PRD1 metalloendopeptidase [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: PRD1
Official Full Name: metalloendopeptidase
Primary source: SGD:S000000562
Locus tag: YCL057W
See related: AllianceGenome:SGD:S000000562; FungiDB:YCL057W; VEuPathDB:YCL057W
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 metalloendopeptidase activity. Involved in proteolysis. Located in Golgi apparatus; fungal-type vacuole; and mitochondrial intermembrane space. Orthologous to several human genes including NLN (neurolysin). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See PRD1 in Genome Data Viewer

Location:: chromosome: III

Exon count:: 1

Sequence:: Chromosome: III; NC_001135.5 (24768..26906)

Chromosome III - NC_001135.5 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001135.5

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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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	IEA Inferred from Electronic Annotation more info
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 peptide metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis	IDA Inferred from Direct Assay more info	PubMed
involved_in proteolysis	IEA Inferred from Electronic Annotation more info
involved_in proteolysis	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in Golgi apparatus	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in fungal-type vacuole	IDA Inferred from Direct Assay more info	PubMed
is_active_in mitochondrial intermembrane space	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrial intermembrane space	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	HDA more info	PubMed

General protein information

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Preferred Names: metalloendopeptidase

NP_009874.1

EC 3.4.24.37

Zinc metalloendopeptidase; found in the cytoplasm and intermembrane space of mitochondria; with Cym1p, involved in degradation of mitochondrial proteins and of presequence peptides cleaved from imported proteins; protein abundance increases in response to DNA replication stress

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_001135.5 Reference assembly

Range

24768..26906

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178701.1 → NP_009874.1 TPA: metalloendopeptidase [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_009874.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VQW0, E9P942, P25375

UniProtKB/TrEMBL

A6ZTD8, B3LU28

Conserved Domains (1) summary

cd06455
Location:54 → 708

M3A_TOP; Peptidase M3 thimet oligopeptidase (TOP), also includes neurolysin