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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1995-12-4
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pubmed:databankReference | |
pubmed:abstractText |
A gene encoding a low-molecular-weight GTP-binding protein was isolated from a retinal cDNA library and mapped to human chromosome 17q12-q21. Comparison of the predicted protein with the protein databases revealed striking homology to the family of ADP-ribosylation factors (ARFs), which are thought to be involved in membrane trafficking and protein secretion. The greatest homology observed was with the rat ARF-like 4 protein (ARL4), with which it shared 58% identity, while the more highly conserved human ARF1 and ARF3 proteins each shared 46% identity. Inspection of the predicted new protein showed that it contained each of the six conserved motifs that are required for guanine nucleotide binding and hydrolysis, and thus it is probably a novel ARF isoform. We have designated the new protein and its corresponding gene ARF4L.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0888-7543
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
113-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7590735-ADP-Ribosylation Factor 1,
pubmed-meshheading:7590735-ADP-Ribosylation Factors,
pubmed-meshheading:7590735-Amino Acid Sequence,
pubmed-meshheading:7590735-Animals,
pubmed-meshheading:7590735-Base Sequence,
pubmed-meshheading:7590735-Chromosome Mapping,
pubmed-meshheading:7590735-Chromosomes, Human, Pair 17,
pubmed-meshheading:7590735-Cloning, Molecular,
pubmed-meshheading:7590735-GTP-Binding Proteins,
pubmed-meshheading:7590735-Humans,
pubmed-meshheading:7590735-Molecular Sequence Data,
pubmed-meshheading:7590735-Rats,
pubmed-meshheading:7590735-Sequence Alignment
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pubmed:year |
1995
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pubmed:articleTitle |
Isolation and mapping of a gene encoding a novel human ADP-ribosylation factor on chromosome 17q12-q21.
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pubmed:affiliation |
Huntsman Cancer Institute, University of Utah, Salt Lake City, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|