P55956 (ASP3_CAEEL) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 84.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Aspartic protease 3 EC=3.4.23.- | ||||
| Gene names |
| ||||
| Organism | Caenorhabditis elegans | ||||
| 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 Reference proteome |
| 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: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aspartic-type endopeptidase activity Inferred 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 – 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
| ||||||||||||||||||
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. Strain: Bristol N2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | FO081559 Genomic DNA. Translation: CCD72415.1. |
| PIR | T33383. |
| RefSeq | NP_509142.1. NM_076741.4. |
| UniGene | Cel.17775. |
3D structure databases | |
| ProteinModelPortal | P55956. |
| SMR | P55956. Positions 18-395. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-26574N. |
| IntAct | P55956. 1 interaction. |
| MINT | MINT-1064632. |
| STRING | P55956. |
Protein family/group databases | |
| MEROPS | A01.A69. |
2D gel databases | |
| Siena-2DPAGE | P55956. |
Proteomic databases | |
| PRIDE | P55956. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | H22K11.1; H22K11.1; H22K11.1. |
| GeneID | 180947. |
| KEGG | cel:H22K11.1. |
| NMPDR | fig|6239.3.peg.23623. |
| UCSC | H22K11.1. c. elegans. |
Organism-specific databases | |
| CTD | 180947. |
| WormBase | H22K11.1; CE19495; WBGene00000216; asp-3. |
Phylogenomic databases | |
| eggNOG | meNOG05119. |
| GeneTree | EMGT00050000005383. |
| HOGENOM | HBG590923. |
| InParanoid | P55956. |
| OMA | FYSVFDH. |
| PhylomeDB | P55956. |
Gene expression databases | |
| ArrayExpress | P55956. |
Family and domain databases | |
| InterPro | IPR001461. Peptidase_A1. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. [Graphical view] |
| Gene3D | G3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits. |
| KO | K01386. |
| PANTHER | PTHR13683. Peptidase_A1. 1 hit. |
| Pfam | PF00026. Asp. 1 hit. [Graphical view] |
| PRINTS | PR00792. PEPSIN. |
| SUPFAM | SSF50630. Pept_Aspartic. 1 hit. |
| PROSITE | PS00141. ASP_PROTEASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| 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 program | Caenorhabditis annotation project | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| Caenorhabditis elegans Caenorhabditis elegans: entries, gene names and cross-references to WormPep |
| SIMILARITY comments Index of protein domains and families |

Clusters with