Search by BoMiProt ID - Bomi1

Primary Information

BoMiProt ID Bomi1
Protein Name Inter-alpha-trypsin inhibitor heavy chain H1
Organism Bos taurus
Uniprot IDF1MMP5
Milk FractionWhey
Ref Sequence ID XP_005222812.1
Aminoacid Length 906
Molecular Weight 101238
FASTA Sequence Download
Gene Name ITIH1
Protein Existence Status Unreviewed: Experimental evidence at protein level

Secondary Information

Presence in other biological fluids/tissue/cells IαI family proteins are mainly secreted by the liver and present in the blood;
Protein Function plasma serine-proteinase inhibitor; ITIH4 is a liver-derived member of the ITI family with diverse functions as an anti-apoptotic and matrix- stabilizing molecule that is important throughout development; ITIH4 is a significant biomarker to assess particulate matter in patients with chronic obstructive pulmonary disease
Biochemical Properties The 3 isoforms are all expressed in the liver and coupled with bikunin before they are released into blood circulation - difference being their selective combination with bikunin; The heavy chain(HC)1–3 prepropeptides (∼900 amino acid residues) comprise a signal peptide, a short propeptide, a mature form of HC, and a C-terminal polypeptide; hyaluronan is the most recognized HC interacting molecule; HCs are observed to be covalently linked to hyaluronan via a transesterification reaction, where they are often referred to as SHAP (serum-derived hyaluronanassociated proteins; The effects of SHAPs on hyaluronan include protection against free radicals, enhancement of macromolecular aggregation, and an increase in the binding avidity to other matrix components;
Significance in milk acute phase protein in cattle- was isolated from heifers with experimentally induced 'summer mastitis'
PTMs Glycosylated: two potential N-glycosylation sites of H1 are effectively fully occupied by complex-type N-glycans- predominantly of biantennary type; H2 heavy chain carries only one complex-type N-glycan attached to Asn64; O-glycan carried by Thr637, two or three additional O-linked carbohydrate chains are present on H2-consist of a type-1 core structure with one or two NeuAc moieties;
Significance of PTMs O glycans influences the metabolism of IaI- preferentially cleaves the H2 heavy chain in its Cterminal part which is enhanced by charge-mediated interactions between the glycosaminoglycan chain of IaI and elastase- mediated byO-glycan chains located in the C-terminal part of H2
Linking IDs
Bibliography 1. Flahaut, C., Capon, C., Balduyck, M., Ricart, G., Sautiere, P., & Mizon, J. (1998). Glycosylation pattern of human inter-alpha-inhibitor heavy chains. The Biochemical Journal, 333 ( Pt 3), 749–756.
2. Soler, L., Dąbrowski, R., García, N., Alava, M. A., Lampreave, F., Piñeiro, M., … Bochniarz, M. (2019). Acute-phase inter-alpha-trypsin inhibitor heavy chain 4 (ITIH4) levels in serum and milk of cows with subclinical mastitis caused by Streptococcus species and coagulase-negative Staphylococcus species. Journal of Dairy Science, 102(1), 539–546.
3. Zhuo, L., Hascall, V. C., & Kimata, K. (2004). Inter-alpha-trypsin inhibitor, a covalent protein-glycosaminoglycan-protein complex. The Journal of Biological Chemistry, 279(37), 38079–38082.
4. Hutadilok, N., Ghosh, P., & Brooks, P. M. (1988). Binding of haptoglobin, inter-alpha-trypsin inhibitor, and alpha 1 proteinase inhibitor to synovial fluid hyaluronate and the influence of these proteins on its degradation by oxygen derived free radicals. Annals of the Rheumatic Diseases, 47(5), 377–385.
5. Zhuo, L., Kanamori, A., Kannagi, R., Itano, N., Wu, J., Hamaguchi, M., … Kimata, K. (2006). SHAP potentiates the CD44-mediated leukocyte adhesion to the hyaluronan substratum. The Journal of Biological Chemistry, 281(29), 20303–20314.
6. Castillo, G. M., & Templeton, D. M. (1993). Subunit structure of bovine ESF (extracellular-matrix stabilizing factor(s)). A chondroitin sulfate proteoglycan with homology to human I alpha i (inter-alpha-trypsin inhibitors). FEBS Letters, 318(3), 292–296.
7. Blom, A. M., Mörgelin, M., Oyen, M., Jarvet, J., & Fries, E. (1999). Structural characterization of inter-alpha-inhibitor. Evidence for an extended shape. The Journal of Biological Chemistry, 274(1), 298–304.
8. Yoneda, M., Suzuki, S., & Kimata, K. (1990). Hyaluronic acid associated with the surfaces of cultured fibroblasts is linked to a serum-derived 85-kDa protein. The Journal of Biological Chemistry, 265(9), 5247–5257. Retrieved from