IPR043154
Sec1-like, domain 1
InterPro entry
Short name | Sec-1-like_dom1 |
Overlapping entries |
Description
This superfamily represents the domain 1 of Sec1 and related proteins.
Sec1-like molecules have been implicated in a variety of eukaryotic vesicle transport processes including neurotransmitter release by exocytosis
[2]. 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
[1].
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-α 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
[3].
Members of the Sec1 family include Sec1, Sly1, Slp1/Vps33, Vps45/Stt10 (yeast), Unc-18 (nematode), Munc-18b/muSec1, Munc-18c (mouse), Rop (Drosophila), Munc-18/n-Sec1/rbSec1A and rbSec1B (rat)
[2].
References
1.The X-ray crystal structure of neuronal Sec1 from squid sheds new light on the role of this protein in exocytosis. Bracher A, Perrakis A, Dresbach T, Betz H, Weissenhorn W. Structure 8, 685-94, (2000). View articlePMID: 10903948
2.The Sec1 family: a novel family of proteins involved in synaptic transmission and general secretion. Halachmi N, Lev Z. J. Neurochem. 66, 889-97, (1996). PMID: 8769846
3.Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex. Misura KM, Scheller RH, Weis WI. Nature 404, 355-62, (2000). View articlePMID: 10746715
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:3.40.50.2060