P00688 (AMYP_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 122.
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: Pancreatic alpha-amylase Short name=PA EC=3.2.1.1 Alternative name(s): 1,4-alpha-D-glucan glucanohydrolase | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
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 protein level |
General annotation (Comments)
| Catalytic activity | Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. |
| 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 |
| Coding sequence diversity | Polymorphism |
| Domain | Signal |
| Ligand | Calcium Chloride Metal-binding |
| Molecular function | Glycosidase Hydrolase |
| PTM | Disulfide bond Pyrrolidone carboxylic acid |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | carbohydrate catabolic process Inferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | extracellular space Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | alpha-amylase activity Inferred from sequence or structural similarity. Source: UniProtKB calcium ion bindingInferred from sequence or structural similarity. Source: UniProtKB chloride ion bindingInferred from sequence or structural similarity. 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_0000001398 | |||||||
Sites | |||||||||||
| Active site | 209 | 1 | Nucleophile By similarity | ||||||||
| Active site | 245 | 1 | Proton donor 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 | ||||||||
| Site | 312 | 1 | Transition state stabilizer By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 16 | 1 | Pyrrolidone carboxylic acid | ||||||||
| 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 | |||||||||
Natural variations | |||||||||||
| Natural variant | 64 | 1 | V → I in A1, B(C) and AMY-2.2Y. | ||||||||
| Natural variant | 66 | 1 | V → I in AMY-2.2Y. | ||||||||
| Natural variant | 120 | 1 | A → S in A1, B(A) and B(C). | ||||||||
| Natural variant | 161 | 1 | D → S in A1, B(A) and B(C); requires 2 nucleotide substitutions. | ||||||||
| Natural variant | 174 | 1 | L → V in A1 and B(C). | ||||||||
| Natural variant | 175 | 1 | T → S in B(A). | ||||||||
| Natural variant | 254 | 1 | I → V in A1 and B(C). | ||||||||
| Natural variant | 270 – 272 | 3 | YGA → FGV in A1 and B(C). | ||||||||
| Natural variant | 298 | 1 | L → M in A1, B(A) and B(C). | ||||||||
| Natural variant | 322 | 1 | S → A in B(A). | ||||||||
| Natural variant | 419 | 1 | S → A in B1. | ||||||||
| Natural variant | 450 | 1 | A → E in B(C). | ||||||||
Experimental info | |||||||||||
| Sequence conflict | 70 | 1 | S → T in AAA37228. Ref.5 | ||||||||
| Sequence conflict | 85 | 1 | C → S in AAA37228. Ref.5 | ||||||||
| Sequence conflict | 217 | 1 | G → R in CAA24098. Ref.1 | ||||||||
| Sequence conflict | 217 | 1 | G → R in CAA26413. Ref.2 | ||||||||
| Sequence conflict | 217 | 1 | G → R in CAA26414. Ref.2 | ||||||||
| Sequence conflict | 217 | 1 | G → R in CAA26415. Ref.2 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Tissue-specific expression of mouse-alpha-amylase genes: nucleotide sequence of isoenzyme mRNAs from pancreas and salivary gland." Hagenbuechle O., Bovey R., Young R.A. Cell 21:179-187(1980) [PubMed: 6157477] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Multiple non-allelic genes encoding pancreatic alpha-amylase of mouse are expressed in a strain-specific fashion." Tosi M., Bovey R., Astolfi S., Bodary S., Meisler M.H., Wellauer P.K. EMBO J. 3:2809-2816(1984) [PubMed: 6098446] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOZYMES A1; B(A) AND B(C)). Strain: CE/J. |
| [3] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Ovary and Uterus. |
| [4] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas. |
| [5] | "The mouse alpha-amylase multigene family. Sequence organization of members expressed in the pancreas, salivary gland and liver." Schibler U., Pittet A.-C., Young R.A., Hagenbuechle O., Tosi M., Gellman S., Wellauer P.K. J. Mol. Biol. 155:247-266(1982) [PubMed: 6176715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94 AND 267-290. Strain: A/J. |
| [6] | "Members of the Amy-2 alpha-amylase gene family of mouse strain CE/J contain duplicated 5' termini." Bodary S., Grossi G., Hagenbuechle O., Wellauer P.K. J. Mol. Biol. 182:1-10(1985) [PubMed: 2987507] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94. |
| [7] | "Tissue-specific and insulin-dependent expression of a pancreatic amylase gene in transgenic mice." Osborn L., Rosenberg M.P., Keller S.A., Meisler M.H. Mol. Cell. Biol. 7:326-334(1987) [PubMed: 2436036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94 (ISOZYMES AMY-2.1Y AND AMY-2.2Y). |
| [8] | "Evolution of the amylase multigene family. YBR/Ki mice express a pancreatic amylase gene which is silent in other strains." Gumucio D.L., Wiebauer K., Dranginis A., Samuelson L.C., Treisman L.O., Caldwell R.M., Antonucci T.K., Meisler M.H. J. Biol. Chem. 260:13483-13489(1985) [PubMed: 2414282] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 267-289 AND 388-470 (ISOZYMES A1 AND B1). Strain: YRB/KI. |
| [9] | "Characterization of the amino termini of mouse salivary and pancreatic amylases." Karn R.C., Petersen T.E., Hjorth J.P., Nieles J.T., Roepstorff P. FEBS Lett. 126:293-296(1981) [PubMed: 6165618] [Abstract] Cited for: SIGNAL SEQUENCE CLEAVAGE SITE. |
| [10] | "Two distinct pancreatic amylase genes are active in YBR mice." Strahler J.R., Meisler M. Genetics 101:91-102(1982) [PubMed: 6180955] [Abstract] Cited for: PROTEIN SEQUENCE OF 407-458. Strain: YBR. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | V00718 mRNA. Translation: CAA24098.1. X02576 mRNA. Translation: CAA26413.1. X02577 mRNA. Translation: CAA26414.1. X02578 mRNA. Translation: CAA26415.1. AK133526 mRNA. Translation: BAE21706.1. BC094924 mRNA. Translation: AAH94924.1. BC100579 mRNA. Translation: AAI00580.1. J00357 Genomic DNA. Translation: AAA37228.1. J00358 Genomic DNA. Translation: AAA37229.1. J00361 Genomic DNA. Translation: AAA37233.1. X02343 Genomic DNA. Translation: CAA26202.1. M16540 Genomic DNA. Translation: AAA37223.1. M15965 Genomic DNA. Translation: AAA37226.1. M11895 mRNA. Translation: AAA37224.1. M11896 mRNA. Translation: AAA37227.1. M11891 Genomic DNA. Translation: AAA37222.1. |
| IPI | IPI00133544. |
| PIR | ALMSP1. A90995. ALMSP. B90798. ALMSPC. B90995. ALMSPA. C90995. I49493. I49494. |
| RefSeq | NP_001036176.1. NM_001042711.2. NP_001153622.1. NM_001160150.1. NP_001153623.1. NM_001160151.1. NP_001153624.1. NM_001160152.1. |
| UniGene | Mm.275426. Mm.443376. Mm.482445. Mm.482540. |
3D structure databases | |
| ProteinModelPortal | P00688. |
| SMR | P00688. Positions 16-508. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P00688. |
Protein family/group databases | |
| CAZy | GH13. Glycoside Hydrolase Family 13. |
PTM databases | |
| PhosphoSite | P00688. |
2D gel databases | |
| SWISS-2DPAGE | P00688. |
Proteomic databases | |
| PRIDE | P00688. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000098667; ENSMUSP00000096264; ENSMUSG00000079850. ENSMUST00000098670; ENSMUSP00000096267; ENSMUSG00000074266. ENSMUST00000098671; ENSMUSP00000096268; ENSMUSG00000074267. ENSMUST00000098673; ENSMUSP00000096270; ENSMUSG00000074268. ENSMUST00000170843; ENSMUSP00000128641; ENSMUSG00000079850. |
| GeneID | 100043684. 100043686. 100043688. 109959. |
| KEGG | mmu:100043684. mmu:100043686. mmu:100043688. mmu:109959. |
Organism-specific databases | |
| CTD | 100043684. 100043686. 100043688. 109959. |
| MGI | MGI:88020. Amy2. |
Phylogenomic databases | |
| eggNOG | roNOG12919. |
| HOGENOM | HBG404170. |
| HOVERGEN | HBG000061. |
| InParanoid | P00688. |
| OrthoDB | EOG4RV2R1. |
Gene expression databases | |
| Genevestigator | P00688. |
| GermOnline | ENSMUSG00000074265. Mus musculus. ENSMUSG00000074266. Mus musculus. ENSMUSG00000074267. Mus musculus. ENSMUSG00000074268. Mus musculus. |
Family and domain databases | |
| InterPro | IPR006048. A-amylase_b_C. IPR015902. Alpha_amylase. IPR006046. Glyco_hydro_13. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat_dom. IPR006589. Glyco_hydro_13_sub_cat_dom. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| Gene3D | G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. |
| KO | K01176. |
| PANTHER | PTHR10357. Alpha_amylase. 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] |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| ProtoNet | Search... |
Other | |
| NextBio | 279405. |
| SOURCE | Search... |
Entry information
| Entry name | AMYP_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P00688 Secondary accession number(s): Q4VBW6 Q64301 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with