MEMBRANE GUANYLATE-CYCLASE IS A CELL-SURFACE RECEPTOR WITH HOMOLOGY TO PROTEIN-KINASES
MEMBRANE GUANYLATE-CYCLASE IS A CELL-SURFACE RECEPTOR WITH HOMOLOGY TO PROTEIN-KINASES
复制标题
DOI：
10.1038/334708a0
复制
发表时间：
1988-08-25
期刊：
影响因子：
64.8
通讯作者：
GARBERS, DL
中科院分区：
文献类型：
--
作者：
SINGH, S;LOWE, DG;GARBERS, DL
鸟苷酸环化酶在精子上作为趋化肽的细胞表面受体1，在其他各种细胞上作为心房钠素肽的受体2 - 4。react （Cys-Val-Thr-Gly-Ala-Pro-Gly-Cys-Val-Gly-Gly-Gly-Arg-Leu-NH2）是由海胆（arbacia punctulataaae）卵释放的趋化肽，特异交联于a。点状曲霉菌鸟苷酸环化酶。在肽结合后，鸟苷酸环化酶的磷酸化状态调节酶的活性1,5,6。我们在此报道，推断的鸟苷酸环化酶精子膜形式的氨基酸序列预测了986个氨基酸的内在膜蛋白与氨基末端信号序列。一个单一的跨膜结构域将蛋白质分成假定的细胞外和细胞质催化结构域。胞质羧基末端95个氨基酸含有20%的丝氨酸，可能是磷酸化的调控位点。出乎意料的是，这种酶与蛋白激酶家族是同源的。
Guanylate cyclase has been strongly implicated as a cell-surface receptor on spermatozoa for a chemotactic peptide1, and on various other cells as a receptor for atrial natriuretic peptides2–4. Resact (Cys-Val-Thr-Gly-Ala-Pro-Gly-Cys-Val-Gly-Gly-Gly-Arg-Leu-NH2), the chemotactic peptide released by sea urchinArbacia punctulataeggs, is specifically crosslinked toA.punctulataspermatozoan guanylate cyclase1. After the binding of the peptide the state of guanylate cyclase phosphorylation modulates enzyme activity1,5,6. We report here that the deduced amino-acid sequence of the spermatozoan membrane form of guanylate cyclase predicts an intrinsic membrane protein of 986 amino acids with an amino-terminal signal sequence. A single transmembrane domain separates the protein into putative extracellular and cytoplasmic-catalytic domains. The cytoplasmic carboxyl-terminal 95 amino acids contain 20% serine, the likely regulatory sites for phosphory-lation. Unexpectedly, the enzyme is homologous to the protein kinase family.