CLONING AND SEQUENCE-ANALYSIS OF BETA-4 CDNA - AN INTEGRIN SUBUNIT THAT CONTAINS A UNIQUE 118 KD CYTOPLASMIC DOMAIN
CLONING AND SEQUENCE-ANALYSIS OF BETA-4 CDNA - AN INTEGRIN SUBUNIT THAT CONTAINS A UNIQUE 118 KD CYTOPLASMIC DOMAIN
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DOI：
10.1002/j.1460-2075.1990.tb08171.x
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发表时间：
1990-03-01
期刊：
影响因子：
11.4
通讯作者：
SONNENBERG, A
中科院分区：
文献类型：
--
作者：
HOGERVORST, F;KUIKMAN, I;SONNENBERG, A
.alpha.6.beta。4复合体是粘附受体整合素超家族的一员。利用单克隆抗体筛选人角化细胞lambda gt11 cDNA文库。4个亚基。选择两个cDNA，随后用于分离一套完整的重叠cDNA克隆。度量。4亚基由1778个氨基酸组成，胞外结构域由683个氨基酸组成，跨膜结构域由23个氨基酸组成，胞质结构域由1072个残基组成。推导出的氨基酸末端序列与已发表的纯化的.beta氨基酸末端序列吻合良好。胞外结构域包含5个潜在的n链糖基化位点和4个富含半胱氨酸的同源重复序列。细胞外部分。4个亚基序列与其他整合蛋白有35%的同源性。亚基是这类分子中最不同的。跨膜区域保守性较差，而细胞质结构域在任何区域都与已知的。β的细胞质尾部没有实质的同一性。序列或其他蛋白质序列。异常长的细胞质结构域表明- β蛋白之间存在明显的相互作用。4个亚基与细胞质蛋白。
The .alpha.6.beta.4 complex is a member of the integrin superfamily of adhesion receptors. A human keratinocyte lambda gt11 cDNA library was screened using a monoclonal antibody directed against the .beta.4 subunit. Two cDNAs were selected and subsequently used to isolate a complete set of overlapping cDNA clones. The .beta.4 subunit consists of 1778 amino acids with a 683 amino acid extracellular domain, a 23 amino acid trans-membrane domain and an exceptionally long cytoplasmic domain of 1072 residues. The deduced amino-terminal sequence is in good agreement with the published amino-terminal sequence of purified .beta.4. The extracellular domain contains five potential N-linked glycosylation sites and four cysteine-rich homologous repeat sequences. The extracellular part of the .beta.4 subunit sequence shows 35% identity with other integrin .beta. subunits, but is the most different among this class of molecules. The trans-membrane region is poorly conserved, whereas the cytoplasmic domain shows no substantial identity in any region to the cytoplasmic tails of the known .beta. sequences or to other protein sequences. The exceptionally long cytoplasmic domain suggests distinct interactions of the .beta.4 subunit with cytoplasmic proteins.