CYM1 pitrilysin family metalloprotease [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: CYM1
Official Full Name: pitrilysin family metalloprotease
Primary source: SGD:S000002838
Locus tag: YDR430C
See related: AllianceGenome:SGD:S000002838; FungiDB:YDR430C; VEuPathDB:YDR430C
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: MOP112
Summary: Enables metalloendopeptidase activity. Involved in mitochondrial protein processing and proteolysis involved in protein catabolic process. Located in mitochondrial intermembrane space. Used to study Alzheimer's disease; hereditary ataxia; and primary cerebellar degeneration. Human ortholog(s) of this gene implicated in autosomal recessive spinocerebellar ataxia 30. Orthologous to human PITRM1 (pitrilysin metallopeptidase 1). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See CYM1 in Genome Data Viewer

Location:: chromosome: IV

Exon count:: 1

Sequence:: Chromosome: IV; NC_001136.10 (1325501..1328470, complement)

Chromosome IV - NC_001136.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001136.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Lack of Cym1 leads to accumulation of immature preproteins in vivo, reflecting the mas1 mutant phenotype with impaired presequence processing activity.
Title: Amyloid-β peptide induces mitochondrial dysfunction by inhibition of preprotein maturation.
Data show that the Cym1/Mop112 presequence has an overall much weaker targeting capacity and only ensures mitochondrial sorting in its host species yeast.
Title: Targeting capacity and conservation of PreP homologues localization in mitochondria of different species.
exerts important functions for the maintenance of the respiratory competence of the cells
Title: Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria.

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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 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	IMP Inferred from Mutant Phenotype more info	PubMed
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 mitochondrial protein processing	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein processing	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info
involved_in proteolysis involved in protein catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in mitochondrial intermembrane space	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial intermembrane space	IEA Inferred from Electronic Annotation more info
is_active_in mitochondrial matrix	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrial matrix	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: pitrilysin family metalloprotease

NP_010718.1

Lysine-specific metalloprotease of the pitrilysin family; metalloprotease of the intermembrane space; degrades proteins and presequence peptides cleaved from imported proteins; required for normal mitochondrial morphology; mutation in human homolog PITRM1 is implicated in autosomal recessive spinocerebellar ataxias (ARCA)

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_001136.10 Reference assembly

Range

1325501..1328470 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001180738.1 → NP_010718.1 TPA: pitrilysin family metalloprotease [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_010718.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VT59, P32898, Q04068

UniProtKB/TrEMBL

A6ZZ26, B3LFM7, G2WBG5, N1PAK0

Conserved Domains (1) summary

COG1026
Location:24 → 989

Cym1; Zn-dependent peptidase, M16 (insulinase) family [Posttranslational modification, protein turnover, chaperones]