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nas-39 Zinc metalloproteinase nas-39 [ Caenorhabditis elegans ]

Gene ID: 3565986, updated on 9-Dec-2024

Summary

Official Symbol
nas-39
Official Full Name
Zinc metalloproteinase nas-39
Primary source
WormBase:WBGene00003555
Locus tag
CELE_F38E9.2
See related
AllianceGenome:WB:WBGene00003555
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 metalloendopeptidase activity. Predicted to be involved in dorsal/ventral pattern formation and protein processing. Predicted to be located in extracellular region. Predicted to be active in extracellular space. Is expressed in body wall musculature; intestine; nervous system; non-striated muscle; and reproductive system. Human ortholog(s) of this gene implicated in atrial heart septal defect 6; congenital heart disease; coronary artery disease; and osteogenesis imperfecta type 13. Orthologous to several human genes including BMP1 (bone morphogenetic protein 1) and TLL2 (tolloid like 2). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

See nas-39 in Genome Data Viewer
Location:
chromosome: X
Exon count:
25
Sequence:
Chromosome: X; NC_003284.9 (16456927..16471333)

Chromosome X - NC_003284.9Genomic Context describing neighboring genes Neighboring gene ADF-H domain-containing protein Neighboring gene Uncharacterized protein Neighboring gene ncRNA Neighboring gene tRNA-Arg Neighboring gene PLCXc domain-containing protein Neighboring gene ncRNA Neighboring gene ncRNA

General gene information

Markers

Gene Ontology Provided by WormBase

Function Evidence Code Pubs
enables calcium ion binding IEA
Inferred from Electronic Annotation
more info
 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
 
enables metalloendopeptidase activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables metalloendopeptidase activity IEA
Inferred from Electronic Annotation
more info
 
enables metallopeptidase activity IEA
Inferred from Electronic Annotation
more info
 
enables metallopeptidase activity ISS
Inferred from Sequence or Structural Similarity
more info
PubMed 
enables serine-type endopeptidase activity IEA
Inferred from Electronic Annotation
more info
 
enables zinc ion binding IEA
Inferred from Electronic Annotation
more info
 
Process Evidence Code Pubs
involved_in dorsal/ventral pattern formation IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in protein processing IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in proteolysis IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
located_in extracellular region IEA
Inferred from Electronic Annotation
more info
 
is_active_in extracellular space IBA
Inferred from Biological aspect of Ancestor
more info
 

General protein information

Preferred Names
Zinc metalloproteinase nas-39
NP_001360030.1
  • 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_003284.9 Reference assembly

    Range
    16456927..16471333
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001373610.4NP_001360030.1  Zinc metalloproteinase nas-39 [Caenorhabditis elegans]

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    Q20176
    Conserved Domains (5) summary
    smart00042
    Location:268343
    CUB; Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein
    cd00041
    Location:669780
    CUB; CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.
    cd04281
    Location:48247
    ZnMc_BMP1_TLD; Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) and TLD (tolloid)-like metalloproteases play vital roles in extracellular matrix formation, by cleaving precursor proteins such as enzymes, structural proteins, ...
    pfam00431
    Location:519622
    CUB; CUB domain
    pfam14670
    Location:629664
    FXa_inhibition; Coagulation Factor Xa inhibitory site