| First Author | Fukuda M | Year | 2001 |
| Journal | Biochem J | Volume | 354 |
| Issue | Pt 2 | Pages | 249-57 |
| PubMed ID | 11171101 | Mgi Jnum | J:67898 |
| Mgi Id | MGI:1931671 | Doi | 10.1042/0264-6021:3540249 |
| Citation | Fukuda M, et al. (2001) Characterization of KIAA1427 protein as an atypical synaptotagmin (Syt XIII). Biochem J 354(Pt 2):249-57 |
| abstractText | Synaptotagmin (Syt) belongs to a family of type-I membrane proteins and is a protein that consists of a short extracellular N-terminus, a single transmembrane domain, two C2 domains and a short C-terminus. Here, we cloned and characterized a mouse orthologue of human KIAA1427 protein as an atypical Syt (named Syt XIII). Subcellular fractionation and antibody-uptake experiments indicate that Syt XIII is indeed a type-I membrane protein, but, unlike other Syt isoforms, lacks an N-terminal extracellular domain. Syt XIII C2 domains show relatively little similarity to Syt I (less than 35% identity at the amino acid level), and lack key amino acids responsible for Ca(2+) binding. Because of these substitutions, the Syt XIII C2 domains did not show Ca(2+)-dependent phospholipid-binding activity, and Syt XIII is thus classified as a Ca(2+)-independent isoform. By contrast, the Syt XIII C-terminal domain is highly homologous with other Syt isoforms and can function as a common receptor for neurexin Ialpha in vitro. Since Syt XIII is expressed in various tissues outside the brain, Syt XIII may be involved in constitutive vesicle transport. |
