TIM9 protein transporter TIM9 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: TIM9
Official Full Name: protein transporter TIM9
Primary source: SGD:S000007256
Locus tag: YEL020W-A
See related: AllianceGenome:SGD:S000007256; FungiDB:YEL020W-A; VEuPathDB:YEL020W-A
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables protein transporter activity and unfolded protein binding activity. Involved in protein insertion into mitochondrial inner membrane. Located in mitochondrion. Part of TIM22 mitochondrial import inner membrane insertion complex and mitochondrial intermembrane space protein transporter complex. Orthologous to human TIMM9 (translocase of inner mitochondrial membrane 9). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See TIM9 in Genome Data Viewer

Location:: chromosome: V

Exon count:: 1

Sequence:: Chromosome: V; NC_001137.3 (117211..117474)

Chromosome V - NC_001137.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001137.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The primary function of Tim9 is to protect Tim10 from degradation by Yme1 via assembly into the Tim9-Tim10 complex.
Title: Mitochondrial Tim9 protects Tim10 from degradation by the protease Yme1.
No individual cysteine residue is required for the function of Tim9 or Tim10 in yeast and defective assembly of the small TIMs induces their proteolytic clearance from mitochondria via the mitochondrial ATP-dependent protease, Yme1.
Title: Impaired folding of the mitochondrial small TIM chaperones induces clearance by the i-AAA protease.
A region within the Tim9 and Tim10 precursors, consisting of only nine amino acid residues, functions as a signal for the engagement of substrate proteins with the Mia40 receptor.
Title: Identification of the signal directing Tim9 and Tim10 into the intermembrane space of mitochondria.
zinc is a powerful inhibitor of Erv1, an essential component of the import pathway used by the small Tim9,10 proteins
Title: Zinc can play chaperone-like and inhibitor roles during import of mitochondrial small Tim proteins.
The structure of the yeast Tim9-Tim10 hexameric assembly determined to 2.5 A is reported and mutational analysis was performed to evaluate the specific roles of Tim9 and Tim10.
Title: Structural and functional requirements for activity of the Tim9-Tim10 complex in mitochondrial protein import.
Data show that assembly of the three small Tim proteins, Tim9, -10, and -12, precedes docking to the mitochondrial carrier translocase.
Title: Assembly of the three small Tim proteins precedes docking to the mitochondrial carrier translocase.
Results show that oxidative folding of Tims 9 and 10 is mediated by site-specific docking onto Mia40 in the mitochondrial intermembrane space.
Title: Oxidative folding of small Tims is mediated by site-specific docking onto Mia40 in the mitochondrial intermembrane space.
oxidative folding and mitochondrial import are kinetically competitive processes; efficiency of mitochondrial import of the small Tim proteins is controlled, at least partially in vitro, by the rate of oxidative folding
Title: Oxidative folding competes with mitochondrial import of the small Tim proteins.
Assembly of the mitochondrial TIM9-TIM10 complex: a multi-step reaction with novel intermediates.
Title: Assembly of the mitochondrial Tim9-Tim10 complex: a multi-step reaction with novel intermediates.
Mia40 acts as a trans receptor in the biogenesis of the Tim9-Tim10 chaperone complex of mitochondria
Title: Biogenesis of the essential Tim9-Tim10 chaperone complex of mitochondria: site-specific recognition of cysteine residues by the intermembrane space receptor Mia40.

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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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Markers

D17S1248 (e-PCR)
- UniSTS:149861

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 protein transporter activity	IDA Inferred from Direct Assay more info	PubMed
enables protein transporter activity	IGI Inferred from Genetic Interaction more info	PubMed
enables unfolded protein binding	IDA Inferred from Direct Assay more info	PubMed
enables zinc ion binding	RCA inferred from Reviewed Computational Analysis more info	PubMed

Process	Evidence Code	Pubs
involved_in protein insertion into mitochondrial inner membrane	IDA Inferred from Direct Assay more info	PubMed
involved_in protein insertion into mitochondrial inner membrane	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein insertion into mitochondrial inner membrane	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein transport	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of TIM22 mitochondrial import inner membrane insertion complex	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial inner membrane	IEA Inferred from Electronic Annotation more info
located_in mitochondrial intermembrane space	IEA Inferred from Electronic Annotation more info
part_of mitochondrial intermembrane space protein transporter complex	IDA Inferred from Direct Assay more info	PubMed
part_of mitochondrial intermembrane space protein transporter complex	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: protein transporter TIM9

NP_010894.1

Essential protein of the mitochondrial intermembrane space; forms a complex with Tim10p (TIM10 complex) that delivers hydrophobic proteins to the TIM22 complex for insertion into the inner membrane