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http://purl.uniprot.org/citations/9827539http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9827539http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9827539http://www.w3.org/2000/01/rdf-schema#comment"We have recently cloned a cDNA for mouse matrilin-4. By sequence comparison we identified the 12 kb long human matrilin-4 gene as a part of a high-throughput genomic sequence (HS453C12) in the databases. Additionally we found a human matrilin-4 expressed sequence tag (H54037) in the database that had been mapped to chromosome 20q13.1-2. The gene contains 10 exons and, like the matrilin-1 gene, the human matrilin-4 gene contains an AT-AC intron between the two exons encoding the coiled-coil domain. The cDNA sequence of human matrilin-4 was determined by sequencing of RT-PCR products obtained from mRNA of the human embryonic kidney cell line HEK 293. At the amino acid level it showed an overall sequence identity to the mature mouse matrilin-4 of 91% with a maximum of 97% in the second vWFA-like module. Alternative splicing leads to three different mRNAs. They all encode the putative signal peptide, the two vWFA-like domains and the potential coiled-coil alpha-helical oligomerisation domain but differ in that either one, two or three EGF-like domains are retained in the mature mRNA. Due to a G to A mutation at the splice donor site of intron C, the third exon encodes an untranslated pseudo-exon specifying the first EGF-like domain when compared to mouse matrilin-4."xsd:string
http://purl.uniprot.org/citations/9827539http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(98)01293-9"xsd:string
http://purl.uniprot.org/citations/9827539http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(98)01293-9"xsd:string
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/author"Wagener R."xsd:string
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/author"Wagener R."xsd:string
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/author"Kobbe B."xsd:string
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/author"Kobbe B."xsd:string
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/author"Paulsson M."xsd:string
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/author"Paulsson M."xsd:string
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/pages"165-170"xsd:string
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/pages"165-170"xsd:string
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/title"Genomic organisation, alternative splicing and primary structure of human matrilin-4."xsd:string
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/title"Genomic organisation, alternative splicing and primary structure of human matrilin-4."xsd:string
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/volume"438"xsd:string
http://purl.uniprot.org/citations/9827539http://purl.uniprot.org/core/volume"438"xsd:string
http://purl.uniprot.org/citations/9827539http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9827539
http://purl.uniprot.org/citations/9827539http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9827539
http://purl.uniprot.org/citations/9827539http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9827539
http://purl.uniprot.org/citations/9827539http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9827539