PAM17 Pam17p [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: PAM17
Official Full Name: Pam17p
Primary source: SGD:S000001773
Locus tag: YKR065C
See related: AllianceGenome:SGD:S000001773; FungiDB:YKR065C; VEuPathDB:YKR065C
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: FMP18
Summary: Involved in protein import into mitochondrial matrix. Located in mitochondrion. Part of PAM complex, Tim23 associated import motor. [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See PAM17 in Genome Data Viewer

Location:: chromosome: XI

Exon count:: 1

Sequence:: Chromosome: XI; NC_001143.9 (565299..565892, complement)

Chromosome XI - NC_001143.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001143.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The presequence translocase constituent Pam17 is specifically recruited by the receptor Tim50 to promote the transport of hypersensitive precursors into the mitochondrial matrix.
Title: Two distinct membrane potential-dependent steps drive mitochondrial matrix protein translocation.
Tim23 mitochondrial motor components are tethered to translocon via the scaffold Tim44, with regulatory protein Pam17 having independent interaction site.
Title: Architecture of the TIM23 inner mitochondrial translocon and interactions with the matrix import motor.
The signal-driven release of Tim21 from Tim50 promotes recruitment of Pam17 and thus triggers formation of the motor-associated form of the TIM23 complex required for matrix transport.
Title: Signal recognition initiates reorganization of the presequence translocase during protein import.
Genetic and biochemical analyses reveal synthetic interactions between PAM17 and TIM44.
Title: Pam17 and Tim44 act sequentially in protein import into the mitochondrial matrix.
Tim44 is not simply a scaffold for binding of motor subunits but plays a differential role in the recruitment of PAM modules to the inner membrane translocase.
Title: Mitochondrial protein import motor: differential role of Tim44 in the recruitment of Pam17 and J-complex to the presequence translocase.
Pam17 is required for formation of a stable complex between the cochaperones Pam16 and Pam18
Title: Pam17 is required for architecture and translocation activity of the mitochondrial protein import motor.

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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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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables molecular_function	ND No biological Data available more info

Process	Evidence Code	Pubs
involved_in protein import into mitochondrial matrix	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein import into mitochondrial matrix	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 PAM complex, Tim23 associated import motor	IBA Inferred from Biological aspect of Ancestor more info
part_of PAM complex, Tim23 associated import motor	IDA Inferred from Direct Assay more info	PubMed
part_of PAM complex, Tim23 associated import motor	IEA Inferred from Electronic Annotation more info
located_in mitochondrial inner membrane	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: Pam17p

NP_012991.3

Constituent of the TIM23 complex; proposed alternatively to be a component of the import motor (PAM complex) or to interact with and modulate the core TIM23 (Translocase of the Inner mitochondrial Membrane) complex; protein abundance increases in response to DNA replication stress