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Sequence of CATL1_HUMAN

EC Number:3.4.22.15

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
cathepsin L
P07711
Homo sapiens
333
37564
Reaction
similar to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity towards protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity
Other sequences found for EC No. 3.4.22.15

General information:

Sequence
show sequence in fasta format
  0 MNPTLILAAF CLGIASATLT FDHSLEAQWT KWKAMHNRLY GMNEEGWRRA VWEKNMKMIE
 60 LHNQEYREGK HSFTMAMNAF GDMTSEEFRQ VMNGFQNRKP RKGKVFQEPL FYEAPRSVDW
120 REKGYVTPVK NQGQCGSCWA FSATGALEGQ MFRKTGRLIS LSEQNLVDCS GPQGNEGCNG
180 GLMDYAFQYV QDNGGLDSEE SYPYEATEES CKYNPKYSVA NDTGFVDIPK QEKALMKAVA
240 TVGPISVAID AGHESFLFYK EGIYFEPDCS SEDMDHGVLV VGYGFESTES DNNKYWLVKN
300 SWGEEWGMGG YVKMAKDRRN HCGIASAASY PTV
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
398382
Gal S.,Gottesman M.M.
Isolation and sequence of a cDNA for human pro-(cathepsin L).
Biochem. J.
253
303-306
1988
398383
Joseph L.J.,Chang L.C.,Stamenkovich D.,Sukhatme V.P.
Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts.
J. Clin. Invest.
81
1621-1629
1988
398385
Bechtel S.,Rosenfelder H.,Duda A.,Schmidt C.P.,Ernst U.,Wellenreuther R.,Mehrle A.,Schuster C.,Bahr A.,Bloecker H.,Heubner D.,Hoerlein A.,Michel G.,Wedler H.,Koehrer K.,Ottenwaelder B.,Poustka A.,Wiemann S.,Schupp I.
The full-ORF clone resource of the German cDNA consortium.
BMC Genomics
8
399-399
2007
398386
Humphray S.J.,Oliver K.,Hunt A.R.,Plumb R.W.,Loveland J.E.,Howe K.L.,Andrews T.D.,Searle S.,Hunt S.E.,Scott C.E.,Jones M.C.,Ainscough R.,Almeida J.P.,Ambrose K.D.,Ashwell R.I.S.,Babbage A.K.,Babbage S.,Bagguley C.L.,Bailey J.,Banerjee R.,Barker D.J.,Barlow K.F.,Bates K.,Beasley H.,Beasley O.,Bird C.P.,Bray-Allen S.,Brown A.J.,Brown J.Y.,Burford D.,Burrill W.,Burton J.,Carder C.,Carter N.P.,Chapman J.C.,Chen Y.,Clarke G.,Clark S.Y.,Clee C.M.,Clegg S.,Collier R.E.,Corby N.,Crosier M.,Cummings A.T.,Davies J.,Dhami P.,Dunn M.,Dutta I.,Dyer L.W.,Earthrowl M.E.,Faulkner L.,Fleming C.J.,Frankish A.,Frankland J.A.,French L.,Fricker D.G.,Garner P.,Garnett J.,Ghori J.,Gilbert J.G.R.,Glison C.,Grafham D.V.,Gribble S.,Griffiths C.,Griffiths-Jones S.,Grocock R.,Guy J.,Hall R.E.,Hammond S.,Harley J.L.,Harrison E.S.I.,Hart E.A.,Heath P.D.,Henderson C.D.,Hopkins B.L.,Howard P.J.,Howden P.J.,Huckle E.,Johnson C.,Johnson D.,Joy A.A.,Kay M.,Keenan S.,Kershaw J.K.,Kimberley A.M.,King A.,Knights A.,Laird G.K.,Langford C.,Lawlor S.,Leongamornlert D.A.,Leversha M.,Lloyd C.,Lloyd D.M.,Lovell J.,Martin S.,Mashreghi-Mohammadi M.,Matthews L.,McLaren S.,McLay K.E.,McMurray A.,Milne S.,Nickerson T.,Nisbett J.,Nordsiek G.,Pearce A.V.,Peck A.I.,Porter K.M.,Pandian R.,Pelan S.,Phillimore B.,Povey S.,Ramsey Y.,Rand V.,Scharfe M.,Sehra H.K.,Shownkeen R.,Sims S.K.,Skuce C.D.,Smith M.,Steward C.A.,Swarbreck D.,Sycamore N.,Tester J.,Thorpe A.,Tracey A.,Tromans A.,Thomas D.W.,Wall M.,Wallis J.M.,West A.P.,Whitehead S.L.,Willey D.L.,Williams S.A.,Wilming L.,Wray P.W.,Young L.,Ashurst J.L.,Coulson A.,Blocker H.,Durbin R.M.,Sulston J.E.,Hubbard T.,Jackson M.J.,Bentley D.R.,Beck S.,Rogers J.,Dunham I.
DNA sequence and analysis of human chromosome 9.
Nature
429
369-374
2004
398387
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
398388
Ritonja A.,Popovic T.,Kotnik M.,Machleidt W.,Turk V.
Amino acid sequences of the human kidney cathepsins H and L.
FEBS Lett.
228
341-345
1988
398389
Joseph L.J.,Lapid S.,Sukhatme V.P.
The major ras induced protein in NIH3T3 cells is cathepsin L.
Nucleic Acids Res.
15
3186-3186
1987
398390
Mason R.W.,Walker J.E.,Northrop F.D.
The N-terminal amino acid sequences of the heavy and light chains of human cathepsin L. Relationship to a cDNA clone for a major cysteine proteinase from a mouse macrophage cell line.
Biochem. J.
240
373-377
1986
398391
Menard R.,Carmona E.,Takebe S.,Dufour E.,Plouffe C.,Mason P.,Mort J.S.
Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro.
J. Biol. Chem.
273
4478-4484
1998
398392
Felbor U.,Dreier L.,Bryant R.A.,Ploegh H.L.,Olsen B.R.,Mothes W.
Secreted cathepsin L generates endostatin from collagen XVIII.
EMBO J.
19
1187-1194
2000
398393
Zhang H.,Li X.-J.,Martin D.B.,Aebersold R.
Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.
Nat. Biotechnol.
21
660-666
2003
398394
Goulet B.,Baruch A.,Moon N.S.,Poirier M.,Sansregret L.L.,Erickson A.,Bogyo M.,Nepveu A.
A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor.
Mol. Cell
14
207-219
2004
398395
Liu T.,Qian W.-J.,Gritsenko M.A.,Camp D.G. II,Monroe M.E.,Moore R.J.,Smith R.D.
Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.
J. Proteome Res.
4
2070-2080
2005
398396
Simmons G.,Gosalia D.N.,Rennekamp A.J.,Reeves J.D.,Diamond S.L.,Bates P.
Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry.
Proc. Natl. Acad. Sci. U.S.A.
102
11876-11881
2005
398397
Huang I.C.,Bosch B.J.,Li F.,Li W.,Lee K.H.,Ghiran S.,Vasilieva N.,Dermody T.S.,Harrison S.C.,Dormitzer P.R.,Farzan M.,Rottier P.J.,Choe H.
SARS coronavirus, but not human coronavirus NL63, utilizes cathepsin L to infect ACE2-expressing cells.
J. Biol. Chem.
281
3198-3203
2006
398398
Bosch B.J.,Bartelink W.,Rottier P.J.
Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide.
J. Virol.
82
8887-8890
2008
398399
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.
8
651-661
2009
398400
Burkard T.R.,Planyavsky M.,Kaupe I.,Breitwieser F.P.,Buerckstuemmer T.,Bennett K.L.,Superti-Furga G.,Colinge J.
Initial characterization of the human central proteome.
BMC Syst. Biol.
5
17-17
2011
398401
Rosenow A.,Noben J.P.,Jocken J.,Kallendrusch S.,Fischer-Posovszky P.,Mariman E.C.,Renes J.
Resveratrol-induced changes of the human adipocyte secretion profile.
J. Proteome Res.
11
4733-4743
2012
398402
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
96
253-262
2014
398403
Zhou N.,Pan T.,Zhang J.,Li Q.,Zhang X.,Bai C.,Huang F.,Peng T.,Zhang J.,Liu C.,Tao L.,Zhang H.
Glycopeptide Antibiotics Potently Inhibit Cathepsin L in the Late Endosome/Lysosome and Block the Entry of Ebola Virus, Middle East Respiratory Syndrome Coronavirus (MERS-CoV), and Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV).
J. Biol. Chem.
291
9218-9232
2016
398404
van den Bogaard E.H.J.,van Geel M.,van Vlijmen-Willems I.M.J.J.,Jansen P.A.M.,Peppelman M.,van Erp P.E.J.,Atalay S.,Venselaar H.,Simon M.E.H.,Joosten M.,Schalkwijk J.,Zeeuwen P.L.J.M.
Deficiency of the human cysteine protease inhibitor cystatin M/E causes hypotrichosis and dry skin.
Genet. Med.
21
1559-1567
2019
398405
Hoffmann M.,Kleine-Weber H.,Schroeder S.,Krueger N.,Herrler T.,Erichsen S.,Schiergens T.S.,Herrler G.,Wu N.H.,Nitsche A.,Mueller M.A.,Drosten C.,Poehlmann S.
SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor.
Cell
181
1-10
2020
398406
Smieszek S.P.,Przychodzen B.P.,Polymeropoulos M.H.
Amantadine disrupts lysosomal gene expression: A hypothesis for COVID19 treatment.
Int. J. Antimicrob. Agents
55
106004-106004
2020
398407
Ou X.,Liu Y.,Lei X.,Li P.,Mi D.,Ren L.,Guo L.,Guo R.,Chen T.,Hu J.,Xiang Z.,Mu Z.,Chen X.,Chen J.,Hu K.,Jin Q.,Wang J.,Qian Z.
Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV.
Nat. Commun.
11
1620-1620
2020
398408
Bruchez A.,Sha K.,Johnson J.,Chen L.,Stefani C.,McConnell H.,Gaucherand L.,Prins R.,Matreyek K.A.,Hume A.J.,Muehlberger E.,Schmidt E.V.,Olinger G.G.,Stuart L.M.,Lacy-Hulbert A.
MHC class II transactivator CIITA induces cell resistance to Ebola virus and SARS-like coronaviruses.
Science
370
241-247
2020
398409
Koch J.,Uckeley Z.M.,Doldan P.,Stanifer M.,Boulant S.,Lozach P.Y.
TMPRSS2 expression dictates the entry route used by SARS-CoV-2 to infect host cells.
EMBO J.
40
1-20
2021
398410
Coulombe R.,Grochulski P.,Sivaraman J.,Menard R.,Mort J.S.,Cygler M.
Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment.
EMBO J.
15
5492-5503
1996
398411
Fujishima A.,Imai Y.,Nomura T.,Fujisawa Y.,Yamamoto Y.,Sugarawa T.
The crystal structure of human cathepsin L complexed with E-64.
FEBS Lett.
407
47-50
1997