IED ID |
IndEnz0002010178 |
Enzyme Type ID |
protease010178 |
Protein Name |
Serine protease inhibitor Cvsi-1
|
Gene Name |
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Organism |
Crassostrea virginica (Eastern oyster) |
Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Metazoa
Eumetazoa
Bilateria
Protostomia
Spiralia
Lophotrochozoa
Mollusca
Bivalvia
Autobranchia
Pteriomorphia
Ostreida
Ostreoidea
Ostreidae (oysters)
Crassostrea
Crassostrea virginica (Eastern oyster)
|
Enzyme Sequence |
MDVVRTLILCVCLFGLTFAVPCIDGVCTSNELQCASGYVKGCHAGLCTCEHATTQSCTVVNNCLHLGTCSLHGRDGFWHCVDSVCKCFFF |
Enzyme Length |
90 |
Uniprot Accession Number |
Q30HU9 |
Absorption |
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Active Site |
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Activity Regulation |
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Binding Site |
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Calcium Binding |
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catalytic Activity |
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DNA Binding |
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EC Number |
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Enzyme Function |
FUNCTION: Slow-binding inhibitor of serine proteases. The inhibitor rapidly binds to the protease forming a weak enzyme-inhibitor complex, and this is followed by a slow isomerization forming a tight-binding enzyme-inhibitor complex. Active against subtilisin A, perkinsin and trypsin with dissociation constants of 0.29 nM, 13.7 nM and 17.7 nM respectively. Not active against thermolysin, papain or pepsin. Has antiparasitic activity against the protozoan P.marinus. {ECO:0000269|PubMed:16872855, ECO:0000269|PubMed:19720077}. |
Temperature Dependency |
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PH Dependency |
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Pathway |
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nucleotide Binding |
|
Features |
Chain (1); Signal peptide (1) |
Keywords |
Antimicrobial;Direct protein sequencing;Disulfide bond;Protease inhibitor;Secreted;Serine protease inhibitor;Signal |
Interact With |
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Induction |
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Subcellular Location |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16872855}. |
Modified Residue |
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Post Translational Modification |
PTM: Contains 6 disulfide bonds. {ECO:0000305}. |
Signal Peptide |
SIGNAL 1..19; /evidence=ECO:0000269|PubMed:16872855 |
Structure 3D |
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Cross Reference PDB |
- |
Mapped Pubmed ID |
- |
Motif |
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Gene Encoded By |
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Mass |
9,715 |
Kinetics |
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Metal Binding |
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Rhea ID |
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Cross Reference Brenda |
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