Amino acid sequence and domain structure of entactin. Homology with epidermal growth factor precursor and low density lipoprotein receptor.

M. E. Durkin, S. Chakravarti, B. B. Bartos, S. H. Liu, R. L. Friedman, A. E. Chung

Research output: Contribution to journalArticle

Abstract

Entactin (nidogen), a 150-kD sulfated glycoprotein, is a major component of basement membranes and forms a highly stable noncovalent complex with laminin. The complete amino acid sequence of mouse entactin has been derived from sequencing of cDNA clones. The 5.9-kb cDNA contains a 3,735-bp open reading frame followed by a 3'-untranslated region of 2.2 kb. The open reading frame encodes a 1,245-residue polypeptide with an unglycosylated Mr of 136,500, a 28-residue signal peptide, two Asn-linked glycosylation sites, and two potential Ca2+-binding sites. Analysis of the deduced amino acid sequence predicts that the molecule consists of two globular domains of 70 and 36 kD separated by a cysteine-rich domain of 28 kD. The COOH-terminal globular domain shows homology to the EGF precursor and the low density lipoprotein receptor. Entactin contains six EGF-type cysteine-rich repeat units and one copy of a cysteine-repeat motif found in thyroglobulin. The Arg-Gly-Asp cell recognition sequence is present in one of the EGF-type repeats, and a synthetic peptide from the putative cell-binding site of entactin was found to promote the attachment of mouse mammary tumor cells.

Original languageEnglish (US)
Pages (from-to)2749-2756
Number of pages8
JournalJournal of Cell Biology
Volume107
Issue number6 Pt 2
StatePublished - Dec 1988
Externally publishedYes

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LDL Receptors
Amino Acid Sequence
Epidermal Growth Factor
Cysteine
Open Reading Frames
Complementary DNA
Binding Sites
Peptides
Thyroglobulin
Protein Sequence Analysis
3' Untranslated Regions
Laminin
Protein Sorting Signals
Glycosylation
Basement Membrane
Glycoproteins
Clone Cells
nidogen
epidermal growth factor precursor
Breast Neoplasms

ASJC Scopus subject areas

  • Cell Biology

Cite this

Durkin, M. E., Chakravarti, S., Bartos, B. B., Liu, S. H., Friedman, R. L., & Chung, A. E. (1988). Amino acid sequence and domain structure of entactin. Homology with epidermal growth factor precursor and low density lipoprotein receptor. Journal of Cell Biology, 107(6 Pt 2), 2749-2756.

Amino acid sequence and domain structure of entactin. Homology with epidermal growth factor precursor and low density lipoprotein receptor. / Durkin, M. E.; Chakravarti, S.; Bartos, B. B.; Liu, S. H.; Friedman, R. L.; Chung, A. E.

In: Journal of Cell Biology, Vol. 107, No. 6 Pt 2, 12.1988, p. 2749-2756.

Research output: Contribution to journalArticle

Durkin, ME, Chakravarti, S, Bartos, BB, Liu, SH, Friedman, RL & Chung, AE 1988, 'Amino acid sequence and domain structure of entactin. Homology with epidermal growth factor precursor and low density lipoprotein receptor.', Journal of Cell Biology, vol. 107, no. 6 Pt 2, pp. 2749-2756.
Durkin, M. E. ; Chakravarti, S. ; Bartos, B. B. ; Liu, S. H. ; Friedman, R. L. ; Chung, A. E. / Amino acid sequence and domain structure of entactin. Homology with epidermal growth factor precursor and low density lipoprotein receptor. In: Journal of Cell Biology. 1988 ; Vol. 107, No. 6 Pt 2. pp. 2749-2756.
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