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Cathepsin D [Homo sapiens]

Names and Origin

Protein names

Official name:

Cathepsin D

Cleaved into the following chains:

  • Cathepsin D light chain
  • Cathepsin D heavy chain

Genes CTSD [EntrezGene:1509]

Homo sapiens

Taxonomy Eukaryota > Opisthokonta > Metazoa > Eumetazoa > Bilateria > Deuterostomia > Chordata > Craniata > Vertebrata > Gnathostomata > Teleostomi > Euteleostomi > Sarcopterygii > Dipnotetrapodomorpha > Tetrapoda > Amniota > Mammalia > Theria > Eutheria > Boreoeutheria > Euarchontoglires > Primates > Haplorrhini > Simiiformes > Catarrhini > Hominoidea > Hominidae > Homininae > Homo

Sequence Attributes

Identifier Name Aliases Sequence length Molecular mass Sequence
P07339-1 Canonical sequence 412412 44551.844,551.8 HSPW:PD2FD56/1




There are currently no glycans associated with the protein.


Abundance and localization of gene products based on both RNA and immunohistochemistry data from the Human Protein Atlas. Click on the tissue names to view primary data.


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3D Structures

1LYAX-ray2.50 AA/C
1LYBX-ray2.50 AA/C
1LYWX-ray2.50 AA/C/E/G
4OBZX-ray2.90 AA/C
4OC6X-ray2.64 AA
4OD9X-ray1.90 AA/C

Cross References

RefSeq NP_001900.1; NM_001909.4
PDB 1LYA; 1LYB; 1LYW; 4OBZ; 4OC6; 4OD9
PeptideAtlas P07339
Ensembl ENST00000236671.7; ENSP00000236671.2; ENSG00000117984.15
GeneCards CTSD


3D-structure, Alzheimer disease, Aspartyl protease, Direct protein sequencing, Disease variant, Disulfide bond, Glycoprotein, Hydrolase, Lysosome, Neurodegeneration, Neuronal ceroid lipofuscinosis, Protease, Reference proteome, Secreted, Signal, Zymogen


1.Faust PL, et al. (1985) Cloning and sequence analysis of cDNA for human cathepsin D. Proc. Natl. Acad. Sci. U.S.A. 82(15):4910-4 [PubMed:3927292]
2.Westley BR and May FE (1987) Oestrogen regulates cathepsin D mRNA levels in oestrogen responsive human breast cancer cells. Nucleic Acids Res. 15(9):3773-86 [PubMed:3588310]
3.Redecker B, et al. Molecular organization of the human cathepsin D gene. DNA Cell Biol. 10(6):423-31 [PubMed:2069717]
4.Gerhard DS, 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 [PubMed:15489334]
5.May FE, et al. (1993) The human cathepsin D-encoding gene is transcribed from an estrogen-regulated and a constitutive start point. Gene 134(2):277-82 [PubMed:8262386]
6.Augereau P, et al. (1994) Characterization of the proximal estrogen-responsive element of human cathepsin D gene. Mol. Endocrinol. 8(6):693-703 [PubMed:7935485]
7.Kobayashi T, et al. (1992) Proteolytic processing sites producing the mature form of human cathepsin D. Int. J. Biochem. 24(9):1487-91 [PubMed:1426530]
8.Basrur V, et al. Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. J. Proteome Res. 2(1):69-79 [PubMed:12643545]
9.Zhang H, et al. (2003) Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat. Biotechnol. 21(6):660-6 [PubMed:12754519]
10.Liu T, et al. Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J. Proteome Res. 4(6):2070-80 [PubMed:16335952]
11.Siintola E, et al. (2006) Cathepsin D deficiency underlies congenital human neuronal ceroid-lipofuscinosis. Brain 129(Pt 6):1438-45 [PubMed:16670177]
12.Chi A, et al. (2006) Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J. Proteome Res. 5(11):3135-44 [PubMed:17081065]
13.Lewandrowski U, et al. (2006) Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. Mol. Cell Proteomics 5(2):226-33 [PubMed:16263699]
14.Chen R, et al. (2009) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J. Proteome Res. 8(2):651-61 [PubMed:19159218]
15.Didangelos A, et al. (2010) Proteomics characterization of extracellular space components in the human aorta. Mol. Cell Proteomics 9(9):2048-62 [PubMed:20551380]
16.Burkard TR, et al. (2011) Initial characterization of the human central proteome. BMC Syst Biol 5:17 [PubMed:21269460]
17.Halim A, et al. (2013) LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins. J. Proteome Res. 12(2):573-84 [PubMed:23234360]
18.Vaca Jacome AS, et al. (2015) N-terminome analysis of the human mitochondrial proteome. Proteomics 15(14):2519-24. doi:10.1002/pmic.201400617 [PubMed:25944712]
19.Letronne F, et al. (2016) ADAM30 Downregulates APP-Linked Defects Through Cathepsin D Activation in Alzheimer's Disease. EBioMedicine 9:278-92. doi:10.1016/j.ebiom.2016.06.002 [PubMed:27333034]
20.Metcalf P and Fusek M (1993) Two crystal structures for cathepsin D: the lysosomal targeting signal and active site. EMBO J. 12(4):1293-302 [PubMed:8467789]
21.Baldwin ET, et al. (1993) Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design. Proc. Natl. Acad. Sci. U.S.A. 90(14):6796-800 [PubMed:8393577]
22.Papassotiropoulos A, et al. (2000) A genetic variation of cathepsin D is a major risk factor for Alzheimer's disease. Ann. Neurol. 47(3):399-403 [PubMed:10716266]
23.Steinfeld R, et al. (2006) Cathepsin D deficiency is associated with a human neurodegenerative disorder. Am. J. Hum. Genet. 78(6):988-98 [PubMed:16685649]
24.Kousi M, et al. (2012) Update of the mutation spectrum and clinical correlations of over 360 mutations in eight genes that underlie the neuronal ceroid lipofuscinoses. Hum. Mutat. 33(1):42-63 [PubMed:21990111]
25.Hu S, et al. (2010) Preclinical validation of salivary biomarkers for primary Sjögren's syndrome. Arthritis Care Res (Hoboken) 62(11):1633-8 [PubMed:20617533]
26.Schwenk JM, et al. (2017) The Human Plasma Proteome Draft of 2017: Building on the Human Plasma PeptideAtlas from Mass Spectrometry and Complementary Assays. J. Proteome Res. 16(12):4299-4310. doi:10.1021/acs.jproteome.7b00467 [PubMed:28938075]

Entry Information

Entry name CATD_HUMAN
Accession Primary accession number: P07339

Secondary accession number(s): Q6IB57

Dataset Swiss-Prot
Created on 1988-04-01
Last modified on 2023-11-08
Link UniProt
HSPW Version 1.5.3. This page was last modified on 23 November 2023, at 05:45.This page has been accessed 1,354 times.