Difference between revisions of "Part:BBa K3889024"

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RLLSAASNKWPMGGSGVVEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSLAPTCLQKGRGIVL<strong>HELMHVLGFWH</strong> EHTRADRDRYIRVNWNEILPGFEINFIKSRSSNMLTPYDYSSVMHYGRLAFSRRGLPTITPLWAPSVHIGQRWNLSASDITRVLKLYGCS
 
RLLSAASNKWPMGGSGVVEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSLAPTCLQKGRGIVL<strong>HELMHVLGFWH</strong> EHTRADRDRYIRVNWNEILPGFEINFIKSRSSNMLTPYDYSSVMHYGRLAFSRRGLPTITPLWAPSVHIGQRWNLSASDITRVLKLYGCS
  
 +
[[File:T--IISER-Tirupati India--Ovastacin.png]]<br>
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Fig 1. Ovastacin (Active site marked in magenta)
  
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{| class=wikitable
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!C-score
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! Estimated TM-score
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! Estimated RMSD
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|-
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| 1.83
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| 0.97±0.05
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| 1.8±1.5 Å
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|}
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here
 
===Usage and Biology===
 
===Usage and Biology===

Revision as of 21:50, 17 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

T--IISER-Tirupati India--Ovastacin.png
Fig 1. Ovastacin (Active site marked in magenta)

C-score Estimated TM-score Estimated RMSD
1.83 0.97±0.05 1.8±1.5 Å

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal XhoI site found at 210
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 479
  • 1000
    COMPATIBLE 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