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   24-JAN-2024, entry version 185.
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,
RC   Pancreas, 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; 5.
DR   IntAct; P97467; 2.
DR   STRING; 10090.ENSMUSP00000095228; -.
DR   GlyCosmos; P97467; 1 site, No reported glycans.
DR   GlyGen; P97467; 1 site.
DR   iPTMnet; P97467; -.
DR   PhosphoSitePlus; P97467; -.
DR   SwissPalm; P97467; -.
DR   CPTAC; non-CPTAC-3445; -.
DR   MaxQB; P97467; -.
DR   PaxDb; 10090-ENSMUSP00000057112; -.
DR   ProteomicsDB; 281968; -.
DR   Pumba; P97467; -.
DR   Antibodypedia; 25194; 169 antibodies from 33 providers.
DR   DNASU; 18484; -.
DR   Ensembl; ENSMUST00000058762.15; ENSMUSP00000057112.9; ENSMUSG00000026335.17.
DR   GeneID; 18484; -.
DR   KEGG; mmu:18484; -.
DR   UCSC; uc007cfp.1; mouse.
DR   AGR; MGI:97475; -.
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; 2908431at2759; -.
DR   PhylomeDB; P97467; -.
DR   TreeFam; TF320698; -.
DR   BRENDA; 1.14.17.3; 3474.
DR   BioGRID-ORCS; 18484; 4 hits in 76 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 224 other cell types or tissues.
DR   ExpressionAtlas; P97467; baseline and differential.
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: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; TAS: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:0062112; P:fatty acid primary amide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; ISO:MGI.
DR   GO; GO:0001519; P:peptide amidation; ISS:UniProtKB.
DR   GO; GO:0006518; P:peptide metabolic process; ISO:MGI.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
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   CDD; cd14958; NHL_PAL_like; 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.
DR   Genevisible; P97467; MM.
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(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P14925"
FT   BINDING         107
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P14925"
FT   BINDING         171
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P14925"
FT   BINDING         241
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P14925"
FT   BINDING         243
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P14925"
FT   BINDING         313
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
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="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: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="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: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="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: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
//