|Ref Sequence Id||NP_776307.1|
|Amino Acid Lenth||416|
|Protein Existence Status||Reviewed: Experimental evidence at protein level|
|Presence in other biological fluids/tissue/cells||saliva, tears, breast milk, urine, semen, bronchoalveolar lavage fluid|
|Protein Function||serine protease inhibitor; major anti-elastase of the lower respiratory tract; modulate both infl ammation and apoptosis;|
|Biochemical Properties||believed to function as ideal substrates with association rates of the order of 104 M_1 s_l or more and negligible dissociation rates; the sequence at the reactive center helps define specificity by providing a putative cleavage site for the target proteinase; crystallizes in three different crystal forms which have been analyzed and found to be based on very similar molecular structures; Disulfide bonds absent in arantitrypsin but present in family members provide direct evidence for structural similarity, but very few of them have been chemically defined;|
|Significance in milk||Acute phase proteins; elevated levels in milk during subclinical mastitis due to bacterial inection|
|PTMs||glycosylation at three distinct asparagine residues; These asparagine-linked side chains are composed of N-acetylglucosamine, mannose, galactose, and sialic acid arranged as a core with two to three branching “antennae”|
|Significance of PTMs||help maintain solubility and allow attachment of protein-processing enzymes; contribute to the antiinflammatory capacity of the protein through negative regulation of IL-8-induced neutrophil chemotaxis|
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