Reviewed,
UniProtKB/Swiss-Prot P55956 (ASP3_CAEEL)
Last modified
November 24, 2009.
Version 68.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Aspartic protease 3 EC=3.4.23.- | ||||
| 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 | 398 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)
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase A1 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Aspartyl protease Hydrolase Protease |
| PTM | Disulfide bond Glycoprotein Zymogen |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cell death Inferred from mutant phenotype. Source: WormBase determination of adult lifespanInferred from mutant phenotype. Source: WormBase proteolysisInferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 17 | 17 | Potential | ||||||||
| Propeptide | 18 – 55 | 38 | Removed in mature form | PRO_0000025937 | |||||||
| Chain | 56 – 398 | 343 | Aspartic protease 3 | PRO_0000025938 | |||||||
Sites | |||||||||||
| Active site | 87 | 1 | By similarity | ||||||||
| Active site | 279 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 321 | 1 | N-linked (GlcNAc...) Ref.3 | ||||||||
| Disulfide bond | 100 ↔ 107 | By similarity | |||||||||
| Disulfide bond | 313 ↔ 351 | By similarity | |||||||||
Sequences
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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] | "Two-dimensional gel electrophoresis of Caenorhabditis elegans homogenates and identification of protein spots by microsequencing." Bini L., Heid H., Liberatori S., Geier G., Pallini V., Zwilling R. Electrophoresis 18:557-562(1997) [PubMed: 9150941] [Abstract] Cited for: PROTEIN SEQUENCE OF 56-65. 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-321, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AF077544 Genomic DNA. Translation: AAK39240.1. | |
| PIR | T33383. |
| RefSeq | NP_509142.1. |
| UniGene | Cel.17775 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:26574N. |
| IntAct | P55956. 3 interactions. |
| STRING | P55956. |
2-D gel databases | |
| Siena-2DPAGE | P55956. |
Genome annotation databases | |
| Ensembl | H22K11.1; H22K11.1; H22K11.1; Caenorhabditis elegans. [Genome view] |
| GeneID | 180947. |
| KEGG | cel:H22K11.1. |
| NMPDR | fig|6239.3.peg.23623. |
| UCSC | H22K11.1. c. elegans. |
Organism-specific databases | |
| CTD | 180947. |
| WormBase | WBGene00000216. asp-3. |
| WormPep | H22K11.1. CE19495. [WorfDB] |
Phylogenomic databases | |
| OMA | FYSVFDH |
Gene expression databases | |
| ArrayExpress | P55956. |
Family and domain databases | |
| InterPro | IPR001461. Peptidase_A1. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. [Graphical view] |
| Gene3D | G3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit. |
| PANTHER | PTHR13683. Peptidase_A1. 1 hit. |
| Pfam | PF00026. Asp. 1 hit. [Graphical view] |
| PRINTS | PR00792. PEPSIN. |
| PROSITE | PS00141. ASP_PROTEASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 911692. |
Entry information
| Entry name | ASP3_CAEEL | ||||||||
| Accession | Primary (citable) accession number: P55956 Secondary accession number(s): Q9TXI5 | ||||||||
| 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 |

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