CLPP

From Wikipedia, the free encyclopedia

ClpP caseinolytic peptidase, ATP-dependent, proteolytic subunit homolog (E. coli)

PDB rendering based on 1tg6.

Available structures: 1tg6

Identifiers

Symbol(s)

CLPP;

External IDs

OMIM: 601119 MGI: 1858213 HomoloGene: 4385

Gene ontology
Molecular Function:	• peptidase activity • endopeptidase Clp activity
Cellular Component:	• mitochondrion
Biological Process:	• proteolysis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006012 (mRNA)
NP_006003 (protein)

NM_017393 (mRNA)
NP_059089 (protein)

Location

Chr 19: 6.31 - 6.32 Mb

Chr 17: 56.68 - 56.68 Mb

Pubmed search

[1]

[2]

ClpP caseinolytic peptidase, ATP-dependent, proteolytic subunit homolog (E. coli), also known as CLPP, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: CLPP ClpP caseinolytic peptidase, ATP-dependent, proteolytic subunit homolog (E. coli).

[edit] Further reading

Kang SG, Dimitrova MN, Ortega J, et al. (2005). "Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX.". J. Biol. Chem. 280 (42): 35424-32. doi:10.1074/jbc.M507240200. PMID 16115876.
Kang SG, Maurizi MR, Thompson M, et al. (2005). "Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP.". J. Struct. Biol. 148 (3): 338-52. doi:10.1016/j.jsb.2004.07.004. PMID 15522782.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Kang SG, Ortega J, Singh SK, et al. (2002). "Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP.". J. Biol. Chem. 277 (23): 21095-102. doi:10.1074/jbc.M201642200. PMID 11923310.
de Sagarra MR, Mayo I, Marco S, et al. (1999). "Mitochondrial localization and oligomeric structure of HClpP, the human homologue of E. coli ClpP.". J. Mol. Biol. 292 (4): 819-25. doi:10.1006/jmbi.1999.3121. PMID 10525407.
Corydon TJ, Bross P, Holst HU, et al. (1998). "A human homologue of Escherichia coli ClpP caseinolytic protease: recombinant expression, intracellular processing and subcellular localization.". Biochem. J. 331 ( Pt 1): 309-16. PMID 9512494.
Bross P, Andresen BS, Knudsen I, et al. (1996). "Human ClpP protease: cDNA sequence, tissue-specific expression and chromosomal assignment of the gene.". FEBS Lett. 377 (2): 249-52. PMID 8543061.