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pghm-1 putative peptidylglycine alpha-hydroxylating monooxygenase 1 [ Caenorhabditis elegans ]

Gene ID: 171746, updated on 9-Dec-2024

Summary

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Official Symbol
pghm-1
Official Full Name
putative peptidylglycine alpha-hydroxylating monooxygenase 1
Primary source
WormBase:WBGene00022144
Locus tag
CELE_Y71G12B.4
See related
AllianceGenome:WB:WBGene00022144
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Caenorhabditis elegans (strain: Bristol N2)
Lineage
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary
Predicted to enable copper ion binding activity and peptidylglycine monooxygenase activity. Predicted to be involved in peptide metabolic process. Predicted to be located in extracellular region and membrane. Is expressed in nervous system. [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See pghm-1 in Genome Data Viewer
Location:
chromosome: I
Exon count:
3
Sequence:
Chromosome: I; NC_003279.8 (1808092..1811835)

Chromosome I - NC_003279.8Genomic Context describing neighboring genes Neighboring gene Cyclin-dependent kinases regulatory subunit Neighboring gene Apolipophorin Neighboring gene Uncharacterized protein Neighboring gene FBA_2 domain-containing protein Neighboring gene DUF38 domain-containing protein

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_003279.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Mass spectrometric evidence for neuropeptide-amidating enzymes in Caenorhabditis elegans. Van Bael S, et al. J Biol Chem, 2018 Apr 20. PMID 29487130, Free PMC Article
  2. Genome sequence of the nematode C. elegans: a platform for investigating biology. C. elegans Sequencing Consortium. Science, 1998 Dec 11. PMID 9851916

GeneRIFs: Gene References Into Functions

General gene information

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Markers

Homology

Gene Ontology Provided by WormBase

Function Evidence Code Pubs
enables catalytic activity IEA
Inferred from Electronic Annotation
more info
  
enables copper ion binding IEA
Inferred from Electronic Annotation
more info
  
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables monooxygenase activity IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen IEA
Inferred from Electronic Annotation
more info
  
enables peptidylglycine monooxygenase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in peptide metabolic process IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in extracellular region IEA
Inferred from Electronic Annotation
more info
  
located_in membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
putative peptidylglycine alpha-hydroxylating monooxygenase 1
NP_490898.1
  • Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_003279.8 Reference assembly

    Range
    1808092..1811835
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_058497.8 → NP_490898.1  putative peptidylglycine alpha-hydroxylating monooxygenase 1 [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_490898.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    Q95XM2
    Conserved Domains (2) summary
    pfam01082
    Location:27 → 145
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:167 → 313
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q95XM2.1

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