Search by BoMiProt ID - Bomi190


Primary Information

BoMiProt ID Bomi190
Protein Name CD97 molecule
Organism Bos taurus
Uniprot IDA6QNW8
Milk FractionMFGM, Exosome
Aminoacid Length 734
Molecular Weight 80305
FASTA Sequence Download
Gene Name ADGRE5
Protein Existence Status Unreviewed: Experimental evidence at transcript level

Secondary Information

Protein Function important role in modulating cell migration and invasion; enhance cell adhesion but reduce cell migration and invasion both in vitro and in vivo; activation-associated human leucocyte antigen
Biochemical Properties presence of seven putative transmembrane domains; extended extracellular segment containing several adhesion molecule structure motifs, and has been shown to interact with the human complement regulator, decay-accelerating factor (DAF, CD55); human CD97 has an extended extracellular domain containing multiple epidermal growth factor (EGF)-like repeats, calcium-binding sites and an Arg-Gly-Asp (RGD) motif; CD97 exists on the cell membrane as a processed heterodimer, consisting of an extracellular a-subunit non-covalently linked to a seven-transmembrane b-subunit;
PTMs contains 8 potential N-glycosylation sites.The first 2 sites are located within the first EGF domain, the thirdsite within the second EGF domain. The other 5 sites are locatedwithin the stalk
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Significance of PTMs N-glycosylation of epitopes plays an important role in the recognition of determinants, folding of proteins and establishment of their biologic activity; regulating ligand-receptor interactions
Bibliography 1. Qian, Y. M., Haino, M., Kelly, K., & Song, W. C. (1999). Structural characterization of mouse CD97 and study of its specific interaction with the murine decay-accelerating factor (DAF, CD55). Immunology, 98(2), 303–311. https://doi.org/10.1046/j.1365-2567.1999.00859.
2. Wobus, M., Vogel, B., Schmücking, E., Hamann, J., & Aust, G. (2004). N-glycosylation of CD97 within the EGF domains is crucial for epitope accessibility in normal and malignant cells as well as CD55 ligand binding. International Journal of Cancer, 112(5), 815–822. https://doi.org/10.1002/ijc.20483.
3. Yang, L.-Y., Liu, X.-F., Yang, Y., Yang, L.-L., Liu, K.-W., Tang, Y.-B., … Huang, W. (2017). Biochemical features of the adhesion G protein-coupled receptor CD97 related to its auto-proteolysis and HeLa cell attachment activities. Acta Pharmacologica Sinica, 38(1), 56–68. https://doi.org/10.1038/aps.2016.89.