Cathepsin H

CTSH
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1BZN
Identifiers
Aliases	CTSH, ACC-4, ACC-5, CPSB, minichain, ACC4, ACC5, cathepsin H
External IDs	MGI: 107285 HomoloGene: 36159 GeneCards: CTSH
Gene location (Human)
Chr.	Chromosome 15 (human)[1]
End	78,949,574 bp[1]
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)[2]
End	90,076,089 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• peptidase activator activity involved in apoptotic process; • cysteine-type peptidase activity; • HLA-A specific activating MHC class I receptor activity; • endopeptidase activity; • protein binding; • cysteine-type endopeptidase activator activity involved in apoptotic process; • cysteine-type endopeptidase activity; • aminopeptidase activity; • serine-type endopeptidase activity; • hydrolase activity; • thyroid hormone binding; • peptidase activity;
Cellular component	• cytosol; • alveolar lamellar body; • lysosome; • extracellular exosome; • multivesicular body lumen; • extracellular region; • extracellular space; • secretory granule lumen; • intracellular membrane-bounded organelle; • tertiary granule lumen; • ficolin-1-rich granule lumen; • cytoplasmic ribonucleoprotein granule;
Biological process	• surfactant homeostasis; • cellular protein metabolic process; • antigen processing and presentation; • adaptive immune response; • bradykinin catabolic process; • response to retinoic acid; • membrane protein proteolysis; • positive regulation of cell migration; • ERK1 and ERK2 cascade; • zymogen activation; • neuropeptide catabolic process; • positive regulation of epithelial cell migration; • positive regulation of apoptotic signaling pathway; • negative regulation of apoptotic process; • proteolysis; • positive regulation of angiogenesis; • positive regulation of peptidase activity; • positive regulation of gene expression; • protein destabilization; • cellular response to thyroid hormone stimulus; • positive regulation of cell proliferation; • immune response-regulating signaling pathway; • proteolysis involved in cellular protein catabolic process; • metanephros development; • dichotomous subdivision of terminal units involved in lung branching; • T cell mediated cytotoxicity; • apoptotic process; • activation of cysteine-type endopeptidase activity involved in apoptotic process; • neutrophil degranulation;
	Sources:Amigo / QuickGO
Orthologs
	1512
	13036
	ENSG00000103811
	ENSMUSG00000032359
	P09668
	P49935
	NM_004390; NM_148979; NM_001319137
	NM_007801; NM_001312649
	NP_001306066; NP_004381
	NP_001299578; NP_031827
	Wikidata
View/Edit Human	View/Edit Mouse

Cathepsin H is a protein that in humans is encoded by the CTSH gene.^[5]^[6]

The protein encoded by this gene is a lysosomal cysteine proteinase important in the overall degradation of lysosomal proteins. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. The encoded protein, which belongs to the peptidase C1 protein family, can act both as an aminopeptidase and as an endopeptidase. Increased expression of this gene has been correlated with malignant progression of prostate tumors. Two transcript variants encoding different isoforms have been found for this gene.^[6]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000103811 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032359 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Fuchs R, Machleidt W, Gassen HG (Feb 1989). "Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H". Biol Chem Hoppe-Seyler. 369 (6): 469–75. doi:10.1515/bchm3.1988.369.1.469. PMID 2849458.
1 2 "Entrez Gene: CTSH cathepsin H".

Sawicki G, Warwas M (1990). "Cathepsin H from human placenta". Acta Biochim. Pol. 36 (3–4): 343–51. PMID 2486008.
Fuchs R, Gassen HG (1990). "Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine proteinase". Nucleic Acids Res. 17 (22): 9471. doi:10.1093/nar/17.22.9471. PMC 335148. PMID 2587265.
Chernaia VI, Reva AD (1990). "[Cathepsin H activity in the human brain and human brain neoplasms]". Ukr. Biokhim. Zh. 61 (5): 47–50. PMID 2588347.
Ritonja A, Popović T, Kotnik M, et al. (1988). "Amino acid sequences of the human kidney cathepsins H and L.". FEBS Lett. 228 (2): 341–5. doi:10.1016/0014-5793(88)80028-0. PMID 3342889.
Järvinen M, Rinne A (1983). "Human spleen cysteineproteinase inhibitor. Purification, fractionation into isoelectric variants and some properties of the variants". Biochim. Biophys. Acta. 708 (2): 210–7. doi:10.1016/0167-4838(82)90222-9. PMID 6184075.
Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
Baumgrass R, Williamson MK, Price PA (1997). "Identification of peptide fragments generated by digestion of bovine and human osteocalcin with the lysosomal proteinases cathepsin B, D, L, H, and S.". J. Bone Miner. Res. 12 (3): 447–55. doi:10.1359/jbmr.1997.12.3.447. PMID 9076588.
Söderström M, Salminen H, Glumoff V, et al. (1999). "Cathepsin expression during skeletal development". Biochim. Biophys. Acta. 1446 (1–2): 35–46. doi:10.1016/S0167-4781(99)00068-8. PMID 10395917.
Jokimaa V, Oksjoki S, Kujari H, et al. (2001). "Expression patterns of cathepsins B, H, K, L and S in the human endometrium". Mol. Hum. Reprod. 7 (1): 73–8. doi:10.1093/molehr/7.1.73. PMID 11134363.
Uusitalo H, Hiltunen A, Söderström M, et al. (2001). "Expression of cathepsins B, H, K, L, and S and matrix metalloproteinases 9 and 13 during chondrocyte hypertrophy and endochondral ossification in mouse fracture callus". Calcif. Tissue Int. 67 (5): 382–90. doi:10.1007/s002230001152. PMID 11136537.
Pol E, Björk I (2001). "Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases". Protein Sci. 10 (9): 1729–38. doi:10.1110/ps.11901. PMC 2253190. PMID 11514663.
Waghray A, Keppler D, Sloane BF, et al. (2002). "Analysis of a truncated form of cathepsin H in human prostate tumor cells". J. Biol. Chem. 277 (13): 11533–8. doi:10.1074/jbc.M109557200. PMID 11796715.
Brasch F, Ten Brinke A, Johnen G, et al. (2002). "Involvement of cathepsin H in the processing of the hydrophobic surfactant-associated protein C in type II pneumocytes". Am. J. Respir. Cell Mol. Biol. 26 (6): 659–70. doi:10.1165/ajrcmb.26.6.4744. PMID 12034564.
Bühling F, Waldburg N, Krüger S, et al. (2003). "Expression of cathepsins B, H, K, L, and S during human fetal lung development". Dev. Dyn. 225 (1): 14–21. doi:10.1002/dvdy.10134. PMID 12203716.
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. PMC 139241. PMID 12477932.
Jenko S, Dolenc I, Guncar G, et al. (2003). "Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases". J. Mol. Biol. 326 (3): 875–85. doi:10.1016/S0022-2836(02)01432-8. PMID 12581647.
Nagai A, Terashima M, Harada T, et al. (2003). "Cathepsin B and H activities and cystatin C concentrations in cerebrospinal fluid from patients with leptomeningeal metastasis". Clin. Chim. Acta. 329 (1–2): 53–60. doi:10.1016/S0009-8981(03)00023-8. PMID 12589965.
Han SR, Momeni A, Strach K, et al. (2004). "Enzymatically modified LDL induces cathepsin H in human monocytes: potential relevance in early atherogenesis". Arterioscler. Thromb. Vasc. Biol. 23 (4): 661–7. doi:10.1161/01.ATV.0000063614.21233.BF. PMID 12615673.
Dodt J, Reichwein J (2004). "Human cathepsin H: deletion of the mini-chain switches substrate specificity from aminopeptidase to endopeptidase". Biol. Chem. 384 (9): 1327–32. doi:10.1515/BC.2003.149. PMID 14515996.

External links

The MEROPS online database for peptidases and their inhibitors: C01.040

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000103811 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032359 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid2849458-5] Fuchs R, Machleidt W, Gassen HG (Feb 1989). "Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H". Biol Chem Hoppe-Seyler. 369 (6): 469–75. doi:10.1515/bchm3.1988.369.1.469. PMID 2849458.

[entrez-6] 1 2 "Entrez Gene: CTSH cathepsin H".

Proteases: cysteine proteases (EC 3.4.22)
Caspase	Caspase 1 Caspase 2 Caspase 3 Caspase 4 Caspase 5 Caspase 6 Caspase 7 Caspase 8 Caspase 9 Caspase 10 Caspase 12 Caspase 13 Caspase 14
Fruit-derived	Papain Ficain Bromelain Actinidain
Calpain	CAPN1 CAPN2 CAPN3 CAPN5 CAPN6 CAPN7 CAPN8 CAPN9 CAPN10 CAPN11 CAPN12 CAPN13 CAPN14 CAPNS1 CAPNS2
Cathepsin	B C F H K L1/L2 O S W Z
Other	Clostripain Cancer procoagulant Separase Autophagin Cruzipain

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

Cathepsin H

References

Further reading

External links