| IED ID | IndEnz0002016195 |
| Enzyme Type ID | protease016195 |
| Protein Name |
Inter-alpha-trypsin inhibitor ITI EI-14 HI-14 Inhibitory fragment of ITI Fragment |
| Gene Name | |
| Organism | Equus caballus (Horse) |
| 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 Laurasiatheria Perissodactyla (odd-toed ungulates) Equidae (horses) Equus Equus Equus caballus (Horse) |
| Enzyme Sequence | SKKEDSCQLDHAQGPCLGMISRYFYNGTSMACETFQYGGCLGNGNNFASQKECLQTCRTVAACNLPIVQGPCRAFIRLWAFDAAQGKCVLFTYGGCRGNGNKFYSQKECKEYCGIPGDGDEELLR |
| Enzyme Length | 125 |
| Uniprot Accession Number | P04365 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: This inhibitory fragment, released from native ITI after limited proteolysis with trypsin, contains two homologous domains. Whereas the second domain is a strong inhibitor of trypsin, the first domain interacts weakly with PMN-granulocytic elastase and not at all with pancreatic elastase. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (6); Domain (2); Glycosylation (1); Non-terminal residue (2); Sequence conflict (1); Site (2) |
| Keywords | Direct protein sequencing;Disulfide bond;Glycoprotein;Protease inhibitor;Reference proteome;Repeat;Secreted;Serine protease inhibitor |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 13,726 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |