Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-4-9
pubmed:abstractText
Synaptophysin is an integral membrane protein of synaptic vesicles found in neurons and endocrine cells. Synaptophysin monomers associate into hexamers forming a large conductance channel. We present an analysis of synaptophysin from the nervous system of the marine ray Torpedo californica. Analysis of cDNA clones reveals a 62% amino acid similarity between the Torpedo and rat sequences. The 4 hydrophobic membrane spanning domains and the glycosylation site are conserved. In contrast, the two intravesicular loops connecting the membrane spanning regions, show varying degrees of sequence conservation, suggesting that portions of these domains may play critical functional roles. The carboxyterminal tail has been proposed to bind calcium and is a major site for tyrosine phosphorylation. The precise sequence of this region has almost completely diverged while the proline-tyrosine rich nature is maintained. Blotting studies reveal the RNA and the protein in nervous system tissues and demonstrate that the molecule copurifies with cholinergic synaptic vesicles.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-8993
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
509
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Torpedo synaptophysin: evolution of a synaptic vesicle protein.
pubmed:affiliation
Department of Biological Sciences, Stanford University, CA 94305.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't