STE24 zinc metalloprotease [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: STE24
Official Full Name: zinc metalloprotease
Primary source: SGD:S000003878
Locus tag: YJR117W
See related: AllianceGenome:SGD:S000003878; FungiDB:YJR117W; VEuPathDB:YJR117W
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: AFC1; PIO2
Summary: Enables metalloendopeptidase activity. Involved in several processes, including negative regulation of post-translational protein targeting to membrane, translocation; post-translational protein targeting to membrane, translocation; and protein maturation. Located in endoplasmic reticulum membrane and nuclear inner membrane. Used to study metabolic dysfunction-associated steatotic liver disease; progeria; restrictive dermopathy; and type 2 diabetes mellitus. Human ortholog(s) of this gene implicated in mandibuloacral dysplasia type B lipodystrophy; progeria; restrictive dermopathy; and restrictive dermopathy 1. Orthologous to human ZMPSTE24 (zinc metallopeptidase STE24). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See STE24 in Genome Data Viewer

Location:: chromosome: X

Exon count:: 1

Sequence:: Chromosome: X; NC_001142.9 (642007..643368)

Chromosome X - NC_001142.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001142.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Overlapping function of Hrd1 and Ste24 in translocon quality control provides robust channel surveillance.
Title: Overlapping function of Hrd1 and Ste24 in translocon quality control provides robust channel surveillance.
The ER-associated protease Ste24 prevents N-terminal signal peptide-independent translocation into the endoplasmic reticulum in Saccharomyces cerevisiae.
Title: The ER-associated protease Ste24 prevents N-terminal signal peptide-independent translocation into the endoplasmic reticulum in Saccharomyces cerevisiae.
The tripartite architecture of the eukaryotic integral membrane protein zinc metalloprotease Ste24.
Title: The tripartite architecture of the eukaryotic integral membrane protein zinc metalloprotease Ste24.
It appears that the very nature of signal recognition particle (SRP)-independent translocation makes it susceptible to unique challenges such as clogging; upon clogging, Ste24 is recruited to the translocon, most likely with other factors. There, Ste24 proceeds to cleave the clogged protein, thereby resolving the stalemate scenario and salvaging the translocon.
Title: The Protease Ste24 Clears Clogged Translocons.
the crystal structure of the CAAX protease Ste24p, a zinc metalloprotease catalyzing two proteolytic steps in the maturation of yeast mating pheromone a-factor was determined.
Title: Structure of the integral membrane protein CAAX protease Ste24p.

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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 endopeptidase activity	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables metalloendopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables metalloendopeptidase activity	IDA Inferred from Direct Assay more info	PubMed
enables metalloendopeptidase activity	IEA Inferred from Electronic Annotation more info
enables metallopeptidase activity	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 CAAX-box protein processing	IBA Inferred from Biological aspect of Ancestor more info
involved_in CAAX-box protein processing	IEA Inferred from Electronic Annotation more info
involved_in CAAX-box protein processing	IGI Inferred from Genetic Interaction more info	PubMed
involved_in CAAX-box protein processing	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in ERAD pathway	IGI Inferred from Genetic Interaction more info	PubMed
involved_in ERAD pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of post-translational protein targeting to membrane, translocation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in peptide mating pheromone maturation involved in positive regulation of conjugation with cellular fusion	IDA Inferred from Direct Assay more info	PubMed
involved_in peptide mating pheromone maturation involved in positive regulation of conjugation with cellular fusion	IGI Inferred from Genetic Interaction more info	PubMed
involved_in peptide mating pheromone maturation involved in positive regulation of conjugation with cellular fusion	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in post-translational protein targeting to membrane, translocation	IGI Inferred from Genetic Interaction more info	PubMed
involved_in post-translational protein targeting to membrane, translocation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein processing	IDA Inferred from Direct Assay more info	PubMed
involved_in proteolysis	IEA Inferred from Electronic Annotation more info
involved_in response to pheromone	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
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 mitochondrial outer membrane	HDA more info	PubMed
located_in nuclear inner membrane	IMP Inferred from Mutant Phenotype more info	PubMed

General protein information

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Preferred Names: zinc metalloprotease

NP_012651.1

EC 3.4.24.84

Highly conserved zinc metalloprotease; component of the ER quality control mechanism that removes faulty proteins clogging translocation channels; inhibits SRP-independent translocation into the ER; has two roles in a-factor maturation, C-terminal CAAX proteolysis and the first step of N-terminal proteolytic processing; cleaves isoprenylated and non-prenylated oligopeptides; human homolog ZMPSTE24 implicated in mandibuloacral dysplasia (MAD), and complements the null mutant

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_001142.9 Reference assembly

Range

642007..643368

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001181775.1 → NP_012651.1 TPA: zinc metalloprotease [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012651.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VWT6, P47154

UniProtKB/TrEMBL

B5VLQ9, C7GM94, G2WHC0, N1P3N5

Conserved Domains (1) summary

cd07343
Location:17 → 446

M48A_Zmpste24p_like; Peptidase M48 subfamily A, a type 1 CaaX endopeptidase