Search by BoMiProt ID - Bomi121


Primary Information

BoMiProt ID Bomi121
Protein Name Alpha-1-antiproteinase
Organism Bos taurus
Uniprot IdP34955
Milk FractionWhey
Ref Sequence Id NP_776307.1
Amino Acid Lenth 416
Molecular Weight 46104
Fasta Sequence https://www.uniprot.org/uniprot/P34955.fasta
Gene Name SERPINA1
Gene Id 280699
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

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
Bibliography 1. Guha, A., Guha, R., and Gera, S. (2013) Comparison of α1-Antitrypsin, α1-Acid Glycoprotein, Fibrinogen and NOx as Indicator of Subclinical Mastitis in Riverine Buffalo (Bubalus bubalis). Asian-Australasian J. Anim. Sci. 26, 788–794.
2. Huber, R. and Carrell, R. W. (1989) Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins. Biochemistry 28, 8951–8966.
3. Burnouf, T., Constans, J., Clerc, A., Descamps, J., Martinache, L., and Goudemand, M. (1987) Biochemical and Biological Properties of an α 1 -Antitrypsin Concentrate. Vox Sang. 52, 291–297.
4. Ekeowa, U. I., Gooptu, B., Belorgey, D., Hägglöf, P., Karlsson-Li, S., Miranda, E., Pérez, J., MacLeod, I., Kroger, H., Marciniak, S. J., Crowther, D. C., and Lomas, D. A. (2009) α 1 -Antitrypsin deficiency, chronic obstructive pulmonary disease and the serpinopathies. Clin. Sci. 116, 837–850.
5. Gadek, J. E., Fells, G. A., Zimmerman, R. L., Rennard, S. I., and Crystal, R. G. (1981) Antielastases of the human alveolar structures. Implications for the protease-antiprotease theory of emphysema. J. Clin. Invest. 68, 889–898.
6. Petrache, I., Fijalkowska, I., Medler, T. R., Skirball, J., Cruz, P., Zhen, L., Petrache, H. I., Flotte, T. R., and Tuder, R. M. (2006) alpha-1 antitrypsin inhibits caspase-3 activity, preventing lung endothelial cell apoptosis. Am. J. Pathol. 169, 1155–1166.
7. Berman, M. B., Barber, J. C., Talamo, R. C., and Langley, C. E. (1973) Corneal ulceration and the serum antiproteases. I. Alpha 1-antitrypsin. Invest. Ophthalmol. 12, 759–770.
8. Poortmans, J. and Jeanloz, R. W. (1968) Quantitative immunological determination of 12 plasma proteins excreted in human urine collected before and after exercise. J. Clin. Invest. 47, 386–393.
9. American Thoracic Society and European Respiratory Society. (2003) American Thoracic Society/European Respiratory Society Statement. Am. J. Respir. Crit. Care Med. 168, 818–900.
10. Hu, C. and Perlmutter, D. H. (2002) Cell-specific involvement of HNF-1β in α 1 -antitrypsin gene expression in human respiratory epithelial cells. Am. J. Physiol. Cell. Mol. Physiol. 282, L757–L765.
11. Brantly, M., Nukiwa, T., and Crystal, R. G. (1988) Molecular basis of alpha-1-antitrypsin deficiency. Am. J. Med. 84, 13–31.
12. Sifers, R. N. (2010) Intracellular Processing of 1-Antitrypsin. Proc. Am. Thorac. Soc. 7, 376–380.
13. Bergin, D. A., Reeves, E. P., Meleady, P., Henry, M., McElvaney, O. J., Carroll, T. P., Condron, C., Chotirmall, S. H., Clynes, M., O’Neill, S. J., and McElvaney, N. G. (2010) α-1 Antitrypsin regulates human neutrophil chemotaxis induced by soluble immune complexes and IL-8. J. Clin. Invest. 120, 4236–4250.