Difference between revisions of "Part:BBa K3889024"
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− | The SAS1B protein or Ovastacin is a member of the astacin family of metalloproteinases. It is a binding partner in the oolemma of oocytes for the intra-acrosomal sperm protein called SLLP1 (Sperm Lysozyme-Like Protein) [1]. In the reproductive system, SAS1B translation is restricted to the tissues at the ovary and oocytes of the reproductive system. It first appears in ovarian follicles during the transition of primary-secondary follicles in the form of zymogen in humans and is released from cortical granules during the cortical reaction in an activated form after getting cleaved[1]. A part of the C-terminal domain of | + | The SAS1B protein or Ovastacin is a member of the astacin family of metalloproteinases. It is a binding partner in the oolemma of oocytes for the intra-acrosomal sperm protein called SLLP1 (Sperm Lysozyme-Like Protein) [1]. In the reproductive system, SAS1B translation is restricted to the tissues at the ovary and oocytes of the reproductive system. It first appears in ovarian follicles during the transition of primary-secondary follicles in the form of zymogen in humans and is released from cortical granules during the cortical reaction in an activated form after getting cleaved[1]. A part of the C-terminal domain of Ovastacin remains attached to the oolemma, while the N-terminal active Ovastacin domain is secreted [2]. The secreted active protease acts specifically on ZP2 as it is a target for cleavage [3]. |
===Protein Sequence=== | ===Protein Sequence=== |
Revision as of 20:20, 18 October 2021
Human Ovastacin protease
The SAS1B protein or Ovastacin is a member of the astacin family of metalloproteinases. It is a binding partner in the oolemma of oocytes for the intra-acrosomal sperm protein called SLLP1 (Sperm Lysozyme-Like Protein) [1]. In the reproductive system, SAS1B translation is restricted to the tissues at the ovary and oocytes of the reproductive system. It first appears in ovarian follicles during the transition of primary-secondary follicles in the form of zymogen in humans and is released from cortical granules during the cortical reaction in an activated form after getting cleaved[1]. A part of the C-terminal domain of Ovastacin remains attached to the oolemma, while the N-terminal active Ovastacin domain is secreted [2]. The secreted active protease acts specifically on ZP2 as it is a target for cleavage [3].
Protein Sequence
RLLSAASNKWPMGGSGVVEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSLAPTCLQKGRGIVLHELMHVLGFWH EHTRADRDRYIRVNWNEILPGFEINFIKSRSSNMLTPYDYSSVMHYGRLAFSRRGLPTITPLWAPSVHIGQRWNLSASDITRVLKLYGCS
where red denotes the active site [1]
C-score | Estimated TM-score | Estimated RMSD |
---|---|---|
1.83 | 0.97±0.05 | 1.8±1.5 Å |
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal XhoI site found at 210
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 479
- 1000COMPATIBLE WITH RFC[1000]
References
1. Pires, E.S., Hlavin, C., Macnamara, E., Ishola-Gbenla, K., Doerwaldt, C., Chamberlain, C., Klotz, K., Herr, A.K., Khole, A., Chertihin, O., Curnow, E., Feldman, S.H., Mandal, A., Shetty, J., Flickinger, C. and Herr, J.C. (2013), SAS1B protein [ovastacin] shows temporal and spatial restriction to oocytes in several eutherian orders and initiates translation at the primary to secondary follicle transition. Dev. Dyn., 242: 1405-1426. https://doi.org/10.1002/dvdy.24040
2. Körschgen, H., Kuske, M., Karmilin, K., Yiallouros, I., Balbach, M., Floehr, J., Wachten, D., Jahnen-Dechent, W., & Stöcker, W. (2017). Intracellular activation of ovastacin mediates pre-fertilization hardening of the zona pellucida. Molecular human reproduction, 23(9), 607–616. https://doi.org/10.1093/molehr/gax040
3. Anna D. Burkart, Bo Xiong, Boris Baibakov, Maria Jiménez-Movilla, Jurrien Dean; Ovastacin, a cortical granule protease, cleaves ZP2 in the zona pellucida to prevent polyspermy. J Cell Biol 2 April 2012; 197 (1): 37–44. doi: https://doi.org/10.1083/jcb.201112094