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P06797 (CATL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
p39 cysteine proteinase

Cleaved into the following 2 chains:

  1. Cathepsin L1 heavy chain
  2. Cathepsin L1 light chain
Gene names
Name:Ctsl
Synonyms:Ctsl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length334 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_processSertoli cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

autophagic cell death

Inferred from sequence or structural similarity. Source: BHF-UCL

catagen

Inferred from mutant phenotype PubMed 11023992. Source: MGI

cell communication

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to starvation

Inferred from sequence or structural similarity. Source: BHF-UCL

decidualization

Inferred from sequence or structural similarity. Source: BHF-UCL

hair follicle morphogenesis

Inferred from mutant phenotype PubMed 11023992. Source: MGI

male gonad development

Inferred from sequence or structural similarity. Source: BHF-UCL

multicellular organismal aging

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of keratinocyte proliferation

Inferred from mutant phenotype PubMed 11023992. Source: MGI

nerve development

Inferred from sequence or structural similarity. Source: BHF-UCL

protein autoprocessing

Inferred from direct assay PubMed 1482371. Source: MGI

protein processing

Inferred from direct assay PubMed 15099520. Source: MGI

proteolysis

Inferred from direct assay PubMed 18957203. Source: BHF-UCL

regulation of actin cytoskeleton reorganization

Inferred from genetic interaction PubMed 21911934. Source: MGI

response to glucocorticoid

Inferred from sequence or structural similarity. Source: BHF-UCL

response to glucose

Inferred from sequence or structural similarity. Source: BHF-UCL

response to gonadotropin

Inferred from sequence or structural similarity. Source: BHF-UCL

response to organic cyclic compound

Inferred from sequence or structural similarity. Source: BHF-UCL

spermatogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoplasmic vesicle

Inferred from direct assay PubMed 9310336. Source: MGI

external side of plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 9310336. Source: MGI

lysosome

Inferred from sequence or structural similarity. Source: BHF-UCL

microvillus

Inferred from sequence or structural similarity. Source: BHF-UCL

neuron projection

Inferred from sequence or structural similarity. Source: BHF-UCL

nucleolus

Inferred from direct assay PubMed 20338168. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 18957203. Source: BHF-UCL

perikaryon

Inferred from sequence or structural similarity. Source: BHF-UCL

vacuole

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionaminopeptidase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

cysteine-type carboxypeptidase activity

Inferred from direct assay PubMed 11023992. Source: MGI

cysteine-type endopeptidase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

histone binding

Inferred from direct assay PubMed 18957203. Source: BHF-UCL

peptide binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 14681235. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.7
Propeptide18 – 11396Activation peptide
PRO_0000026248
Chain114 – 288175Cathepsin L1 heavy chain
PRO_0000026249
Propeptide289 – 2902
PRO_0000026250
Chain291 – 33444Cathepsin L1 light chain
PRO_0000026251

Sites

Active site1381 By similarity
Active site2761 By similarity
Active site3001 By similarity

Amino acid modifications

Glycosylation2211N-linked (GlcNAc...) (high mannose) Ref.4 Ref.9
Disulfide bond135 ↔ 178 By similarity
Disulfide bond169 ↔ 211 By similarity
Disulfide bond269 ↔ 322Interchain (between heavy and light chains) By similarity

Experimental info

Sequence conflict581M → I in AAA39984. Ref.2
Sequence conflict581M → I in AAD32136. Ref.2
Sequence conflict581M → I in AAD32137. Ref.2
Sequence conflict581M → I in AAD32138. Ref.2
Sequence conflict1771G → R Ref.3

Sequences

Sequence LengthMass (Da)Tools
P06797 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: FE6747043307AD98

FASTA33437,547
        10         20         30         40         50         60 
MNLLLLLAVL CLGTALATPK FDQTFSAEWH QWKSTHRRLY GTNEEEWRRA IWEKNMRMIQ 

        70         80         90        100        110        120 
LHNGEYSNGQ HGFSMEMNAF GDMTNEEFRQ VVNGYRHQKH KKGRLFQEPL MLKIPKSVDW 

       130        140        150        160        170        180 
REKGCVTPVK NQGQCGSCWA FSASGCLEGQ MFLKTGKLIS LSEQNLVDCS HAQGNQGCNG 

       190        200        210        220        230        240 
GLMDFAFQYI KENGGLDSEE SYPYEAKDGS CKYRAEFAVA NDTGFVDIPQ QEKALMKAVA 

       250        260        270        280        290        300 
TVGPISVAMD ASHPSLQFYS SGIYYEPNCS SKNLDHGVLL VGYGYEGTDS NKNKYWLVKN 

       310        320        330 
SWGSEWGMEG YIKIAKDRDN HCGLATAASY PVVN 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin."
Troen B.R., Gal S., Gottesman M.M.
Biochem. J. 246:731-735(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[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 [GENOMIC DNA].
[3]"Cloning and characterization of a mouse cysteine proteinase."
Portnoy D.A., Erickson A.H., Kochan J., Ravetch J.V., Unkeless J.C.
J. Biol. Chem. 261:14697-14703(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Comparison of cathepsin L synthesized by normal and transformed cells at the gene, message, protein, and oligosaccharide levels."
Stearns N.A., Dong J., Pan J.X., Brenner D.A., Sahagian G.G.
Arch. Biochem. Biophys. 283:447-457(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, GLYCOSYLATION AT ASN-221.
Tissue: Liver.
[5]"Mutant cells selected during persistent reovirus infection do not express mature cathepsin L and do not support reovirus disassembly."
Baer G.S., Ebert D.H., Chung C.J., Erickson A.H., Dermody T.S.
J. Virol. 73:9532-9543(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H/An.
[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].
Strain: C57BL/6.
Tissue: Brain.
[7]"Identification on melanoma cells of p39, a cysteine proteinase that cleaves C3, the third component of complement: amino-acid-sequence identities with procathepsin L."
Jean D., Hermann J., Rodrigues-Lima F., Barel M., Balbo M., Frade R.
Biochem. J. 312:961-969(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-34; 273-292 AND 295-313.
[8]"Close relationship of the major excreted protein of transformed murine fibroblasts to thiol-dependent cathepsins."
Denhardt D.T., Hamilton R.T., Parfett C.L.J., Edwards D.R., Pierre R.S., Waterhouse P., Nilson-Hamilton M.
Cancer Res. 46:4590-4593(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 89-300.
Strain: BNL.
[9]"High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis."
Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K., Nishimura S.
Mol. Cell. Proteomics 4:1977-1989(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221.
Tissue: Epidermis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06086 mRNA. Translation: CAA29470.1.
J02583 mRNA. Translation: AAA37445.1.
M20495 Genomic DNA. Translation: AAA39984.1.
AF121837 mRNA. Translation: AAD32136.1.
AF121838 mRNA. Translation: AAD32137.1.
AF121839 mRNA. Translation: AAD32138.1.
BC068163 mRNA. Translation: AAH68163.1.
X04392 mRNA. Translation: CAA27980.1.
CCDSCCDS26600.1.
PIRKHMSL. S01177.
RefSeqNP_034114.1. NM_009984.3.
XP_006517143.1. XM_006517080.1.
XP_006517144.1. XM_006517081.1.
UniGeneMm.930.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MVVmodel-A22-334[»]
ProteinModelPortalP06797.
SMRP06797. Positions 21-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP06797. 1 interaction.
MINTMINT-1863740.

Chemistry

BindingDBP06797.
ChEMBLCHEMBL5291.

Protein family/group databases

MEROPSC01.032.

PTM databases

PhosphoSiteP06797.

Proteomic databases

MaxQBP06797.
PaxDbP06797.
PRIDEP06797.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021933; ENSMUSP00000021933; ENSMUSG00000021477.
GeneID13039.
KEGGmmu:13039.
UCSCuc007qyw.1. mouse.

Organism-specific databases

CTD1514.
MGIMGI:88564. Ctsl.

Phylogenomic databases

eggNOGCOG4870.
HOGENOMHOG000230774.
HOVERGENHBG011513.
InParanoidP06797.
KOK01365.
OMASMEMNAF.
OrthoDBEOG786H3P.
PhylomeDBP06797.
TreeFamTF313739.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14812.
BRENDA3.4.22.15. 3474.

Gene expression databases

ArrayExpressP06797.
BgeeP06797.
CleanExMM_CTSL.
GenevestigatorP06797.

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. mouse.
NextBio282928.
PROP06797.
SOURCESearch...

Entry information

Entry nameCATL1_MOUSE
AccessionPrimary (citable) accession number: P06797
Secondary accession number(s): Q91UZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1990
Last modified: July 9, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot