IED ID | IndEnz0009000007 |
Enzyme Type ID | chitinase000007 |
Protein Name |
Acidic mammalian chitinase AMCase EC 3.2.1.14 Lung-specific protein TSA1902 |
Gene Name | CHIA |
Organism | Homo sapiens (Human) |
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
Enzyme Sequence | MTKLILLTGLVLILNLQLGSAYQLTCYFTNWAQYRPGLGRFMPDNIDPCLCTHLIYAFAGRQNNEITTIEWNDVTLYQAFNGLKNKNSQLKTLLAIGGWNFGTAPFTAMVSTPENRQTFITSVIKFLRQYEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQEAKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAPSGSGNGSGSSSSGGSSGGSGFCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA |
Enzyme Length | 476 |
Uniprot Accession Number | Q9BZP6 |
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:18824549, ECO:0000269|PubMed:19241384, ECO:0000269|PubMed:19435888}; |
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. {ECO:0000269|PubMed:11085997, ECO:0000269|PubMed:18824549, ECO:0000269|PubMed:19342690, ECO:0000269|PubMed:19435888}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Alternative sequence (2); Beta strand (15); Binding site (2); Chain (1); Disulfide bond (3); Domain (2); Helix (20); Mutagenesis (1); Natural variant (10); Region (3); Sequence conflict (1); Signal peptide (1); Turn (4) |
Keywords | 3D-structure;Alternative splicing;Apoptosis;Carbohydrate metabolism;Chitin degradation;Chitin-binding;Cytoplasm;Disulfide bond;Glycosidase;Hydrolase;Immunity;Inflammatory response;Polysaccharide degradation;Reference proteome;Secreted;Signal |
Interact With | Q5RI15; P00533; Q8NC74; Q92609 |
Induction | INDUCTION: Up-regulated in lung epithelial cells from asthma patients. {ECO:0000269|PubMed:15192232}. |
Subcellular Location | SUBCELLULAR LOCATION: [Isoform 1]: Secreted. Note=Secretion depends on EGFR activity.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000250 |
Structure 3D | X-ray crystallography (8) |
Cross Reference PDB | 2YBT; 2YBU; 3FXY; 3FY1; 3RM4; 3RM8; 3RM9; 3RME; |
Mapped Pubmed ID | 16584180; 17703412; 18602573; 19085022; 19242357; 19247692; 19258923; 19379605; 19644363; 20226308; 20422678; 20444155; 20503287; 20538957; 20666458; 20800603; 21159721; 21303604; 21511453; 21609838; 21711963; 22200767; 24119614; 24903994; 27702777; 27977724; 29233108; 30117166; |
Motif | |
Gene Encoded By | |
Mass | 52,271 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.2.1.14; |