IED ID | IndEnz0009000008 |
Enzyme Type ID | chitinase000008 |
Protein Name |
Acidic mammalian chitinase AMCase EC 3.2.1.14 YNL |
Gene Name | Chia Chia1 |
Organism | Mus musculus (Mouse) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
Enzyme Sequence | MAKLLLVTGLALLLNAQLGSAYNLICYFTNWAQYRPGLGSFKPDDINPCLCTHLIYAFAGMQNNEITTIEWNDVTLYKAFNDLKNRNSKLKTLLAIGGWNFGTAPFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWEYPGSRGSPPQDKHLFTVLVKEMREAFEQEAIESNRPRLMVTAAVAGGISNIQAGYEIPELSKYLDFIHVMTYDLHGSWEGYTGENSPLYKYPTETGSNAYLNVDYVMNYWKNNGAPAEKLIVGFPEYGHTFILRNPSDNGIGAPTSGDGPAGPYTRQAGFWAYYEICTFLRSGATEVWDASQEVPYAYKANEWLGYDNIKSFSVKAQWLKQNNFGGAMIWAIDLDDFTGSFCDQGKFPLTSTLNKALGISTEGCTAPDVPSEPVTTPPGSGSGGGSSGGSSGGSGFCADKADGLYPVADDRNAFWQCINGITYQQHCQAGLVFDTSCNCCNWP |
Enzyme Length | 473 |
Uniprot Accession Number | Q91XA9 |
Absorption | |
Active Site | ACT_SITE 140; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258 |
Activity Regulation | |
Binding Site | BINDING 141; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; BINDING 360; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000269|PubMed:18294964}; |
DNA Binding | |
EC Number | 3.2.1.14 |
Enzyme Function | FUNCTION: Degrades chitin and chitotriose. May participate in the defense against nematodes, fungi and other pathogens. Plays a role in T-helper cell type 2 (Th2) immune response. Contributes to the response to IL-13 and inflammation in response to IL-13. Stimulates chemokine production by pulmonary epithelial cells. Protects lung epithelial cells against apoptosis and promotes phosphorylation of AKT1. Its function in the inflammatory response and in protecting cells against apoptosis is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding. Presence in saliva and gastric juice suggests a function as a digestive enzyme. {ECO:0000269|PubMed:11085997, ECO:0000269|PubMed:12133911, ECO:0000269|PubMed:15192232, ECO:0000269|PubMed:19076793}. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is below 2.5. {ECO:0000269|PubMed:18294964}; |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Binding site (2); Chain (1); Compositional bias (1); Disulfide bond (4); Domain (2); Erroneous initiation (1); Mutagenesis (1); Region (4); Sequence conflict (2); Signal peptide (1) |
Keywords | Apoptosis;Carbohydrate metabolism;Chitin degradation;Chitin-binding;Cytoplasm;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Immunity;Inflammatory response;Polysaccharide degradation;Reference proteome;Secreted;Signal |
Interact With | |
Induction | INDUCTION: Up-regulated upon pulmonary inflammation elicited by sensitization and aerosol challenge with the aeroallergen ovalbumin. Up-regulated during T-helper cell type 2 (Th2) inflammation. Induction is mediated by IL-13. {ECO:0000269|PubMed:15192232}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasmic granule. Note=Detected in secretory granules of parotid acinar cells and gastric chief cells and secreted from them into saliva and gastric juice, respectively. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000269|PubMed:11085997 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 11217851; 12466851; 14681479; 21677750; 21836154; 22001906; 23558346; 24244337; 25764512; 27043413; 28431248; 28833103; 30903663; |
Motif | |
Gene Encoded By | |
Mass | 52,003 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |