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change 2024-03-14: GO:0099056 replaced by GO:0042734"},{"key":"comment","value":"Rationale: In the context of initial functional studies on the role of synaptotagmin-7 in Ca-dependent release, the authors characterize the subcellular localization of the protein. Sugita et al develop an antibody recognizing the connecting sequence between the N-terminus and the C2A domain of synaptotagmin- 7. By utilizing the antibody to study the tissue distribution of the protein, the authors detect multiple isoforms in different brain regions and show that expression increases in development-dependent manner (Fig 3). Immunocytochemical analysis by light microscopy shows enhanced expression of the protein in mossy fiber terminals and brain stem neurons. Immuno-EM of hippocampal neurons suggests plasma membrane localization of the protein. This observation is supported by monitoring the distribution of the protein during subcellular fractionation of rat brain, which shows strong enrichment of synaptotagmin 7 isoforms in fractions enriched in plasma membranes and conspicuous absence of signal in the synaptic vesicle fraction. (Fig. 4-5) In addition, expression of long, short or truncated isoforms (identified by genomic analysis, Fig. 2) as GFP-tagged proteins in PC12 cells shows clear localization to the plasma membrane (Fig. 6)\n\n1/2/2018 Pim\n- Based on the known transmembrane topology of the protein, the \"integral component of ... membrane\" term was chosen.. Experimental description: Experimental Procedures\n\nA rat brain cDNA-library was screened with cDNA probes from synaptotagmin VII as described (Li et al., 1995a), leading to the isolation of multiple cDNA clones with different combinations of alternatively spliced inserts."},{"key":"https://w3id.org/biolink/vocab/in_taxon","value":"http://purl.obolibrary.org/obo/NCBITaxon_10116"}]}