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Reviewed, UniProtKB/Swiss-Prot P06797 (CATL1_MOUSE)

Last modified June 16, 2009. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Cathepsin L1
    EC=3.4.22.15
Alternative name(s):
    Major excreted protein
      Short name=MEP
    p39 cysteine proteinase
Cleaved into the following 2 chains:
    1- Recommended name:
            Cathepsin L1 heavy chain
    2- Recommended name:
            Cathepsin L1 light chain
Gene names
Name: Ctsl1
Synonyms: Ctsl
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

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Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: MGI

Complete GO annotation...

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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

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Sequences

Sequence LengthMass (Da)Tools
P06797-1 [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

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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: 3689328] [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: 2835398] [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: 3533924] [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: 2275556] [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: 10516062] [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: 15489334] [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: 8554545] [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: 3755373] [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: 16170054] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221, MASS SPECTROMETRY.
Tissue: Epidermis.
+Additional computationally mapped references.

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Cross-references

Sequence databases

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.
IPIIPI00128154.
PIRKHMSL. S01177.
RefSeqNP_034114.1.
UniGeneMm.930

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1MVVmodel-A22-334[»]
SMRP06797. Positions 21-333.
ModBaseSearch...

Protein family/group databases

MEROPSC01.032.

Proteomic databases

PRIDEP06797.

Genome annotation databases

EnsemblENSMUSG00000021477. Mus musculus. [Contig view]
GeneID13039.
KEGGmmu:13039.

Organism-specific databases

MGIMGI:88564. Ctsl.

Phylogenomic databases

HOGENOMP06797.
HOVERGENP06797.
OMAP06797. APARITQ.

Enzyme and pathway databases

BRENDA3.4.22.15. 244.

Gene expression databases

ArrayExpressP06797.
BgeeP06797.
CleanExMM_CTSL.
GermOnlineENSMUSG00000021477. Mus musculus.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. Peptidase_C1A. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
ProDomPD000158. Peptidase_C1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00645. 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 Resources

NextBio282928.
SOURCESearch...

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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: June 16, 2009
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents