Cathepsin E (CTSE)

The protein contains 401 amino acids for an estimated molecular weight of 43312 Da.

 

May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain. (updated: April 1, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  3. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 95%
Model score: 0

(right-click above to access to more options from the contextual menu)

VariantDescription
dbSNP:rs57621203
dbSNP:rs6503

The reference OMIM entry for this protein is 116890

Cathepsin e; ctse
Cate

DESCRIPTION

Cathepsin E, an endolysosomal aspartic proteinase predominantly expressed in cells of the immune system, has an important role in immune responses (Yanagawa et al., 2007).

CLONING

Taggart et al. (1989) used sets of complementary oligonucleotide probes specific for the highly conserved active site region of aspartic proteinases to isolate cDNA clones encoding novel enzymes of this class. They identified 6 classes of cDNA clones in a gastric adenocarcinoma cDNA library using a set of 18-mer probes. One of the cDNAs, designated AGS402, was shown by DNA analysis to correspond to the predicted coding sequence of cathepsin E. Couvreur et al. (1989, 1990) also isolated a full-length CTSE cDNA clone from a gastric adenocarcinoma cDNA library. Azuma et al. (1989, 1989) reported the amino acid sequence of CTSE predicted on the basis of the cDNA sequence and compared the sequence with that of other aspartic proteinases. Azuma et al. (1992) demonstrated that multiple transcripts result from alternative polyadenylation of the primary transcripts of the single CTSE gene.

GENE STRUCTURE

Azuma et al. (1992) determined that the CTSE gene contains 9 exons and spans 17.5 kb. The size and placement of the exons are highly conserved relative to other aspartic proteinases.

MAPPING

By somatic cell hybrid analysis, Taggart et al. (1989) mapped the CTSE gene to chromosome 1. Azuma et al. (1989, 1989) also assigned the CTSE gene to chromosome 1. Couvreur et al. (1989, 1990) mapped the CTSE gene to chromosome 1q23-qter by analysis of human/rodent hybrid cell lines containing different X;1 translocations. CTSE was further localized to chromosome 1q31 by in situ hybridization.

ANIMAL MODEL

Yanagawa et al. (2007) found that cathepsin E deficiency in mice resulted in a lysosome storage disorder in macrophages that was characterized by accumulation of major lysosomal membrane sialoglycoproteins, including Lamp1 (153330), Lamp2 (309060), and Limp2 (SCARB2; 602257), and elevated lysosomal pH. Trafficking of soluble lysosomal proteins to lysosomes was also partially impaired in Cate -/- macrophages. Treatment of wildtype macrophages with a cathepsin E inhibitor also led to accumulation of these lysosomal proteins and elevated pH. Since vacuolar-type H(+) ATPase (see 603097) activity was not altered in Cate -/- macrophages, Yanagawa et al. (2007) hypothesized that the elevated lysosomal pH in Cate -/- macrophages was likely due to the accumulation of the highly acidic lysosomal sialoglycoproteins. ... More on the omim web site

Subscribe to this protein entry history

May 12, 2019: Protein entry updated
Automatic update: model status changed

Nov. 17, 2018: Protein entry updated
Automatic update: model status changed

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

Oct. 26, 2017: Protein entry updated
Automatic update: model status changed

March 25, 2017: Additional information
No protein expression data in P. Mayeux work for CTSE

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 116890 was added.

Feb. 24, 2016: Protein entry updated
Automatic update: model status changed

Jan. 27, 2016: Protein entry updated
Automatic update: model status changed

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed