Thop1 thimet oligopeptidase 1 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Thop1provided by MGI
Official Full Name: thimet oligopeptidase 1provided by MGI
Primary source: MGI:MGI:1354165
See related: Ensembl:ENSMUSG00000004929 AllianceGenome:MGI:1354165
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: EP24.15
Summary: Enables metalloendopeptidase activity. Acts upstream of or within intracellular signal transduction and peptide metabolic process. Predicted to be located in cytoplasm. Predicted to be active in mitochondrial intermembrane space. Is expressed in head mesenchyme and vertebral axis musculature. Orthologous to human THOP1 (thimet oligopeptidase 1). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Broad expression in testis adult (RPKM 160.6), ovary adult (RPKM 53.8) and 24 other tissues See more
Orthologs: human all
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Genomic context

Location:: 10 C1; 10 39.72 cM

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	10	NC_000076.7 (80905917..80918194)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	10	NC_000076.6 (81070083..81082360)

Chromosome 10 - NC_000076.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The Relevance of Thimet Oligopeptidase in the Regulation of Energy Metabolism and Diet-Induced Obesity.
Title: The Relevance of Thimet Oligopeptidase in the Regulation of Energy Metabolism and Diet-Induced Obesity.
the cellular peptidases dipeptidyl peptidase 3 (DPP-3) and thimet oligopeptidase 1 (TOP-1), both of which are present in nonimmunogenic necrotic cells, eliminated proteasomal degradation products and blocked Ag cross-presentation
Title: Peptidases released by necrotic cells control CD8+ T cell cross-priming.
Data show that Thimet oligopeptidase (TOP) is coexpressed with estrogen receptor alpha, and estradiol regulates TOP expression in a brain region-specific manner in female mice.
Title: Nuclear Thimet oligopeptidase is coexpressed with oestrogen receptor alpha in hypothalamic cells and regulated by oestradiol in female mice.
increase in THOP1 expression might be part of a compensatory defense mechanism of the brain against an increased Abeta load.
Title: Increased expression of the oligopeptidase THOP1 is a neuroprotective response to Abeta toxicity.
Melanoma cells secrete thimet oligopeptidase which have an important role in tumor proliferation/angiogenesis in vitro and in vivo.
Title: Characterization of thimet oligopeptidase and neurolysin activities in B16F10-Nex2 tumor cells and their involvement in angiogenesis and tumor growth.
EP24.15 association with lipid rafts on the extracellular surface precedes constitutive release of the peptidase into the extracellular milieu for its action on neuropeptides
Title: Metalloendopeptidase EC3.4.24.15 is constitutively released from the exofacial leaflet of lipid rafts in GT1-7 cells.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (2)
Gene trapped (2)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

AI131655 (e-PCR)
- UniSTS:160009

UniSTS:236402 (e-PCR)
- UniSTS:236402

Gene Ontology Provided by MGI

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 peptidase activity	ISO Inferred from Sequence Orthology more info
enables peptide binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within intracellular signal transduction	IDA Inferred from Direct Assay more info	PubMed
involved_in peptide catabolic process	ISO Inferred from Sequence Orthology more info
involved_in peptide metabolic process	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within peptide metabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in proteolysis	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in mitochondrial intermembrane space	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: thimet oligopeptidase

Names: endopeptidase 24.15

NP_073144.3

EC 3.4.24.15

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_022653.4 → NP_073144.3 thimet oligopeptidase

See identical proteins and their annotated locations for NP_073144.3

Status: VALIDATED

Source sequence(s)

AK028609, BY774276, CF163503, CN723672

Consensus CDS

CCDS24042.1

UniProtKB/Swiss-Prot

Q8C1A5, Q8K0J9, Q8K2D4, Q9EPX1

UniProtKB/TrEMBL

A0A0R4IZY0

Related

ENSMUSP00000005057.7, ENSMUST00000005057.7

Conserved Domains (2) summary

cd06455
Location:35 → 675

M3A_TOP; Peptidase M3 Thimet oligopeptidase (TOP) also includes neurolysin

COG0339
Location:37 → 679

Dcp; Zn-dependent oligopeptidase [Posttranslational modification, protein turnover, chaperones]