IED ID | IndEnz0002014616 |
Enzyme Type ID | protease014616 |
Protein Name |
Salivary cystatin-L Sialostatin-L SialoL |
Gene Name | |
Organism | Ixodes scapularis (Black-legged tick) (Deer tick) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Chelicerata Arachnida Acari Parasitiformes Ixodida (ticks) Ixodoidea Ixodidae (hardbacked ticks) Ixodinae Ixodes Ixodes scapularis (Black-legged tick) (Deer tick) |
Enzyme Sequence | MTSTFALVLLLGGMAVCVATGVFGGYSERANHQANPEFLNLAHYATSTWSAQQPGKTHFDTVAEVVKVETQVVAGTNYRLTLKVAESTCELTSTYNKDTCLPKADAAHRTCTTVVFENLQGDKSVSPFECEAA |
Enzyme Length | 133 |
Uniprot Accession Number | Q8MVB6 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Inhibitor of cysteine proteinases. Inhibits host immune responses via its inhibition of host cathepsins (PubMed:19494265). Contributes to the suppression of the host's immune response to tick salivary proteins and is important for successful feeding on hosts (PubMed:17698852). Inhibits differentiation of host dendritic cells (PubMed:19494265, PubMed:25975355). Inhibits proliferation of host T-cells in response to antigen stimulus (PubMed:19494265). Down-regulates TLR2-mediated host responses to infection by B.burgdorferi and the production of the chemokine CCL3 by host dendritic cells (PubMed:25975355). Down-regulates host responses to infection by B.burgdorferi and the production of IFNB1 by host dendritic cells (PubMed:25975355). Down-regulates IL1B production by host mast cells, and this then leads to impaired activation of IL1R1, resulting in decreased IL9 production (PubMed:26078269). Inhibits host inflammatory reactions and recruitment of host neutrophils (PubMed:16772304). Inhibits papain and cathepsin-L (CTSL) (in vitro) (PubMed:16772304, PubMed:17698852, PubMed:20545851). Inhibits cathepsin-S (CTSS) (in vitro) (PubMed:17698852, PubMed:20545851). Inhibits CTSV and CTSC, but to a lesser degree (in vitro) (PubMed:16772304, PubMed:17698852). {ECO:0000269|PubMed:16772304, ECO:0000269|PubMed:17698852, ECO:0000269|PubMed:19494265, ECO:0000269|PubMed:20545851, ECO:0000269|PubMed:25975355, ECO:0000269|PubMed:26078269}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Beta strand (3); Chain (1); Disulfide bond (2); Domain (1); Helix (1); Signal peptide (1); Site (1); Turn (1) |
Keywords | 3D-structure;Disulfide bond;Protease inhibitor;Reference proteome;Secreted;Signal;Thiol protease inhibitor |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16772304}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 4ZM8; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 14,282 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |