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MT000649

UniProt Annotations

Entry Information

Gene Name	caseinolytic mitochondrial matrix peptidase proteolytic subunit
Protein Entry	CLPP_HUMAN
UniProt ID	Q16740
Species	Human

Comments

Comment type	Description
Catalytic Activity	Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-\|-NHMec; and Leu-Tyr-Leu-\|-Tyr-Trp, in which cleavage of the -Tyr-\|-Leu- and -Tyr-\|-Trp bonds also occurs). {ECO:0000269\|PubMed:11923310, ECO:0000269\|PubMed:15522782}.
Disease	Perrault syndrome 3 (PRLTS3) [MIM:614129]: A sex- influenced disorder characterized by sensorineural deafness in both males and females, and ovarian dysgenesis in females. Affected females have primary amenorrhea, streak gonads, and infertility, whereas affected males show normal pubertal development and are fertile. A spectrum of additional clinical features, including cerebellar ataxia, learning disability, and peripheral neuropathy, have been described in some PRLTS3 affected individuals. {ECO:0000269\|PubMed:23541340}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Function	Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. {ECO:0000269\|PubMed:11923310, ECO:0000269\|PubMed:15522782}.
Similarity	Belongs to the peptidase S14 family. {ECO:0000305}.
Subcellular Location	Mitochondrion matrix {ECO:0000269\|PubMed:10525407}.
Subunit	Fourteen CLPP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity. Component of the Clp complex formed by the assembly of two CLPP heptameric rings with two CLPX hexameric rings, giving rise to a symmetrical structure with two central CLPP rings flanked by a CLPX ring at either end of the complex. {ECO:0000269\|PubMed:10525407, ECO:0000269\|PubMed:11923310, ECO:0000269\|PubMed:15522782, ECO:0000269\|PubMed:16115876}.
Tissue Specificity	Detected in liver (at protein level). Predominantly expressed in skeletal muscle. Intermediate levels in heart, liver and pancreas. Low in brain, placenta, lung and kidney. {ECO:0000269\|PubMed:10525407, ECO:0000269\|PubMed:8543061}.