PHM_CAEEL
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 03-AUG-2022, entry version 125.
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 + 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: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_058497.6.
DR AlphaFoldDB; Q95XM2; -.
DR SMR; Q95XM2; -.
DR STRING; 6239.Y71G12B.4; -.
DR iPTMnet; Q95XM2; -.
DR EPD; Q95XM2; -.
DR PaxDb; Q95XM2; -.
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 CTD; 171746; -.
DR WormBase; Y71G12B.4; CE26253; WBGene00022144; pghm-1.
DR eggNOG; KOG3567; Eukaryota.
DR GeneTree; ENSGT00940000173843; -.
DR HOGENOM; CLU_051564_0_0_1; -.
DR InParanoid; Q95XM2; -.
DR OMA; PELYLCT; -.
DR OrthoDB; 1156284at2759; -.
DR PhylomeDB; Q95XM2; -.
DR PRO; PR:Q95XM2; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00022144; Expressed in larva and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
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; IEA:UniProtKB-EC.
DR GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.230; -; 1.
DR Gene3D; 2.60.120.310; -; 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 Pfam; PF03712; Cu2_monoox_C; 1.
DR Pfam; PF01082; Cu2_monooxygen; 1.
DR PRINTS; PR00790; PAMONOXGNASE.
DR SUPFAM; SSF49742; SSF49742; 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
