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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11-12
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pubmed:dateCreated |
1999-10-19
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pubmed:databankReference |
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pubmed:abstractText |
Circulation and tissue colonization are essential properties of lymphoid cells and involve major families of adhesion molecules (e.g. , integrin, selectin, mucin-like, and molecules from the immunoglobulin superfamily). The mouse Vanin-1 molecule was recently identified and found to be involved in the colonization of the thymus by hematopoietic precursor cells. Here we show based on computational analysis of EST sequence database resources that Vanin-1 belongs to a new family of related molecules present from drosophila to human. This family includes the amidase enzyme Biotinidase, and a central protein domain is shared between Vanin and Nitrilase families, suggesting that Vanin molecules might bear an enzymatic activity. Five of these molecules were new uncharacterized cDNA sequences only described as ESTs. The three human Vanin genes map to the same region of Chromosome 6q. The detailed results are consultable at the VANIN web page (http://tagc. univ-mrs.fr/pub/vanin/).
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Amidohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Aminohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Biotinidase,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GPI-Linked Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/VNN2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/nitrilase,
http://linkedlifedata.com/resource/pubmed/chemical/pantetheinase
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0093-7711
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
49
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
964-72
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:10501839-Amidohydrolases,
pubmed-meshheading:10501839-Amino Acid Sequence,
pubmed-meshheading:10501839-Aminohydrolases,
pubmed-meshheading:10501839-Animals,
pubmed-meshheading:10501839-Biotinidase,
pubmed-meshheading:10501839-Cell Adhesion Molecules,
pubmed-meshheading:10501839-Chromosome Mapping,
pubmed-meshheading:10501839-Chromosomes, Human, Pair 6,
pubmed-meshheading:10501839-DNA, Complementary,
pubmed-meshheading:10501839-Drosophila Proteins,
pubmed-meshheading:10501839-Drosophila melanogaster,
pubmed-meshheading:10501839-Evolution, Molecular,
pubmed-meshheading:10501839-Expressed Sequence Tags,
pubmed-meshheading:10501839-Fungal Proteins,
pubmed-meshheading:10501839-GPI-Linked Proteins,
pubmed-meshheading:10501839-Helminth Proteins,
pubmed-meshheading:10501839-Humans,
pubmed-meshheading:10501839-Hydrolases,
pubmed-meshheading:10501839-Insect Proteins,
pubmed-meshheading:10501839-Molecular Sequence Data,
pubmed-meshheading:10501839-Multigene Family,
pubmed-meshheading:10501839-Phylogeny,
pubmed-meshheading:10501839-Sequence Alignment,
pubmed-meshheading:10501839-Sequence Homology, Amino Acid,
pubmed-meshheading:10501839-Species Specificity
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pubmed:year |
1999
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pubmed:articleTitle |
An ESTs description of the new Vanin gene family conserved from fly to human.
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pubmed:affiliation |
TAGC (Technologie Avancée pour le Génome et la Clinique), Centre d'Immunologie de Marseille-Luminy INSERM-CNRS, Parc Scientifique de Luminy, case 906, 13288 Marseille Cedex 09, France.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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