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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
32
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pubmed:dateCreated |
1991-1-8
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/J05666,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/J05667,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55675,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55676,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55677,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55678,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55679,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55680,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55681,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55682,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55683
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pubmed:abstractText |
Cartilage matrix protein (CMP) is a major component of the extracellular matrix of nonarticular cartilage. The structure and chromosomal location of the human gene encoding CMP was determined by molecular cloning analysis. We used a partial chicken CMP cDNA probe to isolate three overlapping human genomic clones. From one of these clones, a probe containing 2 human CMP exons was isolated and used to map the gene to chromosome 1p35 and to screen a human retina cDNA library. Two overlapping cDNA clones were isolated. The predicted protein sequence of 496 amino acids includes a 22-residue signal peptide and a 474-residue mature protein of Mr 51,344. The human CMP gene and polypeptide are strikingly similar to the chicken CMP gene and polypeptide. Human CMP is 79% identical to chicken CMP and contains two homologous domains separated by an epidermal growth factor-like domain. One potential N-glycosylation site is conserved between the two species. The human CMP gene spans 12 kilobase pairs with 8 exons and 7 introns which are similar in size to those of the chicken CMP gene. Both RNA splice junctions of intron G in the human and chicken CMP genes are nonconforming to the consensus splice sequences. This suggests that the CMP gene utilizes a new RNA splicing mechanism.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
265
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
19624-31
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2246248-Amino Acid Sequence,
pubmed-meshheading:2246248-Animals,
pubmed-meshheading:2246248-Base Sequence,
pubmed-meshheading:2246248-Chickens,
pubmed-meshheading:2246248-Chromosome Mapping,
pubmed-meshheading:2246248-Cloning, Molecular,
pubmed-meshheading:2246248-DNA Probes,
pubmed-meshheading:2246248-Exons,
pubmed-meshheading:2246248-Extracellular Matrix Proteins,
pubmed-meshheading:2246248-Glycoproteins,
pubmed-meshheading:2246248-Glycosylation,
pubmed-meshheading:2246248-Humans,
pubmed-meshheading:2246248-Introns,
pubmed-meshheading:2246248-Molecular Sequence Data,
pubmed-meshheading:2246248-Nucleic Acid Hybridization,
pubmed-meshheading:2246248-Polymorphism, Genetic,
pubmed-meshheading:2246248-Promoter Regions, Genetic,
pubmed-meshheading:2246248-Protein Biosynthesis,
pubmed-meshheading:2246248-RNA Splicing,
pubmed-meshheading:2246248-Restriction Mapping,
pubmed-meshheading:2246248-Sequence Homology, Nucleic Acid
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pubmed:year |
1990
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pubmed:articleTitle |
Structure and chromosomal location of the human gene encoding cartilage matrix protein.
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pubmed:affiliation |
Harold C. Simmons Arthritis Research Center, Dallas, Texas.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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