Bioinformatics analysis and primary identification of the structure and function of mouse Spata3 protein
Received:April 13, 2022  
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DOI:10. 3969 / j.issn.1005-4847. 2022. 06. 005
KeyWord:Spata3; spermatogenesis; bioinformatics; protein modification site; protein-protein interaction
李美宁 山西医科大学生物化学与分子生物学教研室,出生缺陷与细胞再生山西省重点实验室,太原
马庆 山西医科大学生物化学与分子生物学教研室,出生缺陷与细胞再生山西省重点实验室,太原
弓韬 山西医科大学生物化学与分子生物学教研室,出生缺陷与细胞再生山西省重点实验室,太原
张引红 山西 医科大学实验动物中心,实验动物与人类疾病动物模型山西省重点实验室,太原
闫萍 山西医科大学生物化学与分子生物学教研室,出生缺陷与细胞再生山西省重点实验室,太原
翟翔 山西医科大学生物化学与分子生物学教研室,出生缺陷与细胞再生山西省重点实验室,太原
郭睿 山西医科大学生物化学与分子生物学教研室,出生缺陷与细胞再生山西省重点实验室,太原
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       Objective To analyze the sequence of mouse spermatogenesis associated protein 3 ( Spata3) and explore its structure and function. Methods The NCBI database was used to compare the homology of mouse Spata3. ExPASy ProtParam software was used to analyze its physical and chemical characteristics. SOPMA and GOR4 predicted the spatial conformation. NetPhos3. 1 and the STRING database were used to analyze protein modification sites and protein- protein interactions. Immunohistochemistry and immunofluorescence were used to observe the localization of Spata3 protein. Results Mouse Spata3 had 64% homology with humans in coding sequence. It was a basic unstable hydrophilic protein without a signal peptide. It was a non-transmembrane intracellular protein. It was mainly located in the nucleus and cytoplasm of sperm at all levels of testicular tissue, and its expression in round sperm cells was the highest. Spata3 contained an internal disordered domain, 30 potential phosphorylation sites, and 11 potential O-glycosylation sites, which may interact with proteins such as Spata46 and Spert. Conclusions Spata3 is a conserved protein in spermatogenesis and may regulate spermatogenesis.
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