SEC18 AAA family ATPase SEC18 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SEC18
Official Full Name: AAA family ATPase SEC18
Primary source: SGD:S000000284
Locus tag: YBR080C
See related: AllianceGenome:SGD:S000000284; FungiDB:YBR080C; VEuPathDB:YBR080C
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: ANU4
Summary: Enables ATP hydrolysis activity; SNARE binding activity; and phosphatidic acid binding activity. Involved in Golgi vesicle transport; SNARE complex disassembly; and vacuole organization. Located in Golgi apparatus. Human ortholog(s) of this gene implicated in developmental and epileptic encephalopathy 96. Orthologous to human NSF (N-ethylmaleimide sensitive factor, vesicle fusing ATPase). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See SEC18 in Genome Data Viewer

Location:: chromosome: II

Exon count:: 1

Sequence:: Chromosome: II; NC_001134.8 (398614..400890, complement)

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 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.
We also show that IPA more potently and specifically inhibits NSF/Sec18 activity than does N-ethylmaleimide, requiring the administration of only low micromolar concentrations of IPA, demonstrating that this compound could help to further elucidate SNARE-priming dynamics
Title: A small-molecule competitive inhibitor of phosphatidic acid binding by the AAA+ protein NSF/Sec18 blocks the SNARE-priming stage of vacuole fusion.
IPA did not interfere with PA binding to another known target or with Sec18 binding to other kinds of lipids or with other steps in the in vitro fusion assay, indicating clear specificity.
Title: New gadget in the membrane trafficking toolbox: A novel inhibitor of SNARE priming.
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.
PA regulates Sec18 function by altering its architecture and stabilizing membrane-bound Sec18 protomers
Title: Phosphatidic acid induces conformational changes in Sec18 protomers that prevent SNARE priming.
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.
In vitro, Sly1 and Vps33 impede SNARE complex disassembly by Sec18 and ATP
Title: SM proteins Sly1 and Vps33 co-assemble with Sec17 and SNARE complexes to oppose SNARE disassembly by Sec18.
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.

Submit: New GeneRIF Correction See all GeneRIFs (13)

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 ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IBA Inferred from Biological aspect of Ancestor more info
enables ATP hydrolysis activity	IDA Inferred from Direct Assay more info	PubMed
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
enables SNARE binding	IDA Inferred from Direct Assay more info	PubMed
enables phosphatidic acid binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in Golgi to plasma membrane protein transport	IBA Inferred from Biological aspect of Ancestor more info
involved_in Golgi to plasma membrane protein transport	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in SNARE complex disassembly	IDA Inferred from Direct Assay more info	PubMed
involved_in SNARE complex disassembly	IEA Inferred from Electronic Annotation more info
involved_in autophagosome assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in endoplasmic reticulum to Golgi vesicle-mediated transport	IDA Inferred from Direct Assay more info	PubMed
involved_in inter-Golgi cisterna vesicle-mediated transport	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in intra-Golgi vesicle-mediated transport	IBA Inferred from Biological aspect of Ancestor more info
involved_in macroautophagy	IMP Inferred from Mutant Phenotype more info	PubMed
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
located_in Golgi apparatus	IDA Inferred from Direct Assay more info	PubMed
is_active_in Golgi stack	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	HDA more info	PubMed
located_in mating projection tip	HDA more info	PubMed

General protein information

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Preferred Names: AAA family ATPase SEC18

NP_009636.3

AAA ATPase and SNARE disassembly chaperone; required for vesicular transport between ER and Golgi, the 'priming' step in homotypic vacuole fusion, autophagy, and protein secretion; releases Sec17p from SNAP complexes; has similarity to mammalian N-ethylmaleimide-sensitive factor (NSF)

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001134.8 Reference assembly

Range

398614..400890 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178428.3 → NP_009636.3 TPA: AAA family ATPase SEC18 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_009636.3

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VQ79, P18759, Q07067

UniProtKB/TrEMBL

A6ZL24, B5VE44, C7GQJ3, N1P9E8

Conserved Domains (4) summary

smart01072
Location:134 → 204

CDC48_2; Cell division protein 48 (CDC48) domain 2

smart01073
Location:29 → 98

CDC48_N; Cell division protein 48 (CDC48) N-terminal domain

COG0464
Location:263 → 758

SpoVK; AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]

cd19504
Location:240 → 416

RecA-like_NSF-SEC18_r1-like; first of two ATPase domains of NSF and SEC18, and similar ATPase domains