ID   PHM_CAEEL               Reviewed;         324 AA.
AC   Q95XM2;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   02-SEP-2026, entry version 142.
DE   RecName: Full=Probable peptidylglycine alpha-hydroxylating monooxygenase 1 {ECO:0000312|WormBase:Y71G12B.4};
DE            Short=PHM {ECO:0000305};
DE            EC=1.14.17.3 {ECO:0000250|UniProtKB:O01404};
DE   Flags: Precursor;
GN   Name=pghm-1 {ECO:0000312|WormBase:Y71G12B.4};
GN   ORFNames=Y71G12B.4 {ECO:0000312|WormBase:Y71G12B.4};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-182, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=12754521; DOI=10.1038/nbt829;
RA   Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA   Kasai K., Takahashi N., Isobe T.;
RT   "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT   identify N-linked glycoproteins.";
RL   Nat. Biotechnol. 21:667-672(2003).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-182, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
CC   -!- FUNCTION: Monooxygenase that catalyzes an essential reaction in C-
CC       terminal alpha-amidation of peptides. Produces an unstable peptidyl(2-
CC       hydroxyglycine) intermediate. C-terminal amidation of peptides such as
CC       neuropeptides is essential for full biological activity.
CC       {ECO:0000250|UniProtKB:O01404}.
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:0000250|UniProtKB:O01404};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:O01404};
CC       Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:O01404};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC       monooxygenase family. {ECO:0000305}.
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DR   EMBL; FO080942; CCD67961.1; -; Genomic_DNA.
DR   RefSeq; NP_490898.1; NM_058497.8.
DR   AlphaFoldDB; Q95XM2; -.
DR   SMR; Q95XM2; -.
DR   FunCoup; Q95XM2; 497.
DR   STRING; 6239.Y71G12B.4.1; -.
DR   GlyCosmos; Q95XM2; 1 site, No reported glycans.
DR   iPTMnet; Q95XM2; -.
DR   PaxDb; 6239-Y71G12B.4.1; -.
DR   PeptideAtlas; Q95XM2; -.
DR   EnsemblMetazoa; Y71G12B.4.1; Y71G12B.4.1; WBGene00022144.
DR   GeneID; 171746; -.
DR   KEGG; cel:CELE_Y71G12B.4; -.
DR   UCSC; Y71G12B.4; c. elegans.
DR   AGR; WB:WBGene00022144; -.
DR   CTD; 171746; -.
DR   WormBase; Y71G12B.4; CE26253; WBGene00022144; pghm-1.
DR   eggNOG; KOG3567; Eukaryota.
DR   HOGENOM; CLU_051564_0_0_1; -.
DR   InParanoid; Q95XM2; -.
DR   OMA; PELYLCT; -.
DR   OrthoDB; 10044505at2759; -.
DR   PhylomeDB; Q95XM2; -.
DR   PRO; PR:Q95XM2; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00022144; Expressed in larva and 3 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004504; F:peptidylglycine monooxygenase activity; ISS:UniProtKB.
DR   GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR   FunFam; 2.60.120.310:FF:000005; Peptidylglycine alpha-hydroxylating monooxygenase; 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   InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
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; 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   PRINTS; PR00790; PAMONOXGNASE.
DR   SUPFAM; SSF49742; PHM/PNGase F; 2.
DR   PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1.
PE   1: Evidence at protein level;
KW   Copper; Disulfide bond; Glycoprotein; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..324
FT                   /note="Probable peptidylglycine alpha-hydroxylating
FT                   monooxygenase 1"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000248570"
FT   BINDING         66
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754521,
FT                   ECO:0000269|PubMed:17761667"
FT   DISULFID        41..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..101
FT                   /evidence="ECO:0000250"
FT   DISULFID        264..285
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  36647 MW;  46877A0A988B859E CRC64;
     MPRFYLLSSC ALLAFATSFC NAEKSQIRMP GVVPEADSYL CTSLELSDQE NYLTGFKALT
     TKGTAHHILL FGCEEPGSDE LVWDCGEMNK PDDEMPRAPT CGSKPAILYA WALDAPPLEL
     PQDVGFRVGG DSNIRHLVMQ VHYMHSKQEP DETGLEITHT EEPQPKLAAT MLLVTGGTLP
     RNKTESFETA CMIEEDVVMH PFAYRTHTHR HGKEVSGWLV KEDQKHEDHW KLIGRRDPQL
     AQMFVPVEDQ AMTIQQGDMV TARCILQNNE NRDISMGATE EDEMCNFYIM YWTDGEVMQD
     NTCYSPGAPD YKWAREADLN HIPK
//