Cathepsin B


NameCathepsin B
Synonyms3.4.22.1 APP secretase APPS Cathepsin B1 CPSB
Gene NameCTSB
OrganismHuman
Amino acid sequence
>lcl|BSEQ0019038|Cathepsin B
MWQLWASLCCLLVLANARSRPSFHPLSDELVNYVNKRNTTWQAGHNFYNVDMSYLKRLCG
TFLGGPKPPQRVMFTEDLKLPASFDAREQWPQCPTIKEIRDQGSCGSCWAFGAVEAISDR
ICIHTNAHVSVEVSAEDLLTCCGSMCGDGCNGGYPAEAWNFWTRKGLVSGGLYESHVGCR
PYSIPPCEHHVNGSRPPCTGEGDTPKCSKICEPGYSPTYKQDKHYGYNSYSVSNSEKDIM
AEIYKNGPVEGAFSVYSDFLLYKSGVYQHVTGEMMGGHAIRILGWGVENGTPYWLVANSW
NTDWGDNGFFKILRGQDHCGIESEVVAGIPRTDQYWEKI
Number of residues339
Molecular Weight37821.35
Theoretical pI6.27
GO Classification
Functions
    proteoglycan binding
    collagen binding
    peptide binding
    peptidase activity
    cysteine-type endopeptidase activity
    cysteine-type peptidase activity
Processes
    extracellular matrix organization
    viral entry into host cell
    regulation of apoptotic process
    response to peptide hormone
    response to glucose
    cellular response to thyroid hormone stimulus
    proteolysis involved in cellular protein catabolic process
    response to wounding
    spermatogenesis
    regulation of catalytic activity
    decidualization
    autophagy
    response to interleukin-4
    proteolysis
    response to organic cyclic compound
    innate immune response
    skeletal muscle tissue development
    epithelial cell differentiation
    cellular response to mechanical stimulus
    negative regulation of cell death
    collagen catabolic process
    response to ethanol
    toll-like receptor signaling pathway
    extracellular matrix disassembly
    response to amine
Components
    lysosome
    endolysosome lumen
    extracellular exosome
    intracellular membrane-bounded organelle
    intracellular
    nucleolus
    mitochondrion
    perinuclear region of cytoplasm
    apical plasma membrane
    caveola
    extracellular region
    external side of plasma membrane
    sarcolemma
    melanosome
    extracellular space
General FunctionProteoglycan binding
Specific FunctionThiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.
Transmembrane Regions
GenBank Protein ID181192
UniProtKB IDP07858
UniProtKB Entry NameCATB_HUMAN
Cellular LocationLysosome
Gene sequence
>lcl|BSEQ0019039|Cathepsin B (CTSB)
ATGTGGCAGCTCTGGGCCTCCCTCTGCTGCCTGCTGGTGTTGGCCAATGCCCGGAGCAGG
CCCTCTTTCCATCCCCTGTCGGATGAGCTGGTCAACTATGTCAACAAACGGAATACCACG
TGGCAGGCCGGGCACAACTTCTACAACGTGGACATGAGCTACTTGAAGAGGCTATGTGGT
ACCTTCCTGGGTGGGCCCAAGCCACCCCAGAGAGTTATGTTTACCGAGGACCTGAAGCTG
CCTGCAAGCTTCGATGCACGGGAACAATGGCCACAGTGTCCCACCATCAAAGAGATCAGA
GACCAGGGCTCCTGTGGCTCCTGCTGGGCCTTCGGGGCTGTGGAAGCCATCTCTGACCGG
ATCTGCATCCACACCAATGCGCACGTCAGCGTGGAGGTGTCGGCGGAGGACCTGCTCACA
TGCTGTGGCAGCATGTGTGGGGACGGCTGTAATGGTGGCTATCCTGCTGAAGCTTGGAAC
TTCTGGACAAGAAAAGGCCTGGTTTCTGGTGGCCTCTATGAATCCCATGTAGGGTGCAGA
CCGTACTCCATCCCTCCCTGTGAGCACCACGTCAACGGCTCCCGGCCCCCATGCACGGGG
GAGGGAGATACCCCCAAGTGTAGCAAGATCTGTGAGCCTGGCTACAGCCCGACCTACAAA
CAGGACAAGCACTACGGATACAATTCCTACAGCGTCTCCAATAGCGAGAAGGACATCATG
GCCGAGATCTACAAAAACGGCCCCGTGGAGGGAGCTTTCTCTGTGTATTCGGACTTCCTG
CTCTACAAGTCAGGAGTGTACCAACACGTCACCGGAGAGATGATGGGTGGCCATGCCATC
CGCATCCTGGGCTGGGGAGTGGAGAATGGCACACCCTACTGGCTGGTTGCCAACTCCTGG
AACACTGACTGGGGTGACAATGGCTTCTTTAAAATACTCAGAGGACAGGATCACTGTGGA
ATCGAATCAGAAGTGGTGGCTGGAATTCCACGCACCGATCAGTACTGGGAAAAGATCTAA
GenBank Gene IDM14221
GeneCard IDNone
GenAtlas IDCTSB
HGNC IDHGNC:2527
Chromosome Location8
Locus8p22
References
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  2. Cao L, Taggart RT, Berquin IM, Moin K, Fong D, Sloane BF: Human gastric adenocarcinoma cathepsin B: isolation and sequencing of full-length cDNAs and polymorphisms of the gene. Gene. 1994 Feb 25;139(2):163-9.[8112600 ]
  3. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26.[16303743 ]
  4. Ritonja A, Popovic T, Turk V, Wiedenmann K, Machleidt W: Amino acid sequence of human liver cathepsin B. FEBS Lett. 1985 Feb 11;181(1):169-72.[3972105 ]
  5. Moin K, Day NA, Sameni M, Hasnain S, Hirama T, Sloane BF: Human tumour cathepsin B. Comparison with normal liver cathepsin B. Biochem J. 1992 Jul 15;285 ( Pt 2):427-34.[1637335 ]
  6. Fong D, Calhoun DH, Hsieh WT, Lee B, Wells RD: Isolation of a cDNA clone for the human lysosomal proteinase cathepsin B. Proc Natl Acad Sci U S A. 1986 May;83(9):2909-13.[3010323 ]
  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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  11. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22.[24275569 ]
  12. 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 ]
  13. Musil D, Zucic D, Turk D, Engh RA, Mayr I, Huber R, Popovic T, Turk V, Towatari T, Katunuma N, et al.: The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity. EMBO J. 1991 Sep;10(9):2321-30.[1868826 ]
  14. Turk D, Podobnik M, Kuhelj R, Dolinar M, Turk V: Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide. FEBS Lett. 1996 Apr 22;384(3):211-4.[8617355 ]
  15. Podobnik M, Kuhelj R, Turk V, Turk D: Crystal structure of the wild-type human procathepsin B at 2.5 A resolution reveals the native active site of a papain-like cysteine protease zymogen. J Mol Biol. 1997 Sep 5;271(5):774-88.[9299326 ]
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