Reviewed,
UniProtKB/Swiss-Prot Q22396 (NAS20_CAEEL)
Last modified
June 16, 2009.
Version 62.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Zinc metalloproteinase nas-20 EC=3.4.24.21 Alternative name(s): Nematode astacin 20 | ||||
| Gene names |
| ||||
| Organism | Caenorhabditis elegans [Complete proteome] | ||||
| Taxonomic identifier | 6239 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis |
Protein attributes
| Sequence length | 379 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Probable metalloprotease By similarity. |
| Catalytic activity | Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Subcellular location | Secreted Potential. |
| Sequence similarities | Belongs to the peptidase M12A family. Contains 1 EGF-like domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | EGF-like domain Signal |
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase Metalloprotease Protease |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 20 | 20 | Potential | ||||||||
| Chain | 21 – 379 | 359 | Zinc metalloproteinase nas-20 | PRO_0000028924 | |||||||
Regions | |||||||||||
| Domain | 203 – 244 | 42 | EGF-like | ||||||||
Sites | |||||||||||
| Active site | 120 | 1 | By similarity | ||||||||
| Metal binding | 119 | 1 | Zinc; catalytic By similarity | ||||||||
| Metal binding | 123 | 1 | Zinc; catalytic By similarity | ||||||||
| Metal binding | 129 | 1 | Zinc; catalytic By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 67 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 185 | 1 | N-linked (GlcNAc...) Ref.3 | ||||||||
| Glycosylation | 337 | 1 | N-linked (GlcNAc...) Ref.3 | ||||||||
| Glycosylation | 370 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 207 ↔ 218 | By similarity | |||||||||
| Disulfide bond | 209 ↔ 229 | By similarity | |||||||||
| Disulfide bond | 234 ↔ 243 | By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2. |
| [2] | "The astacin protein family in Caenorhabditis elegans." Moehrlen F., Hutter H., Zwilling R. Eur. J. Biochem. 270:4909-4920(2003) [PubMed: 14653817] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 158-308, NOMENCLATURE. Strain: Bristol N2. |
| [3] | "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins." Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T. Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed: 17761667] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185 AND ASN-337, MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| Z74042 Genomic DNA. Translation: CAA98528.2. AJ561210 mRNA. Translation: CAD99212.1. | |
| PIR | T24836. |
| RefSeq | NP_505906.2. |
| UniGene | Cel.34453 |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M12.310. |
Genome annotation databases | |
| Ensembl | T11F9.3. Caenorhabditis elegans. [Contig view] |
| GeneID | 188420. |
| KEGG | cel:T11F9.3. |
| NMPDR | fig|6239.3.peg.19736. |
Organism-specific databases | |
| WormBase | WBGene00003539. nas-20. |
| WormPep | T11F9.3. CE35907. [WorfDB] |
Phylogenomic databases | |
| OMA | Q22396. FEFEYRY. |
Enzyme and pathway databases | |
| BRENDA | 3.4.24.21. 672. |
Gene expression databases | |
| ArrayExpress | Q22396. |
Family and domain databases | |
| InterPro | IPR013032. EGF-like_reg_CS. IPR006025. Pept_M_Zn_BS. IPR006026. Peptidase_M. IPR001506. Peptidase_M12A. IPR017050. Peptidase_M12A_nem. [Graphical view] |
| Pfam | PF01400. Astacin. 1 hit. [Graphical view] |
| PIRSF | PIRSF036365. Astacin_nematoda. 1 hit. |
| PRINTS | PR00480. ASTACIN. |
| SMART | SM00235. ZnMc. 1 hit. [Graphical view] |
| PROSITE | PS00022. EGF_1. 1 hit. PS01186. EGF_2. 1 hit. PS50026. EGF_3. False negative. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 938732. |
Entry information
| Entry name | NAS20_CAEEL | ||||||||
| Accession | Primary (citable) accession number: Q22396 Secondary accession number(s): Q7Z0M9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Caenorhabditis annotation project | ||||||||
Relevant documents
| Caenorhabditis elegans Caenorhabditis elegans: entries, gene names and cross-references to WormPep |
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


