSDAREGAEH EEGGNAILVR DRIHKFHRLE STLRPAESRA
LSFQQPGEGP WEPELAGDFH VEEALEWPGV YLLPGQVSGV ALDSKNNLVI FHRGDHVWDG
NSFDSKFVYQ QRGLGPIEED TILVIDPNKA EILQSSGKNL FYLPHGLSID TDGNYWVTDV
ALHQVFKLEP RSKEGPLLVL GRSMQPGSDQ NHFCQPTDVA VEPSTGAVFV SDGYCNSRIV
QFSPSGKFIT QWGEESSGSS PKPGQFSVPH SLALVPHLNQ LCVADRENGR IQCFKTDTKE
FVREIKHASF GRNVFAISYI PGFLFAVNGK PYFGDQEPVQ GFVMNFSSGE IIDVFKPVRK
HFDMPHDIVA SEDGTVYIGD AHTNTVWKFT LTESRLEVEH RSVKKAGIEV PEIKEAEAVV
EPKVKNKPTS SELQKMQEKK KLIKDPGSGV PVVLITTLLV IPVVVLLAIA MFIRWKKSRA
FGDHDRKLES SSGRVLGRLR GKGSSGLNLG NFFASRKGYS RKGFDRVSTE GSDQEKDEDD
GSESEEEYSA PLPTPAPSS
