| IED ID | IndEnz0009000013 |
| Enzyme Type ID | chitinase000013 |
| Protein Name |
Chitinase-3-like protein 1 BRP39 protein Breast regression protein 39 Cartilage glycoprotein 39 CGP-39 GP-39 |
| Gene Name | Chi3l1 Brp39 Chil1 |
| 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 | MHTSTEARMGMRAALTGFAVLMLLQSCSAYKLVCYFTSWSQYREGVGSFLPDAIQPFLCTHIIYSFANISSDNMLSTWEWNDESNYDKLNKLKTRNTNLKTLLSVGGWKFGEKRFSEIASNTERRTAFVRSVAPFLRSYGFDGLDLAWLYPRLRDKQYFSTLIKELNAEFTKEVQPGREKLLLSAALSAGKVAIDTGYDIAQIAQHLDFINLMTYDFHGVWRQITGHHSPLFQGQKDTRFDRYSNVNYAVQYMIRLGAQASKLLMGIPTFGKSFTLASSENQLGAPISGEGLPGRFTKEAGTLAYYEICDFLKGAEVHRLSNEKVPFATKGNQWVGYEDKESVKNKVGFLKEKKLAGAMVWALDLDDFQGTCQPKEFFPLTNAIKDALA |
| Enzyme Length | 389 |
| Uniprot Accession Number | Q61362 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 150; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; BINDING 361; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia-induced injury, inflammation and epithelial apoptosis in lung. {ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:19041398, ECO:0000269|PubMed:19414556, ECO:0000269|PubMed:20558631, ECO:0000269|PubMed:21546314, ECO:0000269|PubMed:22817986}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (13); Binding site (2); Chain (1); Disulfide bond (2); Domain (1); Erroneous initiation (4); Glycosylation (1); Helix (18); Mutagenesis (1); Region (4); Sequence conflict (4); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Alternative initiation;Alternative splicing;Antimicrobial;Apoptosis;Cytoplasm;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Inflammatory response;Reference proteome;Secreted;Signal |
| Interact With | O88786; P16110 |
| Induction | INDUCTION: Up-regulated in colon under several inflammatory conditions. Up-regulated upon pulmonary inflammation elicited by sensitization and challenge with the chitin-free aeroallergen ovalbumin or with chitin-containing antigen house dust mite (HDM) extract. Up-regulated in lungs after S.pneumoniae infection. Up-regulated in splenic cells of mammary tumor-bearing animals. Down-regulated by hyperoxia in lung. {ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:19414556, ECO:0000269|PubMed:20558631, ECO:0000269|PubMed:21866546, ECO:0000269|PubMed:22817986}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space. Cytoplasm. Endoplasmic reticulum. Note=Detected in bronchoalveolar lavage (BAL) fluids. Localizes mainly to endoplasmic reticulum when overexpressed in cells, with some protein also detected throughout the cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..29; /evidence=ECO:0000250 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5XEP; |
| Mapped Pubmed ID | 12466851; 12529329; 14681479; 16615898; 17660555; 18490894; 20656949; 21362171; 21408140; 21473774; 21677750; 21949714; 21991364; 23041842; 23291472; 23558346; 23613996; 23620511; 23972995; 24347826; 24659093; 24920662; 25047113; 25294623; 25326751; 25377763; 25511377; 25681350; 25955511; 26079949; 26121745; 26238714; 26393907; 26431492; 26745185; 27198666; 27480124; 28143526; 28303416; 28656528; 28679671; 29344304; 29396296; 29403003; 29427412; 29996695; 30214629; 30402955; 30935969; 31397016; 32127023; 32402213; 32816366; 32962417; 33222690; 33328329; 33461162; 33471078; 33498326; 33533316; 33838225; 34110284; 34720089; 34747367; 35237278; 7768902; 9828134; |
| Motif | |
| Gene Encoded By | |
| Mass | 43,893 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |