PAM18 Pam18p [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: PAM18
Official Full Name: Pam18p
Primary source: SGD:S000003998
Locus tag: YLR008C
See related: AllianceGenome:SGD:S000003998; FungiDB:YLR008C; VEuPathDB:YLR008C
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: TIM14
Summary: Enables ATPase activator activity. Involved in protein import into mitochondrial matrix. Located in mitochondrion. Part of PAM complex, Tim23 associated import motor. Human ortholog(s) of this gene implicated in 3-methylglutaconic aciduria type 5. Orthologous to human DNAJC15 (DnaJ heat shock protein family (Hsp40) member C15) and DNAJC19 (DnaJ heat shock protein family (Hsp40) member C19). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See PAM18 in Genome Data Viewer

Location:: chromosome: XII

Exon count:: 1

Sequence:: Chromosome: XII; NC_001144.5 (165577..166083, complement)

Chromosome XII - NC_001144.5 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001144.5

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Coupling to Pam16 differentially controls the dual role of Pam18 in protein import and respiratory chain formation.
Title: Coupling to Pam16 differentially controls the dual role of Pam18 in protein import and respiratory chain formation.
prevents lateral precursor transport from the TIM23 mitochondrial inner membrane translocase and thus traps polypeptide in a translocase-spanning manner
Title: Motor recruitment to the TIM23 channel's lateral gate restricts polypeptide release into the inner membrane.
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.
These data suggest a model in which Tim44 serves as a scaffold for precise positioning of mtHsp70 and its cochaperone Pam18 at the translocon.
Title: Interaction of the J-protein heterodimer Pam18/Pam16 of the mitochondrial import motor with the translocon of the inner membrane.
binding of Tim44 to mHsp70 prevents the formation of a complex between the latter and Tim14/Pam18-Tim16/Pam16.
Title: The interplay between components of the mitochondrial protein translocation motor studied using purified components.
import into the matrix space of mitochondria requires association of the co-chaperones Tim16 and Tim14 with the TIM23 preprotein translocase
Title: Association of the Tim14.Tim16 subcomplex with the TIM23 translocase is crucial for function of the mitochondrial protein import motor.
PAM18 stimulates the ATPase activity of mtHsp70 and thereby enables efficient binding of mtHsp70 to preproteins.
Title: The import motor of the yeast mitochondrial TIM23 preprotein translocase contains two different J proteins, Tim14 and Mdj2.
Tim14 forms a complex with the J-like protein Tim16. The crystal structure of this complex shows that the conserved domains of the two proteins have virtually identical folds but completely different surfaces enabling them to perform different functions.
Title: Structure and function of Tim14 and Tim16, the J and J-like components 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 ATPase activator activity	IBA Inferred from Biological aspect of Ancestor more info
enables ATPase activator activity	IDA Inferred from Direct Assay more info	PubMed
enables ATPase activator activity	IMP Inferred from Mutant Phenotype more info	PubMed

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 TIM23 mitochondrial import inner membrane translocase complex	IDA Inferred from Direct Assay more info	PubMed
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: Pam18p

NP_013108.1

Subunit of the import motor (PAM complex); the PAM complex is a component of the Translocase of the Inner Mitochondrial membrane (TIM23 complex); essential J-protein cochaperone that stimulates Ssc1p ATPase activity to drive import; inhibited by Pam16p

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_001144.5 Reference assembly

Range

165577..166083 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001181895.1 → NP_013108.1 TPA: Pam18p [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_013108.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VY10, Q07914

UniProtKB/TrEMBL

A7A0R3, B3LSY1, B5VMV0, C8ZCY0, G2WIK2, N1P014

Conserved Domains (1) summary

cl02542
Location:103 → 163

DnaJ; DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, ...