SEC17 Sec17p [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SEC17
Official Full Name: Sec17p
Primary source: SGD:S000000146
Locus tag: YBL050W
See related: AllianceGenome:SGD:S000000146; FungiDB:YBL050W; VEuPathDB:YBL050W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: RNS3
Summary: Enables ATPase activator activity and soluble NSF attachment protein activity. Involved in SNARE complex disassembly; autophagy; and organelle fusion. Located in cytosol. Part of SNARE complex. Human ortholog(s) of this gene implicated in developmental and epileptic encephalopathy 107. Orthologous to several human genes including NAPB (NSF attachment protein beta). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See SEC17 in Genome Data Viewer

Location:: chromosome: II

Exon count:: 2

Sequence:: Chromosome: II; NC_001134.8 (125125..126119)

Chromosome II - NC_001134.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001134.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Fusion with wild-type SNARE domains is controlled by juxtamembrane domains, transmembrane anchors, and Sec17.
Title: Fusion with wild-type SNARE domains is controlled by juxtamembrane domains, transmembrane anchors, and Sec17.
Fusion of tethered membranes can be driven by Sec18/NSF and Sec17/alphaSNAP without HOPS.
Title: Fusion of tethered membranes can be driven by Sec18/NSF and Sec17/αSNAP without HOPS.
SNARE-only fusion is abolished by Sec17 and Sec18. Efficient fusion with Sec17 and Sec18 requires a tripartite match between the organellar identities of the R-SNARE, the Q-SNAREs, and the SM protein/complex. Sec17 and Sec18 are not simply negative regulators; they stimulate fusion with either vacuolar SNAREs and their SM protein complex HOPS or endoplasmic reticulum/cis-Golgi SNAREs and their SM protein Sly1.
Title: Sec17 (α-SNAP) and Sec18 (NSF) restrict membrane fusion to R-SNAREs, Q-SNAREs, and SM proteins from identical compartments.
When SNAREs are more disassembled, as by Sec17, Sec18, and ATP (adenosine triphosphate), HOPS is required, and GST-PX does not suffice.
Title: Tethering guides fusion-competent trans-SNARE assembly.
Thus, Vps33/HOPS promotes productive SNARE assembly in the presence of otherwise inhibitory Sec17.
Title: Sec17 (α-SNAP) and an SM-tethering complex regulate the outcome of SNARE zippering in vitro and in vivo.
Sec17 and Sec18 act twice in the fusion cycle, binding to trans-SNARE complexes to accelerate fusion, then hydrolyzing ATP to disassemble cis-SNARE complexes.
Title: Sec17/Sec18 act twice, enhancing membrane fusion and then disassembling cis-SNARE complexes.
Sec17 binds to trans-SNARE complexes, oligomerizes, and inserts apolar loops into the apposed membranes, locally disturbing the lipid bilayer and lowering the energy barrier for fusion without Sec18
Title: Sec17 can trigger fusion of trans-SNARE paired membranes without Sec18.
Using a reconstituted proteoliposome fusion system, the authors show that trans-SNARE complex, like cis-SNARE complex, is sensitive to Sec17p/Sec18p mediated disassembly.
Title: HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusion.
Data show that the ternary synergy of phosphoinositides and 2 SNARE chaperone systems (SNARE Vam7p and Sec17p/Sec18p/ATP
Title: Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables ATPase activator activity	IDA Inferred from Direct Assay more info	PubMed
enables soluble NSF attachment protein activity	IBA Inferred from Biological aspect of Ancestor more info
enables soluble NSF attachment protein activity	IDA Inferred from Direct Assay more info	PubMed
enables soluble NSF attachment protein activity	IPI Inferred from Physical Interaction more info	PubMed
enables syntaxin binding	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in SNARE complex disassembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in SNARE complex disassembly	IDA Inferred from Direct Assay more info	PubMed
involved_in autophagy	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in intracellular protein transport	IBA Inferred from Biological aspect of Ancestor more info
involved_in intracellular protein transport	IEA Inferred from Electronic Annotation more info
involved_in protein transport	IEA Inferred from Electronic Annotation more info
involved_in vacuole fusion, non-autophagic	IDA Inferred from Direct Assay more info	PubMed
involved_in vesicle fusion with Golgi apparatus	IDA Inferred from Direct Assay more info	PubMed
involved_in vesicle-mediated transport	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of SNARE complex	IBA Inferred from Biological aspect of Ancestor more info
part_of SNARE complex	IPI Inferred from Physical Interaction more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in fungal-type vacuole membrane	HDA more info	PubMed
located_in membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Sec17p

NP_009503.1

Alpha-SNAP cochaperone; SNARE-complex adaptor for Sec18 (NSF) during the disassembly of postfusion cis-SNARE complexes; stimulates the ATPase activity of Sec18p; peripheral membrane protein required for vesicular transport between ER and Golgi, the 'priming' step in homotypic vacuole fusion, and autophagy; similar to mammalian alpha-SNAP