Detail Information for IndEnz0002014616
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