CLPP caseinolytic mitochondrial matrix peptidase proteolytic subunit [Homo sapiens (human)] - Gene

Summary

Official Symbol: CLPPprovided by HGNC
Official Full Name: caseinolytic mitochondrial matrix peptidase proteolytic subunitprovided by HGNC
Primary source: HGNC:HGNC:2084
See related: Ensembl:ENSG00000125656 MIM:601119; AllianceGenome:HGNC:2084
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: DFNB81; PRLTS3
Summary: The protein encoded by this gene belongs to the peptidase family S14 and hydrolyzes proteins into small peptides in the presence of ATP and magnesium. The protein is transported into mitochondrial matrix and is associated with the inner mitochondrial membrane. [provided by RefSeq, Jul 2008]
Expression: Ubiquitous expression in kidney (RPKM 19.9), fat (RPKM 18.0) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 19p13.3

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	19	NC_000019.10 (6361531..6370242)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	19	NC_060943.1 (6350432..6359144)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	19	NC_000019.9 (6361542..6370253)

Chromosome 19 - NC_000019.10 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: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

HSPA8-mediated stability of the CLPP protein regulates mitochondrial autophagy in cisplatin-resistant ovarian cancer cells.
Title: HSPA8-mediated stability of the CLPP protein regulates mitochondrial autophagy in cisplatin-resistant ovarian cancer cells.
Selective activator of human ClpP triggers cell cycle arrest to inhibit lung squamous cell carcinoma.
Title: Selective activator of human ClpP triggers cell cycle arrest to inhibit lung squamous cell carcinoma.
Aberrant human ClpP activation disturbs mitochondrial proteome homeostasis to suppress pancreatic ductal adenocarcinoma.
Title: Aberrant human ClpP activation disturbs mitochondrial proteome homeostasis to suppress pancreatic ductal adenocarcinoma.
CLPP deficiency ameliorates neurodegeneration caused by impaired mitochondrial protein synthesis.
Title: CLPP deficiency ameliorates neurodegeneration caused by impaired mitochondrial protein synthesis.
Substrate Profiling of Mitochondrial Caseinolytic Protease P via a Site-Specific Photocrosslinking Approach.
Title: Substrate Profiling of Mitochondrial Caseinolytic Protease P via a Site-Specific Photocrosslinking Approach.
Inactivity of Peptidase ClpP Causes Primary Accumulation of Mitochondrial Disaggregase ClpX with Its Interacting Nucleoid Proteins, and of mtDNA.
Title: Inactivity of Peptidase ClpP Causes Primary Accumulation of Mitochondrial Disaggregase ClpX with Its Interacting Nucleoid Proteins, and of mtDNA.
Mitochondrial Caseinolytic Protease P: A Possible Novel Prognostic Marker and Therapeutic Target in Cancer.
Title: Mitochondrial Caseinolytic Protease P: A Possible Novel Prognostic Marker and Therapeutic Target in Cancer.
Loss of mitochondrial ClpP, Lonp1, and Tfam triggers transcriptional induction of Rnf213, a susceptibility factor for moyamoya disease.
Title: Loss of mitochondrial ClpP, Lonp1, and Tfam triggers transcriptional induction of Rnf213, a susceptibility factor for moyamoya disease.
Genomic sequencing highlights the diverse molecular causes of Perrault syndrome: a peroxisomal disorder (PEX6), metabolic disorders (CLPP, GGPS1), and mtDNA maintenance/translation disorders (LARS2, TFAM).
Title: Genomic sequencing highlights the diverse molecular causes of Perrault syndrome: a peroxisomal disorder (PEX6), metabolic disorders (CLPP, GGPS1), and mtDNA maintenance/translation disorders (LARS2, TFAM).
ClpP is selectively decreased in alphaSyn-expressing cell culture and neurons derived from iPS cells of PD patient carrying alphaSyn A53T mutant, and in dopaminergic neurons of alphaSyn A53T mice and PD patient postmortem brains. ClpP loss damages mitochondria. Overexpression causes oxidative stress and suppresses alphaSyn phosphorylation. alphaSyn WT and A53T mutant interact with ClpP and suppress its peptidase activity.
Title: Alpha-synuclein suppresses mitochondrial protease ClpP to trigger mitochondrial oxidative damage and neurotoxicity.

Submit: New GeneRIF Correction See all GeneRIFs (25)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Associated conditions

Description	Tests
Perrault syndrome 3 MedGen: C3808414 OMIM: 614129 GeneReviews: Perrault Syndrome	Compare labs

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables ATP-dependent peptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables ATP-dependent peptidase activity	TAS Traceable Author Statement more info
enables ATPase binding	IBA Inferred from Biological aspect of Ancestor more info
enables endopeptidase activity	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IEA Inferred from Electronic Annotation more info
enables peptidase activity	TAS Traceable Author Statement more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables serine-type endopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables serine-type endopeptidase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in membrane protein proteolysis	IDA Inferred from Direct Assay more info	PubMed
involved_in mitochondrial protein catabolic process	TAS Traceable Author Statement more info
involved_in protein quality control for misfolded or incompletely synthesized proteins	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis	IDA Inferred from Direct Assay more info	PubMed
involved_in proteolysis involved in protein catabolic process	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
part_of endopeptidase Clp complex	IBA Inferred from Biological aspect of Ancestor more info
part_of endopeptidase Clp complex	IDA Inferred from Direct Assay more info	PubMed
part_of endopeptidase Clp complex	IPI Inferred from Physical Interaction more info	PubMed
located_in mitochondrial matrix	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial matrix	NAS Non-traceable Author Statement more info	PubMed
located_in mitochondrial matrix	TAS Traceable Author Statement more info
located_in mitochondrion	HTP more info	PubMed
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: ATP-dependent Clp protease proteolytic subunit, mitochondrial

Names: ATP-dependent protease ClpAP, proteolytic subunit, human; ClpP caseinolytic peptidase ATP-dependent, proteolytic subunit; ClpP caseinolytic peptidase, ATP-dependent, proteolytic subunit homolog; ClpP caseinolytic protease, ATP-dependent, proteolytic subunit homolog; endopeptidase Clp; putative ATP-dependent Clp protease proteolytic subunit, mitochondrial

NP_006003.1

EC 3.4.21.92

XP_047295442.1

EC 3.4.21.92

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.

Genomic

NG_033887.1 RefSeqGene

Range

5080..13791

Download

GenBank, FASTA, Sequence Viewer (Graphics), LRG_1402

mRNA and Protein(s)

NM_006012.4 → NP_006003.1 ATP-dependent Clp protease proteolytic subunit, mitochondrial precursor

See identical proteins and their annotated locations for NP_006003.1

Status: REVIEWED

Source sequence(s)

AC011491, BC002956

Consensus CDS

CCDS12162.1

UniProtKB/Swiss-Prot

B2R4W5, Q16740

Related

ENSP00000245816.3, ENST00000245816.11

Conserved Domains (1) summary

PRK00277
Location:55 → 249

clpP; ATP-dependent Clp protease proteolytic subunit; Reviewed