SSM4 E3 ubiquitin-protein ligase SSM4 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Gene symbol: SSM4
Gene description: E3 ubiquitin-protein ligase SSM4
Primary source: FungiDB:YIL030C
Locus tag: YIL030C
See related: SGD:S000001292; AllianceGenome:SGD:S000001292; VEuPathDB:YIL030C
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: DOA10; KIS3
Summary: Enables ubiquitin protein ligase activity. Involved in retrograde protein transport, ER to cytosol and ubiquitin-dependent ERAD pathway. Located in nuclear inner membrane. Is integral component of endoplasmic reticulum membrane. Part of Doa10p ubiquitin ligase complex. Human ortholog(s) of this gene implicated in familial adult myoclonic epilepsy 3. Orthologous to human MARCHF6 (membrane associated ring-CH-type finger 6). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See SSM4 in Genome Data Viewer

Location:: chromosome: IX

Exon count:: 1

Sequence:: Chromosome: IX; NC_001141.2 (296050..300009, complement)

Chromosome IX - NC_001141.2 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001141.2

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Doa10 is a membrane protein retrotranslocase in ER-associated protein degradation.
Title: Doa10 is a membrane protein retrotranslocase in ER-associated protein degradation.
Sequential poly-ubiquitylation by specialized conjugating enzymes Ubc6 and Ubc7 expands the versatility of a quality control ubiquitin ligase Doa10.
Title: Sequential Poly-ubiquitylation by Specialized Conjugating Enzymes Expands the Versatility of a Quality Control Ubiquitin Ligase.
Here, the authors show that the ERAD ubiquitin ligase Doa10 controls the levels of some lipid droplet proteins.
Title: Spatial control of lipid droplet proteins by the ERAD ubiquitin ligase Doa10.
Data suggest that human MARCH6 and Saccharomyces cerevisiae Doa10 ubiquitin ligases are functionally similar.
Title: A Conserved C-terminal Element in the Yeast Doa10 and Human MARCH6 Ubiquitin Ligases Required for Selective Substrate Degradation.
Results show Ypf1 is an Endoplasmic Reticulum-resident aspartyl intramembrane protease with a presenilin fold, and identified Doa10 and Dfm1 as its cofactors.
Title: The yeast ER-intramembrane protease Ypf1 refines nutrient sensing by regulating transporter abundance.
the TEB4-Doa10 domain regulates Doa10 association with the Ubc6 membrane anchor, thereby controlling the degradation rate of the E2.
Title: An unusual transmembrane helix in the endoplasmic reticulum ubiquitin ligase Doa10 modulates degradation of its cognate E2 enzyme.
analysis of yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4
Title: Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI).
demonstration that Doa10 reaches the inner nuclear membrane; localization of Doa10 to the inner nuclear membrane is necessary for nuclear substrate degradation
Title: Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase.
Doa10 ubiquitinates both membrane and soluble proteins.
Title: Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways.

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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 metal ion binding	IEA Inferred from Electronic Annotation more info
enables transferase activity	IEA Inferred from Electronic Annotation more info
enables ubiquitin protein ligase activity	IDA Inferred from Direct Assay more info	PubMed
enables ubiquitin-protein transferase activity	IDA Inferred from Direct Assay more info	PubMed
enables zinc ion binding	IEA Inferred from Electronic Annotation more info
enables zinc ion binding	RCA inferred from Reviewed Computational Analysis more info	PubMed

Process	Evidence Code	Pubs
involved_in ERAD pathway	IBA Inferred from Biological aspect of Ancestor more info
involved_in ERAD pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein ubiquitination	IEA Inferred from Electronic Annotation more info
involved_in retrograde protein transport, ER to cytosol	IDA Inferred from Direct Assay more info	PubMed
involved_in retrograde protein transport, ER to cytosol	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of Doa10p ubiquitin ligase complex	IDA Inferred from Direct Assay more info	PubMed
located_in endoplasmic reticulum	HDA more info	PubMed
located_in endoplasmic reticulum	IEA Inferred from Electronic Annotation more info
is_active_in endoplasmic reticulum membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum membrane	IDA Inferred from Direct Assay more info	PubMed
located_in endoplasmic reticulum membrane	IEA Inferred from Electronic Annotation more info
located_in membrane	IEA Inferred from Electronic Annotation more info
located_in nuclear envelope	IDA Inferred from Direct Assay more info	PubMed
located_in nuclear inner membrane	IDA Inferred from Direct Assay more info	PubMed
located_in nuclear inner membrane	IEA Inferred from Electronic Annotation more info
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: E3 ubiquitin-protein ligase SSM4

NP_012234.3

EC 2.3.2.27

Membrane-embedded ubiquitin-protein ligase and retrotranslocase; ER and inner nuclear membrane localized RING-CH domain E3 ligase involved in ER-associated protein degradation (ERAD); aids Cdc48p in the extraction of faulty membrane proteins; targets misfolded cytosolic/nucleoplasmic domains of soluble and membrane embedded proteins (ERAD-C) and Sbh2p, a transmembrane domain-containing substrate (ERAD-M); C-terminal element, conserved in human ortholog MARCH6, determines substrate selectivity

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_001141.2 Reference assembly

Range

296050..300009 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179380.3 → NP_012234.3 TPA: E3 ubiquitin-protein ligase SSM4 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012234.3

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VVQ1, P40318

UniProtKB/TrEMBL

A0A8H4BZE1, B5VKR5, N1P957

Conserved Domains (1) summary

COG5183
Location:22 → 1319

SSM4; E3 ubiquitin-protein ligase DOA10 [Posttranslational modification, protein turnover, chaperones]