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Cathepsin D

NameCathepsin D
Synonyms
  • 3.4.23.5
  • CPSD
Gene NameCTSD
OrganismHuman
Amino acid sequence
>lcl|BSEQ0016260|Cathepsin D
MQPSSLLPLALCLLAAPASALVRIPLHKFTSIRRTMSEVGGSVEDLIAKGPVSKYSQAVP
AVTEGPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIH
HKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCQSASSASALGGVKVERQVFG
EATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDPDAQ
PGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSL
MVGPVDEVRELQKAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQ
AGKTLCLSGFMGMDIPPPSGPLWILGDVFIGRYYTVFDRDNNRVGFAEAARL
Number of residues412
Molecular Weight44551.845
Theoretical pI6.5
GO Classification
Functions
  • aspartic-type endopeptidase activity
Processes
  • collagen catabolic process
  • extracellular matrix disassembly
  • extracellular matrix organization
  • antigen processing and presentation of exogenous peptide antigen via MHC class II
  • protein catabolic process
  • proteolysis
  • autophagy
Components
  • membrane raft
  • lysosomal lumen
  • melanosome
  • extracellular region
  • extracellular space
  • lysosome
  • extracellular exosome
General FunctionAspartic-type endopeptidase activity
Specific FunctionAcid protease active in intracellular protein breakdown. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID181180
UniProtKB IDP07339
UniProtKB Entry NameCATD_HUMAN
Cellular LocationLysosome
Gene sequence
>lcl|BSEQ0016261|Cathepsin D (CTSD)
ATGCAGCCCTCCAGCCTTCTGCCGCTCGCCCTCTGCCTGCTGGCTGCACCCGCCTCCGCG
CTCGTCAGGATCCCGCTGCACAAGTTCACGTCCATCCGCCGGACCATGTCGGAGGTTGGG
GGCTCTGTGGAGGACCTGATTGCCAAAGGCCCCGTCTCAAAGTACTCCCAGGCGGTGCCA
GCCGTGACCGAGGGGCCCATTCCCGAGGTGCTCAAGAACTACATGGACGCCCAGTACTAC
GGGGAGATTGGCATCGGGACGCCCCCCCAGTGCTTCACAGTCGTCTTCGACACGGGCTCC
TCCAACCTGTGGGTCCCCTCCATCCACTGCAAACTGCTGGACATCGCTTGCTGGATCCAC
CACAAGTACAACAGCGACAAGTCCAGCACCTACGTGAAGAATGGTACCTCGTTTGACATC
CACTATGGCTCGGGCAGCCTCTCCGGGTACCTGAGCCAGGACACTGTGTCGGTGCCCTGC
CAGTCAGCGTCGTCAGCCTCTGCCCTGGGCGGTGTCAAAGTGGAGAGGCAGGTCTTTGGG
GAGGCCACCAAGCAGCCAGGCATCACCTTCATCGCAGCCAAGTTCGATGGCATCCTGGGC
ATGGCCTACCCCCGCATCTCCGTCAACAACGTGCTGCCCGTCTTCGACAACCTGATGCAG
CAGAAGCTGGTGGACCAGAACATCTTCTCCTTCTACCTGAGCAGGGACCCAGATGCGCAG
CCTGGGGGTGAGCTGATGCTGGGTGGCACAGACTCCAAGTATTACAAGGGTTCTCTGTCC
TACCTGAATGTCACCCGCAAGGCCTACTGGCAGGTCCACCTGGACCAGGTGGAGGTGGCC
AGCGGGCTGACCCTGTGCAAGGAGGGCTGTGAGGCCATTGTGGACACAGGCACTTCCCTC
ATGGTGGGCCCGGTGGATGAGGTGCGCGAGCTGCAGAAGGCCATCGGGGCCGTGCCGCTG
ATTCAGGGCGAGTACATGATCCCCTGTGAGAAGGTGTCCACCCTGCCCGCGATCACACTG
AAGCTGGGAGGCAAAGGCTACAAGCTGTCCCCAGAGGACTACACGCTCAAGGTGTCGCAG
GCCGGGAAGACCCTCTGCCTGAGCGGCTTCATGGGCATGGACATCCCGCCACCCAGCGGG
CCACTCTGGATCCTGGGCGACGTCTTCATCGGCCGCTACTACACTGTGTTTGACCGTGAC
AACAACAGGGTGGGCTTCGCCGAGGCTGCCCGCCTCTAG
GenBank Gene IDM11233
GeneCard IDNot Available
GenAtlas IDCTSD
HGNC IDHGNC:2529
Chromosome Location11
Locus11p15.5
References
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  2. Westley BR, May FE: Oestrogen regulates cathepsin D mRNA levels in oestrogen responsive human breast cancer cells. Nucleic Acids Res. 1987 May 11;15(9):3773-86. 3588310
  3. Redecker B, Heckendorf B, Grosch HW, Mersmann G, Hasilik A: Molecular organization of the human cathepsin D gene. DNA Cell Biol. 1991 Jul-Aug;10(6):423-31. 2069717
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  5. May FE, Smith DJ, Westley BR: The human cathepsin D-encoding gene is transcribed from an estrogen-regulated and a constitutive start point. Gene. 1993 Dec 8;134(2):277-82. 8262386
  6. Augereau P, Miralles F, Cavailles V, Gaudelet C, Parker M, Rochefort H: Characterization of the proximal estrogen-responsive element of human cathepsin D gene. Mol Endocrinol. 1994 Jun;8(6):693-703. 7935485
  7. Basrur V, Yang F, Kushimoto T, Higashimoto Y, Yasumoto K, Valencia J, Muller J, Vieira WD, Watabe H, Shabanowitz J, Hearing VJ, Hunt DF, Appella E: Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. J Proteome Res. 2003 Jan-Feb;2(1):69-79. 12643545
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  10. Siintola E, Partanen S, Stromme P, Haapanen A, Haltia M, Maehlen J, Lehesjoki AE, Tyynela J: Cathepsin D deficiency underlies congenital human neuronal ceroid-lipofuscinosis. Brain. 2006 Jun;129(Pt 6):1438-45. Epub 2006 May 2. 16670177
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  13. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. 19159218
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  16. Halim A, Ruetschi U, Larson G, Nilsson J: LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins. J Proteome Res. 2013 Feb 1;12(2):573-84. doi: 10.1021/pr300963h. Epub 2013 Jan 11. 23234360
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  18. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. 25944712
  19. Metcalf P, Fusek M: Two crystal structures for cathepsin D: the lysosomal targeting signal and active site. EMBO J. 1993 Apr;12(4):1293-302. 8467789
  20. Baldwin ET, Bhat TN, Gulnik S, Hosur MV, Sowder RC 2nd, Cachau RE, Collins J, Silva AM, Erickson JW: 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. 1993 Jul 15;90(14):6796-800. 8393577
  21. Papassotiropoulos A, Bagli M, Kurz A, Kornhuber J, Forstl H, Maier W, Pauls J, Lautenschlager N, Heun R: A genetic variation of cathepsin D is a major risk factor for Alzheimer's disease. Ann Neurol. 2000 Mar;47(3):399-403. 10716266
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