IED ID | IndEnz0009000016 |
Enzyme Type ID | chitinase000016 |
Protein Name |
Chitotriosidase-1 EC 3.2.1.14 Chitinase-1 |
Gene Name | CHIT1 |
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 | MVRSVAWAGFMVLLMIPWGSAAKLVCYFTNWAQYRQGEARFLPKDLDPSLCTHLIYAFAGMTNHQLSTTEWNDETLYQEFNGLKKMNPKLKTLLAIGGWNFGTQKFTDMVATANNRQTFVNSAIRFLRKYSFDGLDLDWEYPGSQGSPAVDKERFTTLVQDLANAFQQEAQTSGKERLLLSAAVPAGQTYVDAGYEVDKIAQNLDFVNLMAYDFHGSWEKVTGHNSPLYKRQEESGAAASLNVDAAVQQWLQKGTPASKLILGMPTYGRSFTLASSSDTRVGAPATGSGTPGPFTKEGGMLAYYEVCSWKGATKQRIQDQKVPYIFRDNQWVGFDDVESFKTKVSYLKQKGLGGAMVWALDLDDFAGFSCNQGRYPLIQTLRQELSLPYLPSGTPELEVPKPGQPSEPEHGPSPGQDTFCQGKADGLYPNPRERSSFYSCAAGRLFQQSCPTGLVFSNSCKCCTWN |
Enzyme Length | 466 |
Uniprot Accession Number | Q13231 |
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 358; /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:15664516, ECO:0000269|PubMed:19725875, ECO:0000269|PubMed:7836450}; |
DNA Binding | |
EC Number | 3.2.1.14 |
Enzyme Function | FUNCTION: Degrades chitin, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens. Isoform 3 has no enzymatic activity. {ECO:0000269|PubMed:7592832, ECO:0000269|PubMed:7836450}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Alternative sequence (4); Beta strand (22); Binding site (2); Chain (1); Disulfide bond (3); Domain (2); Erroneous initiation (1); Glycosylation (1); Helix (16); Natural variant (5); Region (4); Signal peptide (1); Turn (6) |
Keywords | 3D-structure;Alternative splicing;Carbohydrate metabolism;Chitin degradation;Chitin-binding;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Lysosome;Polysaccharide degradation;Reference proteome;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. Lysosome. Note=A small proportion is lysosomal. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000269|PubMed:7836450 |
Structure 3D | X-ray crystallography (22); NMR spectroscopy (1) |
Cross Reference PDB | 1GUV; 1HKI; 1HKJ; 1HKK; 1HKM; 1LG1; 1LG2; 1LQ0; 1WAW; 1WB0; 4WJX; 4WK9; 4WKA; 4WKF; 4WKH; 5HBF; 5NR8; 5NRA; 5NRF; 6JJR; 6JK6; 6SO0; 6ZE8; |
Mapped Pubmed ID | 16107886; 16110781; 19881466; 23650620; 26143917; 27111557; 29283260; 31891077; 31928006; 33078933; |
Motif | |
Gene Encoded By | |
Mass | 51,681 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |