SSA3 Hsp70 family ATPase SSA3 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SSA3
Official Full Name: Hsp70 family ATPase SSA3
Primary source: SGD:S000000171
Locus tag: YBL075C
See related: AllianceGenome:SGD:S000000171; FungiDB:YBL075C; VEuPathDB:YBL075C
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: YG106
Summary: Enables ATP hydrolysis activity and unfolded protein binding activity. Involved in SRP-dependent cotranslational protein targeting to membrane, translocation; protein folding; and protein quality control for misfolded or incompletely synthesized proteins. Located in cytosol. Human ortholog(s) of this gene implicated in several diseases, including Kawasaki disease; artery disease (multiple); autoimmune disease of musculoskeletal system (multiple); neurodegenerative disease (multiple); and schizophrenia (multiple). Orthologous to several human genes including HSPA8 (heat shock protein family A (Hsp70) member 8). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See SSA3 in Genome Data Viewer

Location:: chromosome: II

Exon count:: 1

Sequence:: Chromosome: II; NC_001134.8 (84499..86448, 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?

Hsp70 binding regulates Sti1 conformation.
Title: Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.
three histone methylation mutants exhibited more severe growth defects and slower activation of GAL1, SSA3 and PHO5 than those of wild type
Title: [Effects of histone H3 K4L and K36L mutations on the cell growth and the transcription of GAL1, SSA3 and PHO5 in Saccharomyces cerevisiae].
Analysis of a previously uncharacterized region of Pam16 revealed its requirement for formation of an active Pam18:Pam16 complex able to stimulate Hsp70's ATPase activity.
Title: Reevaluation of the role of the Pam18:Pam16 interaction in translocation of proteins by the mitochondrial Hsp70-based import motor.
The complex formation between the C-terminal motif of Hsp70/Hsp90 and Tom71 could lock Tom71 in the open state where the preprotein-binding pocket of Tom71 is ready to receive preproteins.
Title: Molecular chaperone Hsp70/Hsp90 prepares the mitochondrial outer membrane translocon receptor Tom71 for preprotein loading.
Functional rescue of mutant human cystathionine beta-synthase by manipulation of Hsp26 and Hsp70 levels in Saccharomyces cerevisiae.
Title: Functional rescue of mutant human cystathionine beta-synthase by manipulation of Hsp26 and Hsp70 levels in Saccharomyces cerevisiae.
Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions
Title: Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.
results indicated that histone acetylation was required for the transcriptional activation of SSA3 and SSA4
Title: Gcn5- and Elp3-induced histone H3 acetylation regulates hsp70 gene transcription in yeast.

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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	IGI Inferred from Genetic Interaction more info	PubMed
enables ATP-dependent protein folding chaperone	IEA Inferred from Electronic Annotation more info
enables heat shock protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein folding chaperone	IBA Inferred from Biological aspect of Ancestor more info
enables unfolded protein binding	IGI Inferred from Genetic Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in SRP-dependent cotranslational protein targeting to membrane, translocation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in chaperone cofactor-dependent protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein quality control for misfolded or incompletely synthesized proteins	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein refolding	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: Hsp70 family ATPase SSA3

NP_009478.1

ATPase involved in protein folding and the response to stress; plays a role in SRP-dependent cotranslational protein-membrane targeting and translocation; member of the heat shock protein 70 (HSP70) family; localized to the cytoplasm; SSA3 has a paralog, SSA4, that arose from the whole genome duplication

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

84499..86448 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178315.1 → NP_009478.1 TPA: Hsp70 family ATPase SSA3 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_009478.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VPS7, P09435, P18862

UniProtKB/TrEMBL

A6ZKM6, B3LNK8, C7GK58, C8Z3R8, N1P8N4

Conserved Domains (1) summary

PTZ00009
Location:4 → 649

PTZ00009; heat shock 70 kDa protein; Provisional