nas-9 Zinc metalloproteinase nas-9 [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: nas-9
Official Full Name: Zinc metalloproteinase nas-9
Primary source: WormBase:WBGene00003528
Locus tag: CELE_C37H5.9
See related: AllianceGenome:WB:WBGene00003528
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 proteolysis. Predicted to be located in extracellular region. Is expressed in hypodermis; spermatheca; and uterus. [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See nas-9 in Genome Data Viewer

Location:: chromosome: V

Exon count:: 9

Sequence:: Chromosome: V; NC_003283.11 (4836027..4840013, complement)

Chromosome V - NC_003283.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003283.11

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

C37H5.10 (e-PCR)
- UniSTS:320877

C37H5.9 (e-PCR)
- UniSTS:313827

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
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 zinc ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
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

General protein information

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Preferred Names: Zinc metalloproteinase nas-9

NP_001379790.1

Confirmed by transcript evidence

NP_741531.1

Partially confirmed by transcript evidence

NP_741532.1

Partially 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

NC_003283.11 Reference assembly

Range

4836027..4840013 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001392505.1 → NP_001379790.1 Zinc metalloproteinase nas-9 [Caenorhabditis elegans]

Status: REVIEWED

Conserved Domains (2) summary

smart00254
Location:436 → 472

ShKT; ShK toxin domain

pfam01400
Location:237 → 431

Astacin; Astacin (Peptidase family M12A)
NM_171927.3 → NP_741532.1 Zinc metalloproteinase nas-9 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_741532.1

Status: REVIEWED

UniProtKB/Swiss-Prot

P91137, Q8I7H6, Q95Q69

Conserved Domains (3) summary

smart00254
Location:510 → 546

ShKT; ShK toxin domain

cd04280
Location:316 → 505

ZnMc_astacin_like; Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of zinc-dependent proteolytic enzymes with a HExxH zinc-binding site/active site. Members of this family may have an amino terminal propeptide, which is cleaved to ...

pfam01400
Location:311 → 505

Astacin; Astacin (Peptidase family M12A)
NM_171452.2 → NP_741531.1 Zinc metalloproteinase nas-9 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_741531.1

Status: REVIEWED

UniProtKB/Swiss-Prot

P91137

Conserved Domains (3) summary

smart00254
Location:481 → 517

ShKT; ShK toxin domain

pfam01400
Location:311 → 476

Astacin; Astacin (Peptidase family M12A)

cl00064
Location:316 → 476

ZnMc; Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which ...