Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P07711 (CATL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cathepsin L1

EC=3.4.22.15
Alternative name(s):
Cathepsin L
Major excreted protein
Short name=MEP

Cleaved into the following 2 chains:

  1. Cathepsin L1 heavy chain
  2. Cathepsin L1 light chain
Gene names
Name:CTSL
Synonyms:CTSL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Important for the overall degradation of proteins in lysosomes.

Catalytic activity

Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.

Subunit structure

Dimer of a heavy and a light chain linked by disulfide bonds.

Subcellular location

Lysosome.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadaptive immune response

Inferred from expression pattern PubMed 15196205. Source: UniProtKB

antigen processing and presentation

Traceable author statement PubMed 15196205. Source: UniProtKB

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

cellular response to thyroid hormone stimulus

Inferred from expression pattern PubMed 21217776. Source: UniProtKB

collagen catabolic process

Inferred from direct assay PubMed 22952693. Source: BHF-UCL

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

macrophage apoptotic process

Non-traceable author statement PubMed 18495127. Source: BHF-UCL

proteolysis

Inferred from direct assay PubMed 8811434. Source: UniProtKB

proteolysis involved in cellular protein catabolic process

Inferred from direct assay PubMed 22952693. Source: BHF-UCL

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentendolysosome lumen

Traceable author statement. Source: Reactome

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 22952693. Source: BHF-UCL

lysosomal lumen

Traceable author statement. Source: Reactome

lysosome

Inferred from direct assay PubMed 15196205PubMed 1837142. Source: UniProtKB

nucleus

Traceable author statement PubMed 21326229. Source: BHF-UCL

   Molecular_functioncollagen binding

Inferred from direct assay PubMed 22952693. Source: BHF-UCL

cysteine-type endopeptidase activity

Inferred from direct assay PubMed 14511383. Source: UniProtKB

cysteine-type peptidase activity

Inferred from direct assay PubMed 8811434. Source: UniProtKB

fibronectin binding

Inferred from physical interaction PubMed 22952693. Source: BHF-UCL

histone binding

Inferred from direct assay PubMed 21326229. Source: BHF-UCL

proteoglycan binding

Inferred from physical interaction PubMed 22952693. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

srp-6G5EFH42EBI-1220160,EBI-1549936From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 11396Activation peptide
PRO_0000026244
Chain114 – 288175Cathepsin L1 heavy chain
PRO_0000026245
Propeptide289 – 2913
PRO_0000026246
Chain292 – 33342Cathepsin L1 light chain
PRO_0000026247

Sites

Active site1381
Active site2761
Active site3001

Amino acid modifications

Glycosylation2211N-linked (GlcNAc...) Ref.10 Ref.11 Ref.12
Disulfide bond135 ↔ 178
Disulfide bond169 ↔ 211
Disulfide bond269 ↔ 322Interchain (between heavy and light chains)

Experimental info

Sequence conflict561M → V in AAH12612. Ref.6
Sequence conflict2681D → N AA sequence Ref.7

Secondary structure

.............................................................. 333
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07711 [UniParc].

Last modified October 1, 1989. Version 2.
Checksum: 8CD17D00EF859D85

FASTA33337,564
        10         20         30         40         50         60 
MNPTLILAAF CLGIASATLT FDHSLEAQWT KWKAMHNRLY GMNEEGWRRA VWEKNMKMIE 

        70         80         90        100        110        120 
LHNQEYREGK HSFTMAMNAF GDMTSEEFRQ VMNGFQNRKP RKGKVFQEPL FYEAPRSVDW 

       130        140        150        160        170        180 
REKGYVTPVK NQGQCGSCWA FSATGALEGQ MFRKTGRLIS LSEQNLVDCS GPQGNEGCNG 

       190        200        210        220        230        240 
GLMDYAFQYV QDNGGLDSEE SYPYEATEES CKYNPKYSVA NDTGFVDIPK QEKALMKAVA 

       250        260        270        280        290        300 
TVGPISVAID AGHESFLFYK EGIYFEPDCS SEDMDHGVLV VGYGFESTES DNNKYWLVKN 

       310        320        330 
SWGEEWGMGG YVKMAKDRRN HCGIASAASY PTV 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and sequence of a cDNA for human pro-(cathepsin L)."
Gal S., Gottesman M.M.
Biochem. J. 253:303-306(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts."
Joseph L.J., Chang L.C., Stamenkovich D., Sukhatme V.P.
J. Clin. Invest. 81:1621-1629(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The full-ORF clone resource of the German cDNA consortium."
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.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon endothelium.
[5]"DNA sequence and analysis of human chromosome 9."
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. expand/collapse author list , 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.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[7]"Amino acid sequences of the human kidney cathepsins H and L."
Ritonja A., Popovic T., Kotnik M., Machleidt W., Turk V.
FEBS Lett. 228:341-345(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 114-288 AND 292-333.
[8]"The major ras induced protein in NIH3T3 cells is cathepsin L."
Joseph L.J., Lapid S., Sukhatme V.P.
Nucleic Acids Res. 15:3186-3186(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 113-154.
[9]"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."
Mason R.W., Walker J.E., Northrop F.D.
Biochem. J. 240:373-377(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 114-154 AND 292-333.
[10]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-221.
[11]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221.
Tissue: Plasma.
[12]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221.
Tissue: Liver.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment."
Coulombe R., Grochulski P., Sivaraman J., Menard R., Mort J.S., Cygler M.
EMBO J. 15:5492-5503(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-333.
[15]"The crystal structure of human cathepsin L complexed with E-64."
Fujishima A., Imai Y., Nomura T., Fujisawa Y., Yamamoto Y., Sugarawa T.
FEBS Lett. 407:47-50(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 114-333.
[16]Cygler M., Coulombe R.
Submitted (AUG-1999) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 18-333.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12451 mRNA. Translation: CAA30981.1.
M20496 mRNA. Translation: AAA66974.1.
CR457053 mRNA. Translation: CAG33334.1.
BX537395 mRNA. Translation: CAD97637.1.
AL160279 Genomic DNA. Translation: CAI16308.1.
BC012612 mRNA. Translation: AAH12612.1.
X05256 mRNA. Translation: CAA28877.1.
PIRKHHUL. S01002.
RefSeqNP_001244900.1. NM_001257971.1.
NP_001244901.1. NM_001257972.1.
NP_001903.1. NM_001912.4.
NP_666023.1. NM_145918.2.
XP_005251773.1. XM_005251716.1.
UniGeneHs.731507.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CJLX-ray2.20A22-333[»]
1CS8X-ray1.80A19-333[»]
1ICFX-ray2.00A/C114-288[»]
B/D292-333[»]
1MHWX-ray1.90A/B114-288[»]
C/D292-333[»]
2NQDX-ray1.75B113-333[»]
2VHSX-ray1.50A/B/C/D114-333[»]
2XU1X-ray1.45A/B/C/D114-333[»]
2XU3X-ray0.90A114-333[»]
2XU4X-ray1.12A114-333[»]
2XU5X-ray1.60A114-333[»]
2YJ2X-ray1.15A114-333[»]
2YJ8X-ray1.30A114-333[»]
2YJ9X-ray1.35A114-333[»]
2YJBX-ray1.40A114-333[»]
2YJCX-ray1.14A114-333[»]
3BC3X-ray2.20A/B114-333[»]
3H89X-ray2.50A/B/C/D/E/F114-333[»]
3H8BX-ray1.80A/B/C/D/E/F114-333[»]
3H8CX-ray2.50A/B114-333[»]
3HHAX-ray1.27A/B/C/D114-333[»]
3HWNX-ray2.33A/B/C/D76-333[»]
3IV2X-ray2.20A/B114-333[»]
3K24X-ray2.50A/B114-333[»]
3KSEX-ray1.71A/B/C114-333[»]
3OF8X-ray2.20A113-333[»]
3OF9X-ray1.76A113-333[»]
4AXLX-ray1.92A114-333[»]
4AXMX-ray2.80A/B/F/I/L/O114-333[»]
ProteinModelPortalP07711.
SMRP07711. Positions 18-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107894. 12 interactions.
IntActP07711. 13 interactions.
MINTMINT-3005764.
STRING9606.ENSP00000345344.

Chemistry

BindingDBP07711.
ChEMBLCHEMBL2111380.
DrugBankDB00040. Glucagon recombinant.
GuidetoPHARMACOLOGY2351.

Protein family/group databases

MEROPSC01.032.

PTM databases

PhosphoSiteP07711.

Polymorphism databases

DMDM115741.

Proteomic databases

PaxDbP07711.
PeptideAtlasP07711.
PRIDEP07711.

Protocols and materials databases

DNASU1514.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340342; ENSP00000365061; ENSG00000135047.
ENST00000343150; ENSP00000345344; ENSG00000135047.
GeneID1514.
KEGGhsa:1514.
UCSCuc004aph.3. human.

Organism-specific databases

CTD1514.
GeneCardsGC09P090352.
H-InvDBHIX0058839.
HIX0170314.
HGNCHGNC:2537. CTSL.
HPACAB000459.
MIM116880. gene.
neXtProtNX_P07711.
PharmGKBPA162382890.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4870.
HOGENOMHOG000230774.
HOVERGENHBG011513.
InParanoidP07711.
KOK01365.
OMANPEYSVA.
OrthoDBEOG786H3P.
PhylomeDBP07711.
TreeFamTF313739.

Enzyme and pathway databases

BRENDA3.4.22.15. 2681.
ReactomeREACT_118779. Extracellular matrix organization.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP07711.
BgeeP07711.
CleanExHS_CTSL1.
GenevestigatorP07711.

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTSL1. human.
EvolutionaryTraceP07711.
GeneWikiCathepsin_L1.
GenomeRNAi1514.
NextBio6271.
PMAP-CutDBP07711.
PROP07711.
SOURCESearch...

Entry information

Entry nameCATL1_HUMAN
AccessionPrimary (citable) accession number: P07711
Secondary accession number(s): Q6IAV1, Q96QJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: October 1, 1989
Last modified: April 16, 2014
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM