Reviewed,
UniProtKB/Swiss-Prot P00689 (AMYP_RAT)
Last modified
October 13, 2009.
Version 93.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Pancreatic alpha-amylase Short name=PA EC=3.2.1.1 Alternative name(s): 1,4-alpha-D-glucan glucanohydrolase | ||
| 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 | 508 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Catalytic activity | Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides. |
| Cofactor | Binds 1 calcium ion per subunit By similarity. Binds 1 chloride ion per subunit By similarity. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the glycosyl hydrolase 13 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism |
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | Calcium Chloride Metal-binding |
| Molecular function | Glycosidase Hydrolase |
| PTM | Disulfide bond Pyrrolidone carboxylic acid |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | alpha-amylase activity Inferred from electronic annotation. Source: EC calcium ion bindingInferred from electronic annotation. Source: UniProtKB-KW chloride ion bindingInferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 15 | 15 | |||||||||
| Chain | 16 – 508 | 493 | Pancreatic alpha-amylase | PRO_0000001400 | |||||||
Sites | |||||||||||
| Active site | 209 | 1 | Nucleophile By similarity | ||||||||
| Active site | 245 | 1 | Proton donor By similarity | ||||||||
| Active site | 312 | 1 | By similarity | ||||||||
| Metal binding | 115 | 1 | Calcium By similarity | ||||||||
| Metal binding | 170 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 179 | 1 | Calcium By similarity | ||||||||
| Metal binding | 213 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Binding site | 207 | 1 | Chloride By similarity | ||||||||
| Binding site | 310 | 1 | Chloride By similarity | ||||||||
| Binding site | 349 | 1 | Chloride By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 16 | 1 | Pyrrolidone carboxylic acid By similarity | ||||||||
| Disulfide bond | 43 ↔ 101 | By similarity | |||||||||
| Disulfide bond | 85 ↔ 130 | By similarity | |||||||||
| Disulfide bond | 156 ↔ 172 | By similarity | |||||||||
| Disulfide bond | 390 ↔ 396 | By similarity | |||||||||
| Disulfide bond | 462 ↔ 474 | By similarity | |||||||||
Sequences
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References
| [1] | MacDonald R. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Structure of a family of rat amylase genes." McDonald R.J., Crerar M.M., Swain W.F., Pictet R.L., Thomas G., Rutter W.J. Nature 287:117-122(1980) [PubMed: 6159531] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-508. |
| [3] | "Pancreas-specific genes: structure and expression." McDonald R.J., Crerar M.M., Swain W.F., Pictet R.L., Rutter W.J. Cancer 47:1497-1504(1981) [PubMed: 6168351] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-508. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| J00703 mRNA. Translation: AAA40725.2. | |
| IPI | IPI00211904. |
| PIR | ALRTP. A00840. |
| RefSeq | NP_113690.1. |
| UniGene | Rn.67070 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1KXQ based on UniProtKB P00690. |
| SMR | P00689. Positions 16-508. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P00689. |
Protein family/group databases | |
| CAZy | GH13. Glycoside Hydrolase Family 13. |
Proteomic databases | |
| PRIDE | P00689. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000022268; ENSRNOP00000022268; ENSRNOG00000030590; Rattus norvegicus. [Genome view] |
| GeneID | 497039. |
| KEGG | rno:497039. |
Organism-specific databases | |
| CTD | 497039. |
| RGD | 1593187. Amy2. |
Phylogenomic databases | |
| HOVERGEN | P00689. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.1. 248. |
Gene expression databases | |
| Genevestigator | P00689. |
| GermOnline | ENSRNOG00000030590. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR006048. A-amylase_b_C. IPR006046. Glyco_hydro_13. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat. IPR006589. Glyco_hydro_13_sub_cat. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view] |
| Gene3D | G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. |
| Pfam | PF00128. Alpha-amylase. 1 hit. PF02806. Alpha-amylase_C. 1 hit. [Graphical view] |
| PRINTS | PR00110. ALPHAAMYLASE. |
| SMART | SM00642. Aamy. 1 hit. SM00632. Aamy_C. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 697675. |
Entry information
| Entry name | AMYP_RAT | ||||||||
| Accession | Primary (citable) accession number: P00689 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


