P00773 (CELA1_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 108.
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: Chymotrypsin-like elastase family member 1 EC=3.4.21.36 Alternative name(s): Elastase-1 | ||||
| Gene names |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||||
| 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
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 | Chymotrypsin-like elastase family member 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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Isolation and characterization of rat pancreatic elastase." Largman C. Biochemistry 22:3763-3770(1983) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-45. Tissue: Pancreas. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | V01234 mRNA. Translation: CAA24544.1. L00117 L00116 Genomic DNA. Translation: AAA98811.1. |
| IPI | IPI00327729. |
| PIR | ELRT1. A00960. |
| RefSeq | NP_036684.1. NM_012552.3. |
| UniGene | Rn.6044. |
3D structure databases | |
| ProteinModelPortal | P00773. |
| SMR | P00773. Positions 27-264. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10116.ENSRNOP00000006351. |
Protein family/group databases | |
| MEROPS | S01.153. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOT00000006351; ENSRNOP00000006351; ENSRNOG00000004725. |
| GeneID | 24331. |
| KEGG | rno:24331. |
| UCSC | RGD:2547. rat. |
Organism-specific databases | |
| CTD | 1990. |
| RGD | 2547. Cela1. |
Phylogenomic databases | |
| eggNOG | COG5640. |
| GeneTree | ENSGT00640000091262. |
| HOGENOM | HOG000251820. |
| InParanoid | P00773. |
| KO | K01326. |
| OrthoDB | EOG4V171P. |
Gene expression databases | |
| Genevestigator | P00773. |
| GermOnline | ENSRNOG00000004725. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR001254. Peptidase_S1. IPR018114. Peptidase_S1_AS. IPR001314. Peptidase_S1A. IPR009003. Trypsin-like_Pept_dom. [Graphical view] |
| Pfam | PF00089. Trypsin. 1 hit. [Graphical view] |
| PRINTS | PR00722. CHYMOTRYPSIN. |
| SMART | SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| SUPFAM | SSF50494. Pept_Ser_Cys. 1 hit. |
| PROSITE | PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 603007. |
Entry information
| Entry name | CELA1_RAT | ||||||||
| Accession | Primary (citable) accession number: P00773 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
