Search by BoMiProt ID - Bomi196


Primary Information

BoMiProt ID Bomi196
Protein Name CD151 antigen
Organism Bos taurus
Uniprot IDA7E3T1
Milk FractionExosome
Ref Sequence ID XP_015316836.1
Aminoacid Length 315
Molecular Weight 34494
FASTA Sequence Download
Gene Name CD151
Gene ID 523328
Protein Existence Status Unreviewed: Experimental evidence at transcript level

Secondary Information

Presence in other biological fluids/tissue/cells widely expressed in vascular and haematopoietic cells;
Protein Function function as the organizers of membrane microdomains; associate with other membrane-bound molecules such as cell-adhesion proteins, growth factor receptors, and Ig superfamily members and regulate key cellular processes such as adhesion, migration, and fusion; involved in both physiological and pathological processes related to angiogenesis, vascular injury, thrombosis, and haemostasis; shows stable and stoichiometric association with laminin-binding integrins in a number of cell systems and functions together with the integrins in a variety of cellular processes; important regulator of vasculogenesis and angiogenesis
Biochemical Properties contain four conserved hydrophobic transmembrane domains (TM1-TM4), intracellular N- and C-termini, and small (EC1) and large (EC2) extracellular domains; EC2 domain of most tetraspanins features four–six cysteine residues, and a highly conserved ‘CCG’ motif; transmembrane protein interactions are relatively weak and readily disrupted under the so called ‘high stringency’ detergent conditions used for cell lysate preparation;
PTMs glycosylation sites in EC2 domain
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Bibliography 1. Sincock, P. M., Fitter, S., Parton, R. G., Berndt, M. C., Gamble, J. R., & Ashman, L. K. (1999). PETA-3/CD151, a member of the transmembrane 4 superfamily, is localised to the plasma membrane and endocytic system of endothelial cells, associates with multiple integrins and modulates cell function. Journal of Cell Science, 112 ( Pt 6), 833–844. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/10036233.
2. Yang, J., Liu, Z., Shen, X., Yao, W., Qu, H., Yang, M., … Wang, D. (2005). Expression of CD151 in human atherosclerotic artery and its implication. Journal of Huazhong University of Science and Technology. Medical Sciences = Hua Zhong Ke Ji Da Xue Xue Bao. Yi Xue Ying De Wen Ban = Huazhong Keji Daxue Xuebao. Yixue Yingdewen Ban, 25(6), 629–631. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/16696309.
3. Zijlstra, A., Lewis, J., Degryse, B., Stuhlmann, H., & Quigley, J. P. (2008). The inhibition of tumor cell intravasation and subsequent metastasis via regulation of in vivo tumor cell motility by the tetraspanin CD151. Cancer Cell, 13(3), 221–234. https://doi.org/10.1016/j.ccr.2008.01.031.
4. Yauch, R. L., Kazarov, A. R., Desai, B., Lee, R. T., & Hemler, M. E. (2000). Direct extracellular contact between integrin alpha(3)beta(1) and TM4SF protein CD151. The Journal of Biological Chemistry, 275(13), 9230–9238. https://doi.org/10.1074/jbc.275.13.9230.
5. Sterk, L. M. T., Geuijen, C. A. W., van den Berg, J. G., Claessen, N., Weening, J. J., & Sonnenberg, A. (2002). Association of the tetraspanin CD151 with the laminin-binding integrins alpha3beta1, alpha6beta1, alpha6beta4 and alpha7beta1 in cells in culture and in vivo. Journal of Cell Science, 115(Pt 6), 1161–1173. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/11884516.
6. Berditchevski, F., Gilbert, E., Griffiths, M. R., Fitter, S., Ashman, L., & Jenner, S. J. (2001). Analysis of the CD151-alpha3beta1 integrin and CD151-tetraspanin interactions by mutagenesis. J Biol Chem, 276(44), 41165–41174. https://doi.org/10.1074/jbc.M104041200\rM104041200