Protein Family Models

Date:

2024-08-14

This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with Pfam:PF07715 and Pfam:PF00593. [1]. 10986238. Characterization of four outer membrane proteins involved in binding starch to the cell surface of Bacteroides thetaiotaomicron. Shipman JA, Berleman JE, Salyers AA;. J Bacteriol. 2000;182:5365-5372. [2]. 11717282. Biochemical analysis of interactions between outer membrane proteins that contribute to starch utilization by Bacteroides thetaiotaomicron. Cho KH, Salyers AA;. J Bacteriol 2001;183:7224-7230. (from Pfam)

Date:

2024-10-16

This domain, found in various hypothetical prokaryotic proteins, has no known function. (from Pfam)

Date:

2024-08-14

Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilisation and tumour metastasis as well as in plasma protease inhibition [1]. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (Pfam:PF00092) in ITI heavy chains (ITIHs) and their precursors. [1]. 14744536. ITIH5, a novel member of the inter-alpha-trypsin inhibitor heavy chain family is downregulated in breast cancer. Himmelfarb M, Klopocki E, Grube S, Staub E, Klaman I, Hinzmann B, Kristiansen G, Rosenthal A, Durst M, Dahl E;. Cancer Lett 2004;204:69-77. [2]. 10830112. VIT-1: the second member of a new branch of the von Willebrand factor A domain superfamily. Mayne R, Ren ZX, Liu J, Cook T, Carson M, Narayana S;. Biochem Soc Trans. 1999;27:832-835. (from Pfam)

Date:

2024-10-16