TY - JOUR

T1 - Exon organization of the mouse entactin gene corresponds to the structural domains of the polypeptide and has regional homology to the low-density lipoprotein receptor gene

AU - Durkin, M E

AU - Wewer, U M

AU - Chung, A E

PY - 1995/3/20

Y1 - 1995/3/20

N2 - Entactin is a widespread basement membrane protein of 150 kDa that binds to type IV collagen and laminin. The complete exon-intron structure of the mouse entactin gene has been determined from lambda genomic DNA clones. The gene spans at least 65 kb and contains 20 exons. The exon organization of the mouse entactin gene closely corresponds to the organization of the polypeptide into distinct structural and functional domains. The two amino-terminal globular domains are encoded by three exons each. Single exons encode the two protease-sensitive, O-glycosylated linking regions. The six EGF-like repeats and the single thyroglobulin-type repeat are each encoded by separate exons. The carboxyl-terminal half of entactin displays sequence homology to the growth factor-like region of the low-density lipoprotein receptor, and in both genes this region is encoded by eight exons. The positions of four introns are also conserved in the homologous region of the two genes. These observations suggest that the entactin gene has evolved via exon shuffling. Finally, several sequence polymorphisms useful for gene linkage analysis were found in the 3' noncoding region of the last exon.

AB - Entactin is a widespread basement membrane protein of 150 kDa that binds to type IV collagen and laminin. The complete exon-intron structure of the mouse entactin gene has been determined from lambda genomic DNA clones. The gene spans at least 65 kb and contains 20 exons. The exon organization of the mouse entactin gene closely corresponds to the organization of the polypeptide into distinct structural and functional domains. The two amino-terminal globular domains are encoded by three exons each. Single exons encode the two protease-sensitive, O-glycosylated linking regions. The six EGF-like repeats and the single thyroglobulin-type repeat are each encoded by separate exons. The carboxyl-terminal half of entactin displays sequence homology to the growth factor-like region of the low-density lipoprotein receptor, and in both genes this region is encoded by eight exons. The positions of four introns are also conserved in the homologous region of the two genes. These observations suggest that the entactin gene has evolved via exon shuffling. Finally, several sequence polymorphisms useful for gene linkage analysis were found in the 3' noncoding region of the last exon.

KW - Amino Acid Sequence

KW - Animals

KW - Consensus Sequence

KW - Exons

KW - Genes

KW - Membrane Glycoproteins

KW - Mice

KW - Mice, Inbred AKR

KW - Mice, Inbred C57BL

KW - Mice, Inbred CBA

KW - Molecular Sequence Data

KW - Protein Structure, Tertiary

KW - Receptors, LDL

KW - Sequence Homology, Amino Acid

M3 - Journal article

C2 - 7601446

VL - 26

SP - 219

EP - 228

JO - Genomics

JF - Genomics

SN - 0888-7543

IS - 2

ER -