Detail Information for IndEnz0009000007
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;