Member database | Pfam |
Pfam type | family |
Short name | Sec1 |
Author | Bateman A;0000-0002-6982-4660 Griffiths-Jones SR;0000-0001-6043-807X |
Sequence Ontology | 0100021 |
Description Imported from IPR001619
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].
References Imported from IPR001619
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
Integrated to
Representative structure
6xjl: Structure of the SM protein Vps45