| IED ID | IndEnz0009000003 |
| Enzyme Type ID | chitinase000003 |
| Protein Name |
Chitinase-like protein 3 EC 3.2.1.52 Beta-N-acetylhexosaminidase Ym1 Chitinase-3-like protein 3 ECF-L Eosinophil chemotactic cytokine Secreted protein Ym1 |
| Gene Name | Chil3 Chi3l3 Ym1 |
| 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 | MAKLILVTGLAILLNVQLGSSYQLMCYYTSWAKDRPIEGSFKPGNIDPCLCTHLIYAFAGMQNNEITYTHEQDLRDYEALNGLKDKNTELKTLLAIGGWKFGPAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGSPPKDKHLFSVLVKEMRKAFEEESVEKDIPRLLLTSTGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDIGKSADLNVDSIISYWKDHGAASEKLIVGFPAYGHTFILSDPSKTGIGAPTISTGPPGKYTDESGLLAYYEVCTFLNEGATEVWDAPQEVPYAYQGNEWVGYDNVRSFKLKAQWLKDNNLGGAVVWPLDMDDFSGSFCHQRHFPLTSTLKGDLNIHSASCKGPY |
| Enzyme Length | 398 |
| Uniprot Accession Number | O35744 |
| Absorption | |
| Active Site | |
| 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=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52; Evidence={ECO:0000269|PubMed:11733538}; |
| DNA Binding | |
| EC Number | 3.2.1.52 |
| Enzyme Function | FUNCTION: Lectin that binds saccharides with a free amino group, such as glucosamine or galactosamine. Binding to oligomeric saccharides is much stronger than binding to mono- or disaccharides. Also binds chitin and heparin. Has weak hexosaminidase activity but no chitinase activity. Has chemotactic activity for T-lymphocytes, bone marrow cells and eosinophils. May play a role in inflammation and allergy. {ECO:0000269|PubMed:10625674, ECO:0000269|PubMed:11297523, ECO:0000269|PubMed:11733538}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-5.0. {ECO:0000269|PubMed:11733538}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (15); Binding site (2); Chain (1); Disulfide bond (3); Domain (1); Helix (18); Region (3); Sequence conflict (4); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Carbohydrate metabolism;Chitin-binding;Cytoplasm;Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Glycosidase;Hydrolase;Inflammatory response;Lectin;Nucleus;Polysaccharide degradation;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Up-regulated in response to IL3 and IL4, during the inflammatory response and upon parasitic infection. {ECO:0000269|PubMed:10625674, ECO:0000269|PubMed:11297523, ECO:0000269|PubMed:12101265, ECO:0000269|PubMed:12215441}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. Rough endoplasmic reticulum lumen. Nucleus envelope. Cytoplasm. Cytoplasmic granule. Note=Predominantly localizes to the lumen of rough endoplasmic reticulum (rER) and nuclear envelope in alveolar macrophages. Localizes to the dilated lumen of rER in immature neutrophils in spleen and in cytoplasmic granules in peritoneal neutrophils. Detected in needle-shaped crystals present in the cytoplasm of bone marrow macrophages. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence="ECO:0000269|PubMed:10625674, ECO:0000269|PubMed:11297523" |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1E9L; 1VF8; |
| Mapped Pubmed ID | 11141507; 12854845; 15514019; 15743827; 16015370; 16174095; 16528013; 16682645; 16966445; 16966459; 16984263; 16996813; 17082650; 17579183; 17901120; 18794523; 19095958; 19380786; 20226534; 21084671; 21677750; 23558346; 23703548; 25082704; 25294623; 25307347; 26079949; 26258883; 27256220; 27318131; 27732846; 28096401; 28228256; 29391024; 30291130; 30500858; 30644388; 32182218; |
| Motif | |
| Gene Encoded By | |
| Mass | 44,458 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=120.8 uM for 4-methylumbelliferone-N-acetylglucosamine (at pH 4-4.5) {ECO:0000269|PubMed:11733538}; Vmax=0.023 umol/min/mg enzyme {ECO:0000269|PubMed:11733538}; Note=4-methylumbelliferone-N-acetylglucosamine (MU-(GlcNAc)1) is a GlcNAc2 analog.; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |