编码人补体成分C1r前体的全长cDNA的克隆与测序
Cloning and sequencing of full-length cDNA encoding the precursor of human complement component C1r.
作者信息
Journet A, Tosi M
出版信息
Biochem J. 1986 Dec 15;240(3):783-7. doi: 10.1042/bj2400783.
Abstract
The sequencing of human liver cDNA clones encoding the entire C1r precursor protein has confirmed the previously determined peptide sequence and has shown that there is a leader peptide which is 17 amino acids long. A residue tentatively identified as beta-hydroxyaspartic acid [Arlaud, Willis & Gagnon (1986) Biochem. J., in the press] located in the C1r A-chain, within an epidermal-growth-factor consensus sequence, was found to be encoded as asparagine. Two sequence elements, tandemly located in the A-chain, are related to a sequence widespread among proteins which interact with C3b or C4b. Structural comparisons between different clones indicate that multiple polyadenylation sites are responsible for the length heterogeneity observed for C1r mRNA from liver and Hep G2 cells.
摘要
对编码完整C1r前体蛋白的人肝脏cDNA克隆进行测序，证实了先前确定的肽序列，并表明存在一个长度为17个氨基酸的前导肽。在C1r A链中位于表皮生长因子共有序列内的一个暂定为β-羟基天冬氨酸的残基[Arlaud、Willis和Gagnon（1986年），《生物化学杂志》，即将发表]，被发现编码为天冬酰胺。在A链中串联定位的两个序列元件与在与C3b或C4b相互作用的蛋白质中广泛存在的一个序列相关。不同克隆之间的结构比较表明，多个聚腺苷酸化位点导致了从肝脏和Hep G2细胞中观察到的C1r mRNA长度异质性。
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