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Primary structure of the gene for the murine Ia antigen‐associated invariant chains (Ii). An alternatively spliced exon encodes a cysteine‐rich domain highly homologous to a repetitive sequence of thyroglobulin.
Author(s) -
Koch N.,
Lauer W.,
Habicht J.,
Dobberstein B.
Publication year - 1987
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1987.tb02417.x
Subject(s) - exon , biology , exon shuffling , exon trapping , microbiology and biotechnology , tandem exon duplication , gene , peptide sequence , coding region , alternative splicing , untranslated region , genetics , messenger rna
The gene for murine Ia‐associated invariant (Ii) chains (Ii31 and Ii41) was characterized by sequence analysis. The gene extends over approximately 9 kb and is organized in nine exons. Exon 1 encodes the 5′ untranslated region and the cytoplasmic segment, exon 2 the membrane spanning segment and adjacent amino acids and exons 3‐8 the extracytoplasmic portion of Ii31. Putative promoter sequences were found upstream of the start of the coding sequence. Between exons 6 and 7 an additional, alternatively spliced exon 6b has been identified. This exon is spliced into the mRNA coding for the Ii‐related Ii41 protein. Exon 6b encodes a cysteine‐rich domain of 64 amino acids. It shows a remarkably high homology to the repetitive elements in thyroglobulin, a precursor for thyroid hormone. Based on this homology, it is suggested that this domain (TgR) in Tg and in Ii41 may play a role either in hormone formation or as a carrier in the transport of molecules (thyroid hormone or processed antigen respectively) between intracellular compartments.