Reviewed,
UniProtKB/Swiss-Prot P00773 (ELA1_RAT)
Last modified
June 16, 2009.
Version 81.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Elastase-1 EC=3.4.21.36 | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 266 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 | Acts upon elastin. |
| Catalytic activity | Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa. |
| Cofactor | Binds 1 calcium ion per subunit By similarity. |
| Subcellular location | |
| Tissue specificity | Pancreas. |
| Sequence similarities | Belongs to the peptidase S1 family. Elastase subfamily. Contains 1 peptidase S1 domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | Calcium Metal-binding |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Disulfide bond Zymogen |
| Technical term | Direct protein sequencing |
| 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 | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 16 | 16 | Ref.3 | ||||||||
| Propeptide | 17 – 26 | 10 | Activation peptide | PRO_0000027683 | |||||||
| Chain | 27 – 266 | 240 | Elastase-1 | PRO_0000027684 | |||||||
Regions | |||||||||||
| Domain | 27 – 264 | 238 | Peptidase S1 | ||||||||
Sites | |||||||||||
| Active site | 71 | 1 | Charge relay system By similarity | ||||||||
| Active site | 119 | 1 | Charge relay system By similarity | ||||||||
| Active site | 214 | 1 | Charge relay system By similarity | ||||||||
| Metal binding | 85 | 1 | Calcium By similarity | ||||||||
| Metal binding | 90 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 95 | 1 | Calcium By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 56 ↔ 72 | By similarity | |||||||||
| Disulfide bond | 153 ↔ 220 | By similarity | |||||||||
| Disulfide bond | 184 ↔ 200 | By similarity | |||||||||
| Disulfide bond | 210 ↔ 240 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 104 | 1 | M → V in AAA98811. Ref.2 | ||||||||
| Sequence conflict | 108 | 1 | T → N in AAA98811. Ref.2 | ||||||||
| Sequence conflict | 244 | 1 | K → R in AAA98811. Ref.2 | ||||||||
| Sequence conflict | 266 | 1 | T → N in AAA98811. Ref.2 | ||||||||
Sequences
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References
| [1] | "Primary structure of two distinct rat pancreatic preproelastases determined by sequence analysis of the complete cloned messenger ribonucleic acid sequences." MacDonald R.J., Swift G.H., Quinto C., Swain W., Pictet R.L., Nikovits W., Rutter W.J. Biochemistry 21:1453-1463(1982) [PubMed: 6918221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Structure of the two related elastase genes expressed in the rat pancreas." Swift G.H., Craik C.S., Stary S.J., Quinto C., Lahaie R.G., Rutter W.J., MacDonald R.J. J. Biol. Chem. 259:14271-14278(1984) [PubMed: 6094548] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Isolation and characterization of rat pancreatic elastase." Largman C. Biochemistry 22:3763-3770(1983) [PubMed: 6555050] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-45. Tissue: Pancreas. |
Cross-references
Sequence databases | |
|---|---|
| V01234 mRNA. Translation: CAA24544.1. L00117 L00116 Genomic DNA. Translation: AAA98811.1. | |
| IPI | IPI00327729. |
| PIR | ELRT1. A00960. |
| UniGene | Rn.6044 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1QNJ based on UniProtKB P00772. |
| SMR | P00773. Positions 27-264. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S01.153. |
Genome annotation databases | |
| Ensembl | ENSRNOG00000004725. Rattus norvegicus. [Contig view] |
Organism-specific databases | |
| RGD | 2547. Ela1. |
Phylogenomic databases | |
| HOVERGEN | P00773. |
Enzyme and pathway databases | |
| BRENDA | 3.4.21.36. 248. |
Gene expression databases | |
| ArrayExpress | P00773. |
| GermOnline | ENSRNOG00000004725. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view] |
| Pfam | PF00089. Trypsin. 1 hit. [Graphical view] |
| PRINTS | PR00722. CHYMOTRYPSIN. |
| SMART | SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| PROSITE | PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ELA1_RAT | ||||||||
| Accession | Primary (citable) accession number: P00773 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


