Cathepsin L1

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Cathepsin L
Protein CTSL1 PDB 1cjl.png
PDB rendering based on 1cjl.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CTSL ; CATL; CTSL1; MEP
External IDs OMIM116880 HomoloGene129366 ChEMBL: 3837 GeneCards: CTSL Gene
EC number 3.4.22.15
RNA expression pattern
PBB GE CTSL1 202087 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1514 n/a
Ensembl ENSG00000135047 n/a
UniProt P07711 n/a
RefSeq (mRNA) NM_001257971 n/a
RefSeq (protein) NP_001244900 n/a
Location (UCSC) Chr 9:
90.34 – 90.35 Mb
n/a
PubMed search [1] n/a

Cathepsin L1 is a protein that in humans is encoded by the CTSL1 gene.[1][2][3]

The protein encoded by this gene is a lysosomal cysteine proteinase that plays a major role in intracellular protein catabolism. Its substrates include collagen and elastin, as well as alpha-1 protease inhibitor, a major controlling element of neutrophil elastase activity. The encoded protein has been implicated in several pathologic processes, including myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria. This protein, which is a member of the peptidase C1 family, is a dimer composed of disulfide-linked heavy and light chains, both produced from a single protein precursor. At least two transcript variants encoding the same protein have been found for this gene.[3]

Interactions[edit]

CTSL1 has been shown to interact with Cystatin A.[4][5]

References[edit]

  1. ^ Chauhan SS, Popescu NC, Ray D, Fleischmann R, Gottesman MM, Troen BR (Feb 1993). "Cloning, genomic organization, and chromosomal localization of human cathepsin L". J Biol Chem 268 (2): 1039–45. PMID 8419312. 
  2. ^ Joseph LJ, Chang LC, Stamenkovich D, Sukhatme VP (Jun 1988). "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 (5): 1621–9. doi:10.1172/JCI113497. PMC 442598. PMID 2835398. 
  3. ^ a b "Entrez Gene: CTSL1 cathepsin L1". 
  4. ^ Majerle, Andreja; Jerala Roman (Sep 2003). "Protein inhibitors form complexes with procathepsin L and augment cleavage of the propeptide". Arch. Biochem. Biophys. (United States) 417 (1): 53–8. doi:10.1016/S0003-9861(03)00319-9. ISSN 0003-9861. PMID 12921779. 
  5. ^ Estrada, S; Nycander M; Hill N J; Craven C J; Waltho J P; Björk I (May 1998). "The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin L". Biochemistry (UNITED STATES) 37 (20): 7551–60. doi:10.1021/bi980026r. ISSN 0006-2960. PMID 9585570. 

Further reading[edit]

External links[edit]

  • The MEROPS online database for peptidases and their inhibitors: C01.032