cDNA cloning, genomic organization and chromosomal localization of human heparan glucosaminyl N-deacetylase/N-sulphotransferase-2

The cDNA and gene encoding human heparan glucosaminyl N-deacetylase/N-sulphotransferase-2 have been cloned. The cDNA encoded a protein of 883 amino acids that was 94% similar to heparan N-sulphotransferase-2 from mouse mast cells. Comparison of the deduced amino acid sequences of human heparan N-sul...

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Veröffentlicht in:Biochemical journal 1998-06, Vol.332 ( Pt 2) (2), p.303-307
Hauptverfasser: Humphries, D E, Lanciotti, J, Karlinsky, J B
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container_title Biochemical journal
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creator Humphries, D E
Lanciotti, J
Karlinsky, J B
description The cDNA and gene encoding human heparan glucosaminyl N-deacetylase/N-sulphotransferase-2 have been cloned. The cDNA encoded a protein of 883 amino acids that was 94% similar to heparan N-sulphotransferase-2 from mouse mast cells. Comparison of the deduced amino acid sequences of human heparan N-sulphotransferase-1 and -2 showed that the enzymes were 70% similar; greater than 90% of the amino acids between residues 418 and 543 were identical. The least conserved amino acids were found in the N-terminus/putative transmembrane regions of the two enzymes. The human heparan N-sulphotransferase-2 gene was localized to chromosome arm 10q (band 10q22) by in situ fluorescent hybridization. The gene contains 13 exons spanning 6.5 kb, ranging in size from 88 bp (exon 2) to >1 kb (exon 1), and 12 introns, which were found to occur at similar sites within the coding sequence of the human heparan N-sulphotransferase-1 gene. The structure of the two genes differed in that the heparan N-sulphotransferase-1 gene contained one additional intron. The similarity of the heparan N-sulphotransferase-1 and -2 proteins and their similar exon-intron organization suggest that they derive from a common ancestral gene.
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The cDNA encoded a protein of 883 amino acids that was 94% similar to heparan N-sulphotransferase-2 from mouse mast cells. Comparison of the deduced amino acid sequences of human heparan N-sulphotransferase-1 and -2 showed that the enzymes were 70% similar; greater than 90% of the amino acids between residues 418 and 543 were identical. The least conserved amino acids were found in the N-terminus/putative transmembrane regions of the two enzymes. The human heparan N-sulphotransferase-2 gene was localized to chromosome arm 10q (band 10q22) by in situ fluorescent hybridization. The gene contains 13 exons spanning 6.5 kb, ranging in size from 88 bp (exon 2) to &gt;1 kb (exon 1), and 12 introns, which were found to occur at similar sites within the coding sequence of the human heparan N-sulphotransferase-1 gene. The structure of the two genes differed in that the heparan N-sulphotransferase-1 gene contained one additional intron. 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subjects Amidohydrolases - chemistry
Amino Acid Sequence
Chromosome Mapping
Chromosomes, Human, Pair 10 - genetics
Cloning, Molecular
Conserved Sequence - genetics
Exons - genetics
Humans
In Situ Hybridization, Fluorescence
Isoenzymes - chemistry
Molecular Sequence Data
RNA, Messenger - metabolism
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Sulfotransferases - chemistry
title cDNA cloning, genomic organization and chromosomal localization of human heparan glucosaminyl N-deacetylase/N-sulphotransferase-2
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