| Primary Identifier | IPR027482 | Type | Homologous_superfamily |
| Short Name | Sec1-like_dom2 |
| description | Sec1-like molecules have been implicated in a variety of eukaryotic vesicle transport processes including neurotransmitter release by exocytosis [].They regulate vesicle transport by binding to a t-SNARE from the syntaxin family. This process is thought to prevent SNARE complex formation, a protein complex required for membrane fusion. Whereas Sec1 molecules are essential for neurotransmitter release and other secretory events, their interaction with syntaxin molecules seems to represent a negative regulatory step in secretion []. The nSec1 polypeptide chain can be divided into three domains. The first domain, consists of a five-stranded parallel β-sheet flanked by five α-helices. The second domain, like the first one, has an α-β-alpha fold, however the β-sheet of domain 2 features five parallel strands with an additional antiparallel strand on one edge. The third domain is a large insertion between the third and fourth parallel strands of domain 2, and can be subdivided in two [].This entry represents domain 2 from the Sec1 family which includes Sec1, Sly1, Slp1/Vps33, yeast Vps45/Stt10, Unc-18 from nematodes, Munc-18b/muSec1, Munc-18c from mouse, Rop from Drosophila, Munc-18/n-Sec1/rbSec1A and rbSec1B from rat [, , , ]. |
