P06797 (CATL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 134.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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: | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 334 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 | |
| Sequence similarities | Belongs to the peptidase C1 family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 17 | 17 | Ref.7 | ||||||||
| Propeptide | 18 – 113 | 96 | Activation peptide | PRO_0000026248 | |||||||
| Chain | 114 – 288 | 175 | Cathepsin L1 heavy chain | PRO_0000026249 | |||||||
| Propeptide | 289 – 290 | 2 | PRO_0000026250 | ||||||||
| Chain | 291 – 334 | 44 | Cathepsin L1 light chain | PRO_0000026251 | |||||||
Sites | |||||||||||
| Active site | 138 | 1 | By similarity | ||||||||
| Active site | 276 | 1 | By similarity | ||||||||
| Active site | 300 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 221 | 1 | N-linked (GlcNAc...) (high mannose) Ref.4 Ref.9 | ||||||||
| Disulfide bond | 135 ↔ 178 | By similarity | |||||||||
| Disulfide bond | 169 ↔ 211 | By similarity | |||||||||
| Disulfide bond | 269 ↔ 322 | Interchain (between heavy and light chains) By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 58 | 1 | M → I in AAA39984. Ref.2 | ||||||||
| Sequence conflict | 58 | 1 | M → I in AAD32136. Ref.2 | ||||||||
| Sequence conflict | 58 | 1 | M → I in AAD32137. Ref.2 | ||||||||
| Sequence conflict | 58 | 1 | M → I in AAD32138. Ref.2 | ||||||||
| Sequence conflict | 177 | 1 | G → R Ref.3 | ||||||||
Sequences
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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] [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, MASS SPECTROMETRY. 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. | ||||||||||||
| IPI | IPI00128154. | ||||||||||||
| PIR | KHMSL. S01177. | ||||||||||||
| RefSeq | NP_034114.1. NM_009984.3. | ||||||||||||
| UniGene | Mm.930. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P06797. | ||||||||||||
| SMR | P06797. Positions 21-333. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| MINT | MINT-1863740. | ||||||||||||
Protein family/group databases | |||||||||||||
| MEROPS | C01.032. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | P06797. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | P06797. | ||||||||||||
| PRIDE | P06797. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSMUST00000021933; ENSMUSP00000021933; ENSMUSG00000021477. | ||||||||||||
| GeneID | 13039. | ||||||||||||
| KEGG | mmu:13039. | ||||||||||||
| UCSC | uc007qyw.1. mouse. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 13039. | ||||||||||||
| MGI | MGI:88564. Ctsl. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG4870. | ||||||||||||
| HOGENOM | HOG000230774. | ||||||||||||
| HOVERGEN | HBG011513. | ||||||||||||
| InParanoid | P06797. | ||||||||||||
| KO | K01365. | ||||||||||||
| OMA | EEFRATH. | ||||||||||||
| OrthoDB | EOG48PMKF. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | MetaCyc:MONOMER-14812. | ||||||||||||
| BRENDA | 3.4.22.15. 3474. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P06797. | ||||||||||||
| Bgee | P06797. | ||||||||||||
| CleanEx | MM_CTSL. | ||||||||||||
| Genevestigator | P06797. | ||||||||||||
| GermOnline | ENSMUSG00000021477. Mus musculus. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR025661. Pept_asp_AS. IPR000169. Pept_cys_AS. IPR025660. Pept_his_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. IPR013201. Prot_inhib_I29. [Graphical view] | ||||||||||||
| PANTHER | PTHR12411. PTHR12411. 1 hit. | ||||||||||||
| Pfam | PF08246. Inhibitor_I29. 1 hit. PF00112. Peptidase_C1. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00705. PAPAIN. | ||||||||||||
| SMART | SM00848. Inhibitor_I29. 1 hit. SM00645. Pept_C1. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS00640. THIOL_PROTEASE_ASN. 1 hit. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| BindingDB | P06797. | ||||||||||||
| ChEMBL | CHEMBL5291. | ||||||||||||
| ChiTaRS | CTSL1. mouse. | ||||||||||||
| NextBio | 282928. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | CATL1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P06797 Secondary accession number(s): Q91UZ0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
